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Information on EC 1.11.1.13 - manganese peroxidase
for references in articles please use BRENDA:EC1.11.1.13
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EC Tree 1 Oxidoreductases
1.11 Acting on a peroxide as acceptor
1.11.1 Peroxidases
1.11.1.13 manganese peroxidase
IUBMB Comments
A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ . The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates . It is inactive with veratryl alcohol or nonphenolic substrates.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.11.1.13
- lignin
- laccase
-
ligninolytic
- phanerochaete
- chrysosporium
-
white-rot
-
basidiomycete
-
decolor
- peroxidases
- pleurotus
-
lignin-degrading
- trametes
- versicolor
-
veratryl
- ostreatus
- straw
-
mniii
-
lignocellulosic
- bjerkandera
- sordida
-
lignocellulolytic
-
remazol
- subvermispora
- lacteus
- eryngii
- irpex
-
lignin-modifying
-
kraft
- sawdust
- phlebia
- adusta
-
ceriporiopsis
- 1-hydroxybenzotriazole
- nutrition
-
lignocellulose-degrading
-
ligninase
- sajor-caju
-
wood-rotting
-
dye-decolorizing
- tigrinus
- mnso4
-
biosorption
-
delignification
-
delignified
-
biobleaching
- degradation
- synthesis
- lentinula
-
biotreatment
-
non-phenolic
- industry
-
decolourisation
- 2,6-dimethoxyphenol
- paper production
-
low-nitrogen
- environmental protection
- biotechnology
- biofuel production
showSynonyms
manganese peroxidase, manganese-dependent peroxidase, lemnp2, il-mnp1, short mnp, mnp-gy, hybrid mn-peroxidase, peroxidase-m2, mnp-pgy, mrmnp1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CmMnP
extralong PMnP
hybrid Mn-peroxidase
Il-MnP1
Il-MnP6
LeMnP2
long PMnP
manganese peroxidase
manganese-dependent peroxidase
Mn-dependent (NADH-oxidizing) peroxidase
-
-
-
-
Mn2+: hydrogen peroxide oxidoreductase
Mn2+:H2O2 oxidoreductase
Mn2+:hydrogen peroxide oxidoreductase
MnP
MnP II
MnP-BBP6
MnP-GY
-
isoenzyme synthesized in glucose-yeast extract medium has VTCATGQTTANE at the N-terminus
MnP-PGY
-
isoenzyme synthesized in peptone-glucose-yeast extract medium has ATCADGRTTANA at the N-terminus
mnp1
MnP10
MnP117436
MnP12
MnP157986
MnP2
MnP3
MnP50297
MnP6
Moror_3885
MP
-
-
-
-
MrMnP1
peroxidase, manganese
-
-
-
-
peroxidase-M2
-
-
-
-
rMnP3-BBP6
short manganese peroxidase
short MnP
manganese peroxidase
Lyophyllum subglobisporium ECN 100606
-
-
-
MnP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
ping-pong mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
mechanism
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
shows properties of a peroxidase and an oxidase
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
the proton-coupled electron transfer (PCET) process dominates the catalytic circle of MnP and the transformation of Mn3+, density functional theory (DFT) calculations, overview. During the reaction of H2O2 in the active MnP system, a typical signal of DMPO-Mn3+ is observed, indicating that MnP catalyzes Mn2+ to Mn3+
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
shows properties of a peroxidase and an oxidase
Phanerodontia chrysosporium BKM-F-1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
shows properties of a peroxidase and an oxidase
Phanerodontia chrysosporium BKM-F 1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
ping-pong mechanism
Phanerodontia chrysosporium OGC101
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
ping-pong mechanism
Phanerodontia chrysosporium VKM F-1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
the proton-coupled electron transfer (PCET) process dominates the catalytic circle of MnP and the transformation of Mn3+, density functional theory (DFT) calculations, overview. During the reaction of H2O2 in the active MnP system, a typical signal of DMPO-Mn3+ is observed, indicating that MnP catalyzes Mn2+ to Mn3+
Phanerodontia chrysosporium BKMF-1767
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
the proton-coupled electron transfer (PCET) process dominates the catalytic circle of MnP and the transformation of Mn3+, density functional theory (DFT) calculations, overview. During the reaction of H2O2 in the active MnP system, a typical signal of DMPO-Mn3+ is observed, indicating that MnP catalyzes Mn2+ to Mn3+
Phanerodontia chrysosporium CCTCC AF96007
-
-
2 Mn(II) + 2 H+ + H2O2 = 2 Mn(III) + 2 H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
manganese oxidation I
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SYSTEMATIC NAME
IUBMB Comments
Mn(II):hydrogen-peroxide oxidoreductase
A hemoprotein. The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. The enzyme oxidizes a bound Mn2+ ion to Mn3+ in the presence of hydrogen peroxide. The product, Mn3+, is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn2+ and insoluble Mn4+ [4]. The complexed Mn3+ ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates [1]. It is inactive with veratryl alcohol or nonphenolic substrates.
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CAS REGISTRY NUMBER
COMMENTARY
114995-15-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonate + H2O2
?
-
Substrates: reaction with and without Mn2+
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + Mn2+
?
-
Substrates: -
Products: -
Products: -
?
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate + H+ + H2O2
?
-
Substrates: -
Products: -
Products: -
r
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate + Mn2+ + H2O2
?
-
Substrates: -
Products: -
Products: -
r
2,4,6-trichlorophenol + H2O2
?
-
Substrates: no oxidation in absence of Mn2+
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
coerulignone + 2 H2O
Substrates: MnP activity is determined spectrophotometrically by measuring the oxidation of 2,6-dimethoxyphenol to coerulignone (epsilon = 49.6 mM/cm) in 50 mM malonate buffer (pH 4.5) containing 1.0 mM MnSO4, 1.0 mM 2,6-dimethoxyphenol, and 0.2 mM H2O2 at 469 nm, 37°C
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2 + H+
coerulignone + H2O
-
Substrates: -
Products: -
Products: -
r
2-bromonaphthalene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
4-aminophenol + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
4-methoxyphenol + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
acenaphthene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
acenaphthylene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
alizarin red S + H2O2
? + 2 H2O
Substrates: substrate of A172W variants mutant enzymes, poor activity with the wild-type enzyme
Products: -
Products: -
?
alpha-naphthol + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
anthracene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
benzo[a]anthracene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
benzo[a]pyrene + ?
?
-
Substrates: key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
Products: -
Products: -
?
benzo[a]pyrene + ?
benzo[a]pyrene-1,6-quinone + ?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
benzo[b]fluoroanthrene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
benzo[g,h,i]perylene + H2O
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
brilliant blue R + H2O2
?
Substrates: dye decolorization
Products: -
Products: -
?
catechol + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
chrysene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
Co2+ + H+ + H2O2
Co3+ + H2O
-
Substrates: reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
Products: -
Products: -
?
crystal violet + H2O2
?
Substrates: dye decolorization
Products: -
Products: -
?
crystal violet + H2O2
? + 2 H2O
Substrates: substrate of wild-type and A172W variants mutant enzymes
Products: -
Products: -
?
dibenzo[a,h]anthracene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
fluoranthene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
fluorene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
guaiacol + H2O2
tetraguaiacol + H2O
-
Substrates: -
Products: -
Products: -
?
guaiacylglycerol-beta-guaiacyl ether + H2O2
? + 2 H2O
Substrates: substrate of A172W variants mutant enzymes
Products: -
Products: -
?
indeno[1,2,3-c,d]pyrene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
indigo carmine + H2O2
? + 2 H2O
Substrates: substrate of wild-type and A172W variants mutant enzymes
Products: -
Products: -
?
methyl orange + H2O2
? + 2 H2O
Substrates: substrate of wild-type and A172W variants mutant enzymes
Products: -
Products: -
?
Mn(III)-tartrate + H2O
Mn(II)-tartrate + H+ + H2O
-
Substrates: -
Products: -
Products: -
r
Mn2+ + di(2-methylpent-2-enyl) sulfide + H+
Mn3+ + 2,4-dimethylthiophene + 2-methyl-2-pentenal + H2O
-
Substrates: -
Products: -
Products: -
?
naphthalene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
pyrene + ?
?
-
Substrates: oxidation in presence of Tween 80
Products: -
Products: -
?
Reactive Black 5 + 2 H+ + H2O2
Reactive Black 5 + 2 H2O
Substrates: dye decolorization
Products: -
Products: -
?
remazol brilliant blue R + H2O2
? + 2 H2O
Substrates: substrate of wild-type and A172W variants mutant enzymes
Products: -
Products: -
?
veratryl alcohol + H2O2 + Mn2+
?
-
Substrates: veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
Products: -
Products: -
?
veratrylglycerol-beta-guaiacyl ether + H2O2
? + 2 H2O
Substrates: substrate of A172W variants mutant enzymes
Products: -
Products: -
?
2 2,6-dimethoxyphenol + H2O2
coerulignone + 2 H2O
-
Substrates: -
Products: -
Products: -
r
2 2,6-dimethoxyphenol + H2O2
coerulignone + 2 H2O
-
Substrates: -
Products: -
Products: -
r
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Bacillus velezensis Al-Dhabi 140
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: the kcat value for the reaction is dependent of the Mn(III) chelator molecules malonate, lactate and oxalate, indicating that the enzyme oxidizes chelated Mn(II) to Mn(III)
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Phanerodontia chrysosporium BKMF-1767
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Phanerodontia chrysosporium CCTCC AF96007
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Pseudolagarobasidium sp. PP17-33
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
Substrates: maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
Products: -
Products: -
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
Substrates: maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
Products: -
Products: -
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
Substrates: no substrate of wild-type
Products: -
Products: -
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
Substrates: no substrate of wild-type
Products: -
Products: -
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Cerrena unicolor BBP6
Substrates: -
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: ABTS
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: ABTS
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Irpex lacteus F17
Substrates: ABTS
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: substrate of A172W variants mutant enzymes
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + 2 H+
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
Substrates: substrate of A172W variants mutant enzymes
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
Substrates: in absence or presence of Mn2+
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
Substrates: in absence or presence of Mn2+
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
Substrates: no substrate of wild-type
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
Substrates: no substrate of wild-type
Products: -
Products: -
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
r
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
r
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
Substrates: -
Products: -
Products: -
r
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
Substrates: -
Products: -
Products: -
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Bacillus velezensis Al-Dhabi 140
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Cerrena unicolor BBP6
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Irpex lacteus CCTCC AF2014020
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: substrate of A172W variants mutant enzymes, very low activity with the wild-type enzyme
Products: -
Products: -
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Substrates: substrate of A172W variants mutant enzymes, very low activity with the wild-type enzyme
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2
?
-
Substrates: reaction in absence or in presence of Mn2+
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2
?
-
Substrates: the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2
?
Lyophyllum subglobisporium ECN 100606
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
2,6-dimethoxyphenol + H2O2
?
-
Substrates: -
Products: -
Products: -
?
2,6-dimethoxyphenol + Mn2+ + H2O2
coerulignone + Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
r
2,6-dimethoxyphenol + Mn2+ + H2O2
coerulignone + Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
r
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
Substrates: 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
Products: -
Products: -
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
Products: -
Products: -
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
Substrates: -
Products: -
Products: -
?
bromophenol blue + H2O2
?
Substrates: dye decolorization
Products: -
Products: -
?
ferrocyanide + H+ + H2O2
ferricyanide + H2O
-
Substrates: -
Products: -
Products: -
r
ferrocyanide + H+ + H2O2
ferricyanide + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: -
Products: -
Products: -
r
fluorene + H2O2
9H-fluorene-3,4-diol
Substrates: denim bleaching PAH degradation, product analysis by HPLC
Products: -
Products: -
?
fluorene + H2O2
9H-fluorene-3,4-diol
Cerrena unicolor BBP6
Substrates: denim bleaching PAH degradation, product analysis by HPLC
Products: -
Products: -
?
guaiacol + H2O2
?
-
Substrates: no oxidation in absence of Mn2+
Products: -
Products: -
?
guaiacol + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
guaiacol + H2O2 + 2 H+
4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione + ?
Substrates: Il-MnP1 oxidizes guaiacol and provides a first radical A, which undergoes a variety of non-enzymatic reactions that mainly consists of reactions of resonance stabilization to generate the next radical B. In turn the C-C radical coupling of two B radicals generates a dimeric 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol, which can be further oxidized by Il-MnP1 to produce 3,3'-dimethoxy[1,1'-bi(cyclohexa-2,5-diene)]-4,4'-dione and 1-[[1(1')Z]-3'-methoxy-4,4'-dioxo[1,1'-bi(cyclohexa-2,5-dien-1-yliden)]-3-yl]-1-methyldioxidan-1-ium. Furthermore, Il-MnP1 oxidizes 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol to produce a radical C,which is also subject to a variety of non-enzymatic reactions to produce a radical D. Finally, radical D is subjected to further oxidation and C-C coupling for the production of 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione, 1(3),2(5),3(3)-trimethoxy-2(3),2(4)-dihydro[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4),3(4)-triol, and [1(1)(2(1))E]-3(4)-hydroxy-1(3),2(5),3(3)-trimethoxy-1(4)H,2(4)H-[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4)-dione
Products: -
Products: -
?
guaiacol + H2O2 + 2 H+
4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione + ?
Irpex lacteus CCTCC AF2014020
Substrates: Il-MnP1 oxidizes guaiacol and provides a first radical A, which undergoes a variety of non-enzymatic reactions that mainly consists of reactions of resonance stabilization to generate the next radical B. In turn the C-C radical coupling of two B radicals generates a dimeric 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol, which can be further oxidized by Il-MnP1 to produce 3,3'-dimethoxy[1,1'-bi(cyclohexa-2,5-diene)]-4,4'-dione and 1-[[1(1')Z]-3'-methoxy-4,4'-dioxo[1,1'-bi(cyclohexa-2,5-dien-1-yliden)]-3-yl]-1-methyldioxidan-1-ium. Furthermore, Il-MnP1 oxidizes 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol to produce a radical C,which is also subject to a variety of non-enzymatic reactions to produce a radical D. Finally, radical D is subjected to further oxidation and C-C coupling for the production of 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione, 1(3),2(5),3(3)-trimethoxy-2(3),2(4)-dihydro[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4),3(4)-triol, and [1(1)(2(1))E]-3(4)-hydroxy-1(3),2(5),3(3)-trimethoxy-1(4)H,2(4)H-[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4)-dione
Products: -
Products: -
?
guaiacol + H2O2 + 2 H+
4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione + ?
Irpex lacteus F17
Substrates: Il-MnP1 oxidizes guaiacol and provides a first radical A, which undergoes a variety of non-enzymatic reactions that mainly consists of reactions of resonance stabilization to generate the next radical B. In turn the C-C radical coupling of two B radicals generates a dimeric 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol, which can be further oxidized by Il-MnP1 to produce 3,3'-dimethoxy[1,1'-bi(cyclohexa-2,5-diene)]-4,4'-dione and 1-[[1(1')Z]-3'-methoxy-4,4'-dioxo[1,1'-bi(cyclohexa-2,5-dien-1-yliden)]-3-yl]-1-methyldioxidan-1-ium. Furthermore, Il-MnP1 oxidizes 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol to produce a radical C,which is also subject to a variety of non-enzymatic reactions to produce a radical D. Finally, radical D is subjected to further oxidation and C-C coupling for the production of 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione, 1(3),2(5),3(3)-trimethoxy-2(3),2(4)-dihydro[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4),3(4)-triol, and [1(1)(2(1))E]-3(4)-hydroxy-1(3),2(5),3(3)-trimethoxy-1(4)H,2(4)H-[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4)-dione
Products: -
Products: -
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
Substrates: oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Products: -
Products: -
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
Substrates: oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Products: -
Products: -
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
Substrates: oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Products: -
Products: -
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
Substrates: oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Products: -
Products: -
?
H2O2 + guaiacol
H2O + ?
-
Substrates: oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Products: -
Products: -
?
H2O2 + guaiacol
H2O + ?
-
Substrates: oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
Products: -
Products: -
?
H2O2 + Poly R-478
?
-
Substrates: MnP2 depolymerizes the polymeric azo dye,Poly R-478, regardless of the presence of Mn2+, to complete its catalytic cycle
Products: -
Products: -
?
H2O2 + Poly R-478
?
-
Substrates: Mn2+ is required for reaction with Poly R-478 with MnP3
Products: -
Products: -
?
hydroquinone + H2O2
?
-
Substrates: reaction in absence or in presence of Mn2+
Products: -
Products: -
?
hydroquinone + H2O2
?
-
Substrates: reaction in absence or in presence of Mn2+
Products: -
Products: -
?
methyl orange + H2O2
?
Substrates: dye decolorization
Products: -
Products: -
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
Substrates: -
Products: -
Products: -
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
-
Substrates: activity assay
Products: -
Products: -
?
Mn2+ + guaiacol + H2O2
?
Substrates: activity assay
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
Substrates: -
Products: product Mn3+ possibly migrates into polymer molecules, such as lignin, nylon and melanin, and initiates nonspecific oxidation
Products: product Mn3+ possibly migrates into polymer molecules, such as lignin, nylon and melanin, and initiates nonspecific oxidation
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: single Mn2+ binding site in the vicinity of the heme
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
Products: dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
Products: Mn3+ oxidizes o-phenylenediamine and p-anisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: chelating organic acids facilitate the dissociation of Mn3+ from enzyme
Products: chelating organic acids facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes curcumin
Products: Mn3+ oxidizes curcumin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
Products: in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes methoxy benzenes: 1,2,4-tri-, 1,2,3,5-tetra-, 1,2,4,5-tetra-, pentamethoxybenzene, veratryl alcohol is oxidized by thiyl radicals derived from Mn3+ oxidation of glutathione, not directly by Mn3+
Products: Mn3+ oxidizes methoxy benzenes: 1,2,4-tri-, 1,2,3,5-tetra-, 1,2,4,5-tetra-, pentamethoxybenzene, veratryl alcohol is oxidized by thiyl radicals derived from Mn3+ oxidation of glutathione, not directly by Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: oxidation and cleavage of a phenolic lignin model dimer and its products, MnP catalyzes C-alpha-C-beta cleavages, C-alpha-oxidation and alkyl-aryl cleavages of phenolic syringyl type beta-1 lignin structures via Mn3+
Products: oxidation and cleavage of a phenolic lignin model dimer and its products, MnP catalyzes C-alpha-C-beta cleavages, C-alpha-oxidation and alkyl-aryl cleavages of phenolic syringyl type beta-1 lignin structures via Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes vanillyl alcohol
Products: Mn3+ oxidizes vanillyl alcohol
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction
Products: Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes thiols
Products: Mn3+ oxidizes thiols
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: the diffusible product is Mn3+
Products: the diffusible product is Mn3+
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: each catalytic cycle step is irreversible
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds
Products: product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411
Products: Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: the diffusible product is Mn3+
Products: the diffusible product is Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: specifically oxidizes Mn2+
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: in presence of H2O2 enzyme oxidizes Mn2+ significantly faster than all other substrates, main function of enzyme is oxidation of Mn2+ to Mn3+
Products: Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411
Products: Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: in presence of H2O2 enzyme oxidizes Mn2+ significantly faster than all other substrates, main function of enzyme is oxidation of Mn2+ to Mn3+
Products: the diffusible product is Mn3+
Products: the diffusible product is Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: in presence of H2O2 enzyme oxidizes Mn2+ significantly faster than all other substrates, main function of enzyme is oxidation of Mn2+ to Mn3+
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ complex oxidizes a variety of organic substrates
Products: Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillyl alcohol
Products: Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: the diffusible product is Mn3+
Products: the diffusible product is Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ oxidizes syringic acid, 4-hydroxy-3-methoxycinnamic acid, isoeugenol, ascorbate
Products: Mn3+ oxidizes syringic acid, 4-hydroxy-3-methoxycinnamic acid, isoeugenol, ascorbate
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ oxidizes vanillyl alcohol
Products: Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ oxidizes p-cresol
Products: Mn3+ oxidizes p-cresol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+ oxidizes vanillyl alcohol
Products: Mn3+ oxidizes vanillyl alcohol
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction
Products: Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+ oxidizes thiols
Products: Mn3+ oxidizes thiols
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: the diffusible product is Mn3+
Products: the diffusible product is Mn3+
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: free divalent Mn is the substrate, not Mn2+-complexes
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: Mn3+ oxidizes p-cresol
Products: Mn3+ oxidizes p-cresol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+ complex oxidizes a variety of organic substrates
Products: Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes phenol red
Products: Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ complex oxidizes a variety of organic substrates
Products: Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: the diffusible product is Mn3+
Products: the diffusible product is Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: MnP isoenzymes serve different functions in lignin biodegradation, each may have a preferred substrate
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: initial depolymerization of the lignin polymer
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is a component of woody plant tissues
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
Products: Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: Mn3+ is produced under lignolytic conditions
Products: Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: acts together with lignin peroxidase in lignin-degradation of white rot fungi
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: acts together with lignin peroxidase in lignin-degradation of white rot fungi
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: acts together with lignin peroxidase in lignin-degradation of white rot fungi
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ complex oxidizes a variety of organic substrates
Products: Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes phenol red
Products: Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: little or no enzyme activity in absence of Mn2+
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes curcumin
Products: Mn3+ oxidizes curcumin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes o-dianisidine
Products: Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes amines
Products: Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: -
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ complex oxidizes a variety of organic substrates
Products: Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
Products: Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: each catalytic cycle step is irreversible
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
Products: alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes vanillyl alcohol
Products: Mn3+ oxidizes vanillyl alcohol
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: each catalytic cycle step is irreversible
Products: Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction
Products: Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillyl alcohol
Products: Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
Products: chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: -
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: -
Products: in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
Products: in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: -
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
Products: Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: important component of lignin degradation system
Products: Mn3+ is produced under lignolytic conditions
Products: Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: specifically oxidizes Mn2+
Products: product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds
Products: product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: specifically oxidizes Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+ complex oxidizes a variety of organic substrates
Products: Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+ oxidizes phenolic lignin model compounds
Products: Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
Products: Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes phenol red
Products: Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
Products: Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phlebia radiata 79 / ATCC 64658
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes vanillylacetone
Products: Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phlebia radiata 79 / ATCC 64658
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes phenol red
Products: Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phlebia radiata 79 / ATCC 64658
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phlebia radiata 79 / ATCC 64658
-
Substrates: completion of MnP catalytic cycle requires Mn2+
Products: Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
Products: Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes vanillylideneacetone
Products: Mn3+ oxidizes vanillylideneacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes phenol red
Products: Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes a variety of phenols
Products: Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: preferential degradation of lignin in wheat straw
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes syringaldazine
Products: Mn3+ oxidizes syringaldazine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes guaiacol
Products: Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ as the best substrate
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: preferential degradation of lignin in wheat straw
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: oxidizes Mn2+ as the best substrate
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
Products: Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: Mn3+ oxidizes lignin
Products: Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H2O2 + oxytetracycline
Mn3+ + ?
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H2O2 + oxytetracycline
Mn3+ + ?
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H2O2 + tetracycline
Mn3+ + ?
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H2O2 + tetracycline
Mn3+ + ?
Phanerodontia chrysosporium BKM-F-1767
-
Substrates: -
Products: -
Products: -
?
o-dianisidine + H2O2
?
-
Substrates: in absence or in presence of of Mn2+
Products: -
Products: -
?
o-dianisidine + H2O2
?
-
Substrates: in absence or in presence of of Mn2+
Products: -
Products: -
?
p-phenylenediamine + H2O2
?
-
Substrates: in absence or in presence of Mn2+
Products: -
Products: -
?
p-phenylenediamine + H2O2
?
-
Substrates: in absence or in presence of Mn2+
Products: -
Products: -
?
phenanthrene + 2 H+ + 2 H2O2
phenanthrene-9,10-dione + 2 H2O
Substrates: denim bleaching PAH degradation, product analysis by HPLC
Products: -
Products: -
?
phenanthrene + 2 H+ + 2 H2O2
phenanthrene-9,10-dione + 2 H2O
Cerrena unicolor BBP6
Substrates: denim bleaching PAH degradation, product analysis by HPLC
Products: -
Products: -
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Substrates: dye decolorization, substrate of A172W variants mutant enzymes
Products: -
Products: -
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Substrates: dye decolorization, substrate of A172W variants mutant enzymes
Products: -
Products: -
?
Reactive Black 5 + H2O2
? + H2O
Substrates: no substrate of wild-type
Products: -
Products: -
?
Reactive Black 5 + H2O2
? + H2O
Substrates: no substrate of wild-type
Products: -
Products: -
?
Reactive Blue 19 + 2 H+ + H2O2
oxidized Reactive Blue 19 + 2 H2O
Substrates: dye decolorization
Products: -
Products: -
?
Reactive Blue 19 + 2 H+ + H2O2
oxidized Reactive Blue 19 + 2 H2O
Irpex lacteus F17
Substrates: dye decolorization
Products: -
Products: -
?
Remazol Brilliant Blue R + H2O2
?
Substrates: dye decolorization
Products: -
Products: -
?
Remazol Brilliant Blue R + H2O2
?
Cerrena unicolor BBP6
Substrates: dye decolorization
Products: -
Products: -
?
vanillylacetone + H2O2
?
-
Substrates: reaction in presence of Mn2+
Products: -
Products: -
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
Substrates: -
Products: -
Products: -
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
Irpex lacteus CCTCC AF2014020
Substrates: -
Products: -
Products: -
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
Irpex lacteus F17
Substrates: -
Products: -
Products: -
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
Substrates: substrate of A172W variants mutant enzymes
Products: -
Products: -
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
Substrates: substrate of A172W variants mutant enzymes
Products: -
Products: -
?
veratryl alcohol + H2O2
? + 2 H2O
Substrates: -
Products: -
Products: -
?
veratryl alcohol + H2O2
? + H2O
-
Substrates: reaction in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 4-aminophenol and hydroquinone
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,6-dimethoxyphenol
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the oxidation of Mn(II) to Mn(III), which in turn can oxidize phenolic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 4-aminophenol and hydroquinone
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,6-dimethoxyphenol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme MnP3 shows a broad substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: evaluation of the dye decolorization ability of the purified enzyme, MnP-BBP6, the enzyme is used to decolorize different types of synthetic dyes including RBBR, Congo red (CR), brilliant blue R (BBR), methyl orange (MO), bromophenol blue (BPB), and crystal violet (CV). Denim bleaching by the purified MnP-BBP6
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes humic substances
Products: -
Products: -
?
additional information
?
-
Deuteromycotina sp.
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of Co2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of Fe2+, Cu2+, Zn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no other metal can substitute Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,6-dimethoxyphenol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of Ni2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: dye decolorization
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes polycyclic aromatic hydrocarbons
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes humic substances
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes chlorophenols and arsenic-containing warefare agents
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes nitroaromatic compounds
Products: -
Products: -
?
additional information
?
-
Substrates: the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with veratryl alcohol (VA)
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol (VA)
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes non-phenolic lignin-related compounds, including veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is able to oxidatively depolymerize both dimeric lignin-model compounds and milled spruce-wood lignin
Products: -
Products: -
?
additional information
?
-
-
Substrates: protein complex containing MnP, laccase and beta-glucosidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 3,3,5,5-tetramethylbenzidine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes veratryl alcohol and o-tolidine
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of H2O2 and Mn2+ the enzyme oxidizes lignin and lignin-model compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
Substrates: the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes polycyclic aromatic hydrocarbons
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of Co2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes polycyclic aromatic hydrocarbons
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
Products: -
Products: -
?
additional information
?
-
-
Substrates: primary reaction product of peroxidation with H2O2 is enzyme compound I, formation of compound II from I follows second-order kinetic
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes pinacyanol as most easily oxidized dye at 1.7% of the rate of the Mn2+ oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes ferrocyanide
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes ferrocyanide
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes ferrocyanide
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes ferrocyanide
Products: -
Products: -
?
additional information
?
-
-
Substrates: large substrates have no ready access to the catalytic center
Products: -
Products: -
?
additional information
?
-
-
Substrates: large substrates have no ready access to the catalytic center
Products: -
Products: -
?
additional information
?
-
-
Substrates: presence of proximal and distal histidines at the active center
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes phenol red
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes phenol red
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes phenol red
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes bromide
Products: -
Products: -
?
additional information
?
-
-
Substrates: no other metal can substitute Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes nitroaromatic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,6-dimethoxyphenol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes the polymeric dyes poly R-481 and poly B-411
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of Mn2+ enzyme oxidizes various organic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of Mn2+ enzyme oxidizes various organic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of Mn2+ enzyme oxidizes various organic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of Mn2+ enzyme oxidizes various organic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of Ni2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of Ni2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: enzyme oxidizes phenol red
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium BKMF-1767
-
Substrates: manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium CCTCC AF96007
-
Substrates: manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: enzyme oxidizes ferrocyanide
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: structural properties
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: enzyme oxidizes ferrocyanide
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium OGC101
-
Substrates: Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
-
Substrates: enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
Products: -
Products: -
?
additional information
?
-
Phanerodontia chrysosporium VKM F-1767
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: poor substrates: benzoate, benzaldehyde or benzyl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalytic cycle with oxidized intermediates MnP compound I and II
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn-dependent oxidation of phenols requires superoxide anion and H2O2, phenolic hydroxyl group is essential
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes nitroaromatic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: in presence of Mn2+ enzyme oxidizes various organic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity against phenolic substrates, e.g. phenol red
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-dependent and Mn2+-independent peroxidase activities when tested on the phenolic substrates 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and syringaldazine, more rapid oxidation in presence of Mn2+
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme oxidizes 2,6-dimethoxyphenol
Products: -
Products: -
?
additional information
?
-
-
Substrates: direct oxidation of Rnase by MnP2
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
-
Substrates: in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: Mn2+-independent oxidase activity on NAD(P)H
Products: -
Products: -
?
additional information
?
-
Pseudolagarobasidium sp. PP17-33
-
Substrates: MnP activity is determined by monitoring the oxidation of 2,6-dimethoxyphenol (DMP) as the oxidation of Mn2+ to Mn3+ by following the formation of the Mn3+-tartrate complex at 469 nm
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes nitroaromatic compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: MnP oxidizes synthetic melanoidine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: lingnin containing agricultural waste, like almond shells, hazelnut husks, clover straw, sunflower stems and hazelnut cobs are used as substrate for submerged cultures
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of veratryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of veratryl alcohol
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzo[a]pyrene + ?
?
-
Substrates: key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Bacillus velezensis Al-Dhabi 140
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Phanerodontia chrysosporium BKMF-1767
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Phanerodontia chrysosporium CCTCC AF96007
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Pseudolagarobasidium sp. PP17-33
-
Substrates: -
Products: -
Products: -
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
Substrates: -
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: MnP isoenzymes serve different functions in lignin biodegradation, each may have a preferred substrate
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: initial depolymerization of the lignin polymer
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: Mn2+ is a component of woody plant tissues
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
Products: Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
Products: freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: Mn3+ is produced under lignolytic conditions
Products: Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: acts together with lignin peroxidase in lignin-degradation of white rot fungi
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: acts together with lignin peroxidase in lignin-degradation of white rot fungi
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
Products: Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: acts together with lignin peroxidase in lignin-degradation of white rot fungi
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium BKM-F 1767
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium OGC101
-
Substrates: important component of lignin degradation system
Products: Mn3+ is produced under lignolytic conditions
Products: Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phanerodontia chrysosporium VKM F-1767
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: -
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
Products: the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: preferential degradation of lignin in wheat straw
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: preferential degradation of lignin in wheat straw
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: important component of lignin degradation system
Products: -
Products: -
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Substrates: involved in lignin-degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for lignin degradation
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
heme protein containing protoporphyrin IX, 0.7 heme per enzyme molecule, iron ions are coordinated with prosthetic groups as high-spin ferriheme complexes
heme
-
enzyme contains a pentacoordinated, essentially high-spin ferric heme
heme
-
enzyme contains a pentacoordinated, essentially high-spin ferric heme
heme
-
one iron protoporphyrin IX prosthetic group per enzyme molecule
heme
-
enzyme contains prosthetic heme, substrates are oxidized via delta-meso heme edge of the enzyme
heme
-
heme iron of the native enzyme is ferric, high-spin and pentacoordinate with a proximal histidine ligand, important catalytic residues in the heme pocket are conserved: proximal His-173 and Asp-242, distal His-46, Arg-42, Asn-80 and Glu-74
heme
-
heme environment, Phe-190 plays a critical role in stabilizing the heme environment, it acts as a steric barrier that protects the heme from reducing agents, increasing pH from 5.0 to 8.5 induces a Fe3+ high- to a low-spin transition
heme
-
heme protein
heme
-
important cofactor for production of active recombinant enzyme. Amendment of yeast cultures with heme increases concentrations of active recombinant enzyme
heme b
the enzyme binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit
heme b
manganese peroxidase (MnP) is an extracellular glycosylated heme protein, it harbors one heme b (iron(II)-protoporphyrin IX) group per subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Cd2+ exhibizs octahedral, hexacoordinate ligation geom,etry similar to that of Mn2+. Cd2+ also binds to a putative second weak metal-binding site with tetrahedral geometry at the C-terminus of the protein
Fe2+
Manganese
Mn2+
NaCl
high concentration of NaCl (over 200 mM to 1200 mM) can enhance the activity of isozyme MGMnP1
Sm3+
coordination of Sm(III) at the Mn-binding site is octacoordinate. The reversible binding of Sm(III) may be a useful model for the reversible binding of Mn(III) to the enzyme, which is too unstable to allow similar examination
additional information
Ca2+
the enzyme binds 2 calcium ions per subunit, required, activates
Ca2+
-
MnP calcium binding site, calcium content: 4 mol per mol of native MnP, 2 mol per mol of recombinant and A48C/A63C double mutant MnP, calcium decreases the rate of thermal inactivation
Mn2+
-
stimulates oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate and o-phenylenediamine
Mn2+
Mn2+ binds to MnPs in a site that is composed of three acidic amino acids. Isozyme Il-MnP1 exhibits higher oxidative activity in the presence of Mn2+ than in the absence of Mn2+ toward the majority of the selected substrates at pH 4.0
Mn2+
-
veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
Mn2+
-
Mn2+ causes a concentration-dependent increase in total enzyme activity, little or no activity in absence of Mn2+
Mn2+
-
the proposed role of Mn2+ chelators in the enzyme mechanism is to release Mn3+ from the enzyme
Mn2+
-
required for oxidation of 2,6-dimethoxyphenol, 4-methoxyphenol, 4-aminophenol, guaiacol, alpha-naphthol, vanillylacetone and catechol
Mn2+
-
2,2'-azino-bis(3-ethyl-benzothiazoline)-6-sulfonic acid, guaiacol and 2,6-dimethoxyphenol are oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
additional information
poor effects by 10 mM of Zn2+, Na+, and K+
additional information
-
expression of MnP isoenzymes is dependent on the presence of Mn, expression rather than enzymatic activity is regulated by Mn
additional information
-
MnP synthesis depends on Mn2+ in growth medium
additional information
poor effect on enzyme activity by Mn2+, Na+, and Mg2+ at 0.1-10 mM
additional information
-
poor effect on enzyme activity by Mn2+, Na+, and Mg2+ at 0.1-10 mM
additional information
-
11 ppm Mn2+ in growth medium induces MnP synthesis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
inhibits competitive Mn(III)-malonate formation
ethylhydrazine
-
time-dependent inactivation via delta-meso-ethylheme adduct at pH 7.0, slightly stimulated by Co2+
methylhydrazine
-
slow inactivation in presence of H2O2, concentration- and time-dependent, slightly stimulated by Co2+
nitrilotriacetate
-
inhibits competitive Mn(III)-malonate formation
Pc reducer
-
the activity of manganese peroxidase is inhibited by Pc reducer at concentrations higher than 0.2 mg/ml
-
phenylhydrazine
-
rapid inactivation, concentration-dependent, no heme adducts detectable, inactivation is slightly stimulated by Co2+
Sodium metavanadate
-
partially inhibits only peroxidase activity against veratryl alcohol
2-mercaptoethanol
85% inhibition at 0.1 mM, complete inhibition at 1 mM
Ca2+
30% inhibition at 10 mM, Ca2+ reduces the enzyme stability by 40%
catalase
-
inhibits oxidation of vanillylacetone completely, oxidation of NADH at high concentrations partially
-
catalase
-
inhibits oxidation of NADH in reaction mixture containing alpha-hydroxy acid
-
Cd2+
-
competitive inhibitor to Mn2+, uncompetitive to H2O2, reversibly inhibits oxidation of Mn2+ and Mn3+-mediated oxidation of 2,6-dimethoxyphenol, but not oxidation of phenols in absence of Mn2+, Cd2+ inhibits reduction of compound I and II by Mn2+ at pH 4.5 and binds at the Mn2+-binding site, kinetics of inhibition
Co2+
-
at concentrations below 4 mM in presence of H2O2 competitive inhibitor to Mn2+, slightly stimulates NaN3 or alkylhydrazine inactivation
Cu2+
-
inhibits by catalyzing the H2O2-dependent reduction of Mn3+
diphosphate
-
inhibits oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
diphosphate
-
diphosphate, as a Mn(III) complexing agent can negatively influence the oxidation capacity of Mn3+, which is used to verify the contribution of Mn3+ and other active species to the degradation of SMX
diphosphate
-
inhibits phenol red oxidation to 50%, NADH oxidation at high concentrations partially
H2O2
the enzyme activity is reduced by 10% as the H2O2 concentration increases from 0.1 to 4 mM
H2O2
-
inactivation fits a first-order decay, rapid initial inactivation step
H2O2
-
inhibitory at high concentrations, phenol red is the most sensitive, vanillylacetone the least sensitive substrate to inhibition, Mn2+ protects against inhibition
H2O2
1 mM, complete, irreversible inactivation of wild-type enzyme correlated with the production of methionine sulfoxide, full activity can be retained by engineering Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
Mn2+
-
partial inhibition of oxidation of NAD(P)H at the beginning of the reaction, NADH: 0.1 mM Mn2+ causes 97% inhibition of MP1 and 72% inhibition of MP2
NaN3
-
complete inactivation within 2 min in presence of H2O2, accompanied by azidyl radical formation, prosthetic heme is converted to meso-azido adduct which is more rapidly oxidized by H2O2 than prosthetic heme, 2 equivalents of azide are oxidized before the enzyme molecule is inactivated, inactivation is slightly stimulated by Co2+
Superoxide dismutase
-
inhibits oxidation of vanillylacetone by about 80%
-
Superoxide dismutase
-
inhibits phenol red oxidation to 50%, vanillylacetone oxidation to 90%, NADH oxidation at high concentrations partially
-
Superoxide dismutase
-
inhibits oxidation of NADH in reaction mixture containing acetate
-
additional information
-
not inhibited by 0.1 mM Cu2+, Co2+ or salicylic acid; not inhibited by salicylic acid
-
additional information
-
not inhibited by 5% ethanol, v/v; not inhibited by salicylic acid
-
additional information
-
not inhibited by sodium diphosphate, mannitol, Mn3+-chelators
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
copper
-
ACE1 transcription factor-mediated expression of genes encoding manganese peroxidase
dithiothreitol
-
greatly enhances the oxidation of verartryl alcohol, lignin-model compounds and lignin
glutathione
-
greatly enhances the oxidation of verartryl alcohol, lignin-model compounds and lignin
Pc reducer
-
the activity of manganese peroxidase is promoted by Pc reducer at concentrations less than 0.2 mg/ml
-
Polyglutamate
-
slightly activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
Tartrate
-
the highest rate of Mn3+ formation is obtained with 10 mM tartrate
alpha-hydroxy acid
-
activates by chelating and stabilizing Mn3+ rather than activating the enzyme
alpha-hydroxy acid
-
activates by chelating and stabilizing Mn3+ rather than activating the enzyme
alpha-hydroxy acid
-
stimulates by chelating Mn3+ and stabilizing its high redox potential
citrate
-
stimulates by chelating Mn3+ and stabilizing its high redox potential
citrate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
diphosphate
-
diphosphate proves to be the worst chelator, leading to a specific activity about 4.6% of that obtained with tartrate
H2O2
-
highest Mn2+-oxidation activity when the H2O2 concentration is 0.1 mM
H2O2
-
H2O2-dependent
394594, 394601, 439814, 439815, 439816, 439817, 439820, 439821, 439822, 439823, 439824, 439825, 439826, 439828, 439831, 439832, 439833
H2O2
-
accelerates oxidation of NADH in reaction mixture containing alpha-hydroxy acid, no acceleration in reaction mixture containing acetate
L-Tartrate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
Lactate
-
lactate serves as a chelator for the Mn3+ chelate formation, leading to a specific activity about 48.4% of that obtained with tartrate
Lactate
-
stimulates by complexing with and stabilizing Mn3+
Lactate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential
malonate
-
the highest stimulation of 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate, malonate also serves as a chelator for the Mn3+ chelate formation, leading to a specific activity about 54.8% of that obtained with tartrate
malonate
-
activates, stabilizes Mn3+ in aqueous solution with a relatively high redox potential, most effective physiological chelator excreted by the fungus
malonate
-
stabilizes Mn3+ at a relatively high redox potential and facilitate oxidation of organic substrates
oxalate
-
oxalate serves as a chelator for the Mn3+ chelate formation, leading to a specific activity about 64.7% of that obtained with tartrate
oxalate
-
activates by chelating and stabilizing Mn3+
succinate
-
activates, stabilizes Mn3+ less effective than citrate or lactate
Tween 80
-
enhances oxidation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
additional information
-
no Mn3+ chelators and activators: acetate, propionate, citrate, D-malate, ethylene glycol
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
production of MnP is induced by nitrogen limitation and by oxygen
-
additional information
-
dramatic stimulation by chelating organic acids as C2- and C3-dicarboxylic or alpha-hydroxyl acids facilitate the dissociation of Mn(III) from manganese-enzyme complex, greater activation with weakly binding chelators with a low binding constant, e.g. lactate or tartrate
-
additional information
-
succinate, formate and acetate do not stabilize Mn3+
-
additional information
-
succinate is no Mn3+ chelator and activator
-
additional information
-
1 mM verartryl alcohol in growth medium increases activity 2fold
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
additional information
-
strong increase of MnP levels by growth in presence of peptone, compared with glucose-ammonium tartrate medium
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Macular Degeneration
Recombinant Manganese Peroxidase Reduces A2E Burden in Age-Related and Stargardt's Macular Degeneration Models.
Starvation
Characterization of manganese peroxidases from the hyperlignolytic fungus IZU-154.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0478
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
30°C, pH 4.5
0.083
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 45°C, recombinant His6-tagged enzyme
0.06
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
mutant S168W, 25°C, pH 5.0
0.667
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
-
0.1 mM H2O2, Mn2+-independent activity, MnP1
0.0713
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
0.196
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
0.0125
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-independent activity
0.015
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-dependent activity
0.0156
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+
0.053
2,6-dimethoxyphenol
pH 4.5, 55°C, recombinant His6-tagged enzyme
0.076
2,6-dimethoxyphenol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
0.096
2,6-dimethoxyphenol
pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+
0.435
2,6-dimethoxyphenol
pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+
3.03
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166G, in absence of Mn2+
3.76
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+
3.96
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+
6.954
2,6-dimethoxyphenol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
7.23
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant wild-type enzyme, in absence of Mn2+
0.0365
guaiacol
pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+
0.195
guaiacol
pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+
0.213
guaiacol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
0.271
guaiacol
pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+
1.3
guaiacol
pH 4.0, 30°C, recombinant wild-type enzyme, in absence of Mn2+
2.3
guaiacol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
4.63
guaiacol
pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+
5.75
guaiacol
pH 4.0, 30°C, recombinant mutant E166G, in absence of Mn2+
6.31
guaiacol
pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+
0.039 - 0.041
H2O2
-
MnP1 from mutants F190Y, F190L, F190I and F190A
0.011
Mn(II)
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
0.0122
Mn(II)
pH 5.0, 25°C, recombinant isozyme
0.0226
Mn(II)
pH 5.0, 25°C, recombinant isozyme
0.074 - 0.08
Mn2+
-
MnP1 from mutants F190Y, F190L, F190I and F190A
0.293
pyrogallol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
3.74
pyrogallol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
0.0044
Reactive Black 5
pH 3.0, 35°C, recombinant His6-tagged enzyme
0.0054
Reactive Black 5
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
0.56
veratryl alcohol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
21.6
veratryl alcohol
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
additional information
2,6-dimethoxyphenol
-
apparent Km, 417 microM/l, chromatographic MnP form 1
additional information
2,6-dimethoxyphenol
-
apparent Km, 216 microM/l, chromatographic MnP form 2
additional information
2,6-dimethoxyphenol
-
apparent Km, 516 microM/l, chromatographic MnP form 3
additional information
Mn2+
-
apparent Km, 24 microM/l, chromatographic MnP form 1
additional information
Mn2+
-
apparent Km, 44 microM/l, chromatographic MnP form 2
additional information
Mn2+
-
apparent Km, 47 microM/l, chromatographic MnP form 3
additional information
additional information
-
additional information
-
additional information
additional information
-
additional information
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
87.1
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid)
-
30°C, pH 4.5
1.4
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
mutant S168W, 25°C, pH 5.0
245
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 45°C, recombinant His6-tagged enzyme
1.87
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
20.2
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
120
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-dependent activity
139
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
Mn2+-independent activity
1.82
2,6-dimethoxyphenol
pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+
5.67
2,6-dimethoxyphenol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
26.26
2,6-dimethoxyphenol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
37.86
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant wild-type enzyme, in absence of Mn2+
80.1
2,6-dimethoxyphenol
pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+
148
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+
379
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+
647
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+
989
2,6-dimethoxyphenol
pH 4.5, 55°C, recombinant His6-tagged enzyme
2590
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166G, in absence of Mn2+
0.74
guaiacol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
0.75
guaiacol
pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+
8.92
guaiacol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
11.26
guaiacol
pH 4.0, 30°C, recombinant wild-type enzyme, in absence of Mn2+
20.54
guaiacol
pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+
26.15
guaiacol
pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+
64.57
guaiacol
pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+
142
guaiacol
pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+
5.3
Mn(II)
pH 5.0, 25°C, recombinant isozyme
9.1
Mn(II)
pH 5.0, 25°C, recombinant isozyme
66.9
Mn(II)
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
24
Mn2+
-
A48C/A63C double mutant MnP after thermal treatment at 37°C for 15 min
9.98
pyrogallol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C
20.95
pyrogallol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
7
Reactive Black 5
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
0.45
veratryl alcohol
-
in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C
1.69
veratryl alcohol
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2951.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 45°C, recombinant His6-tagged enzyme
23
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid)
mutant S168W, 25°C, pH 5.0
4.18
2,6-dimethoxyphenol
pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+
5.24
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant wild-type enzyme, in absence of Mn2+
95.7
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+
172.1
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+
834.4
2,6-dimethoxyphenol
pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+
854.8
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant mutant E166G, in absence of Mn2+
9487
2,6-dimethoxyphenol
pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+
18660.4
2,6-dimethoxyphenol
pH 4.5, 55°C, recombinant His6-tagged enzyme
3.85
guaiacol
pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+
4.14
guaiacol
pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+
8.66
guaiacol
pH 4.0, 30°C, recombinant wild-type enzyme, in absence of Mn2+
13.95
guaiacol
pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+
75.79
guaiacol
pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+
3890
guaiacol
pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+
402.7
Mn(II)
pH 5.0, 25°C, recombinant isozyme
434.4
Mn(II)
pH 5.0, 25°C, recombinant isozyme
6060
Mn(II)
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
1310
Reactive Black 5
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
0.078
veratryl alcohol
mutant T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G, 25°C, pH 5.0
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
transient-state inhibition constants
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.04
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, dialyzed extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 4.0
0.1
-
specific MnP activity recovered from solid-state culture after 3h and 10°C, U/mg of fugal biomass, pH 6.0
0.12
-
specific MnP activity recovered from solid-state culture after 3h and 25°C, U/mg of fugal biomass, pH 6.0
0.16
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, dialyzed extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 5.0
0.2
-
specific MnP activity recovered from solid-state culture after 1h and 25°C, U/mg of fugal biomass, pH 4.0
0.21
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, dialyzed extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 5.0
0.27
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, dialyzed extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 4.0
0.31
0.35
0.41
0.45
-
specific MnP activity recovered from solid-state culture after 1h and 25°C, U/mg of fugal biomass, pH 5.0
0.48
-
specific MnP activity recovered from solid-state culture after 3h and 25°C, U/mg of fugal biomass, pH 4.0
0.7
-
specific MnP activity recovered from solid-state culture after 3h and 25°C, U/mg of fugal biomass, pH 5.0
10.2
-
oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate in presence of Mn2+ and H2O2
169
-
purification step chromatography on a concanavalin-A Sepharose column
288
40
additional information
0.01
-
specific MnP activity recovered from solid-state culture after 1h and 10°C, U/mg of fugal biomass, pH 6.0
0.01
-
specific MnP activity recovered from solid-state culture after 1h and 25°C, U/mg of fugal biomass, pH 6.0
0.31
-
specific MnP activity recovered from solid-state culture after 3h and 10°C, U/mg of fugal biomass, pH 4.0
0.31
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, crude extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 4.0
0.35
-
specific MnP activity recovered from solid-state culture after 1h and 10°C, U/mg of fugal biomass, pH 4.0
0.35
-
specific MnP activity recovered from solid-state culture after 1h and 10°C, U/mg of fugal biomass, pH 5.0
0.35
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, crude extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 4.0
0.35
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, crude extract, extraction conducted for 1h without agitation, U/mg of fugal biomass, pH 5.0
0.41
-
specific MnP activity recovered from solid-state culture after 3h and 10°C, U/mg of fugal biomass, pH 5.0
0.41
-
effect of dialysis on MnP recovered from solid-state culture at 10°C, crude extract, extraction conducted for 3h at 100 rpm, U/mg of fugal biomass, pH 5.0
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
oxidative activity for phenols/non-phenols by recombinant isozyme Il-MnP1 in the presence/absence of Mn2+ in U/l, overview. For monophenols (DMP, guaiacol) without Mn2+, the reaction results in a 95% reduction of oxidative activity, whereas bisphenols are only found to obtain a 20% reduction (catechol) or 50% increase (HQ). As for non-phenols, veratryl alcohol is oxidized only when Mn2+ is present, while Il-MnP1 still retains 70% of its oxidative activity toward ABTS in the absence of Mn2+
additional information
-
oxidative activity for phenols/non-phenols by recombinant isozyme Il-MnP1 in the presence/absence of Mn2+ in U/l, overview. For monophenols (DMP, guaiacol) without Mn2+, the reaction results in a 95% reduction of oxidative activity, whereas bisphenols are only found to obtain a 20% reduction (catechol) or 50% increase (HQ). As for non-phenols, veratryl alcohol is oxidized only when Mn2+ is present, while Il-MnP1 still retains 70% of its oxidative activity toward ABTS in the absence of Mn2+
additional information
-
maximum MnP activity for strain NITW715076_2 is 92.77 U/ml at 50°C. For strains NITW715076_1 and NITW715076, the MnP activity is 145.65 U/ml1 at 70°C and 107.24 U/ml1 at 60°C, respectively
additional information
-
66.6, 1 unit: oxidation of 3,3,5,5-tetramethylbenzidine so that the change in A650 is 0.01 per min
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
216-467, 1 unit: initial increase in absorbance of 1.0 per min at 465 nm
additional information
-
216-467, 1 unit: initial increase in absorbance of 1.0 per min at 465 nm
additional information
0.076 U/ml, wild-type enzyme, in the presence of 2,6-dimethoxyphenol
additional information
-
0.076 U/ml, wild-type enzyme, in the presence of 2,6-dimethoxyphenol
additional information
0.055 U/ml, R42A mutant, in the presence of 2,6-dimethoxyphenol
additional information
-
0.055 U/ml, R42A mutant, in the presence of 2,6-dimethoxyphenol
additional information
0.069 U/ml, N131D mutant, in the presence of 2,6-dimethoxyphenol
additional information
-
0.069 U/ml, N131D mutant, in the presence of 2,6-dimethoxyphenol
additional information
-
425 U/l of MnP is extracted from the liquid fermentation medium of Phanerochaete chrysosporium and exhibits an efficient catalytic performance for SMX transformation. Optimal activity when the external parameters are designed at pH 5.0, an enzyme activity above 40 U/l, and an H2O2 concentration of 0.2 mM
additional information
Pseudolagarobasidium sp. PP17-33
-
screening of enzyme activity duirng optimization of enzyme production method from Pseudolagarobasidium sp. PP17-33, overview
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
additional information
-
284-422: 5 isozymes, expressed as spectral change in DELTAA per min and mg of heme-containing protein
additional information
-
enzyme yield is species-dependent and strain-dependent, the carbon source and lignocellulosic substrate play a crucial role in enzyme production
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
3.5 - 4.5
4 - 4.5
4.5
4.8
additional information
3
-
oxidation of 2,6-dimethoxyphenol and veratryl alcohol in absence of Mn2+
3
-
oxidation of 2,6-dimethoxyphenol and veratryl alcohol in absence of Mn2+
4
-
decolorization of bromocresol green, bromophenol red, bromothymol blue, o-cresol red, m-cresol purple, phenol red and thymol blue
4.5
-
oxidation of 2,2-azino-bis-3-ethyl-6-benzothiazolinesulfonate
additional information
when comparing the oxidative activity of Il-MnP1 between pH 4.0 and pH 7.4, the oxidative activity of Il-MnP1 at pH 4.0 is usually higher than that at pH 7.4. But there are some exceptions
additional information
-
when comparing the oxidative activity of Il-MnP1 between pH 4.0 and pH 7.4, the oxidative activity of Il-MnP1 at pH 4.0 is usually higher than that at pH 7.4. But there are some exceptions
additional information
-
isozyme H5: pI 4.2, isoenzyme H4: pI 4.5, isoenzyme H3: pI 4.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 6
-
active in the range, below pH 2 and above pH 6: completely inactive
3 - 3.5
-
pH 3.5: decrease of 95% of oxidation of Mn2+, pH 3: nearly no oxidation of Mn2+
3 - 5
-
oxidation of veratryl alcohol decreases more than 95% when the pH is increased from 3 to 4.5 and nearly absent at pH 5
3 - 8
3.1 - 6.1
-
veratryl alcohol oxidation, activity increases with increasing pH
3.1 - 8.3
-
in presence of H2O2 the formation of enzyme compound I is independent of pH over the range
3.5 - 6
3.5 - 6.5
-
Mn2+ oxidation shows an optimum in the range 5.5-5.75 and negligible activity at pH values below 3.5 and above 6.5
4 - 5.5
-
about half-maximal activity at pH 4.0 and 5.5, 2,2-azino-bis-3-ethyl-6-benzothiazolinesulfonate-oxidation
4.5 - 5.7
-
about 65% of maximal activity at pH 4.5 and about 50% at pH 5.7, Mn(III)-lactate formation
5.5 - 5.8
-
the pH-activity profile for Mn2+ oxidation shows an optimum in the range 5.5 - 5.75 and negligible activity at pHs below 3.5 and above 6.5
3 - 8
the highest activity of all enzymes with all tested substrates is at pH 3, except for the WT with 2,6-DMP as a substrate, for which the activity is almost twice as high at pH 8 than that at pH 3. Although the activity of the mutants towards ABTS drops to 5-10% at pH 5 and higher, the residual activities of the mutants towards Reactive Black 5 and veratryl alcohol drops less at higher pH values (20-40% residual activity at pH 5). For 2,6-dimethoxyphenol as a substrate, the activities of MrMnP1 and mutants are lowest at pH 6, but increase at pH 7 and pH 8. The activity at high pH values is transient, presumably due to Ca2+ loss and inactivation of the enzyme. Autoxidation of 2,6-DMP in Britton Robinson buffer at pH 8 in the presence of H2O2 is not detected
3.5 - 6
-
pH 3.5: about 30% of maximal activity, pH 4.0: about 70% of maximal activity, pH 6.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
35
37
40
45
50 - 70
-
maximum MnP activity for strain NITW715076_2 is observed at 50°C, for strains NITW715076_1 and NITW715076 at 70°C and 60°C, respectively
60
additional information
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
-
the enzyme shows relative activities of 34, 50, and 47% at 10, 40, and 60°C, respectively
20 - 35
-
the activity increases raising culture initial temperature from 20°C to 35°C, with a maximum degrading value of 76.7 mg/l at 35°C, which is 1.5fold higher than that at 20°C
25 - 45
-
25°C: about 80% of maximal activity, 45°C: about 60% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Deuteromycotina sp.
Phanerodontia chrysosporium BKM-F-1767
MG-60 TUFC40001, isolated from a mangrove forest, three manganese peroxidase (MGMnP) isozymes: MGMnP1, MGMnP2, and MGMnP3
UniProt
brenda
Pseudolagarobasidium sp. PP17-33
fruiting bodies of basidiomycete fungi found on decayed or fallen wood are collected from various parts of Thailand, e.g. provinces of Chaiyaphum, Nakhon Phanom, Sakon Nakhon and Udon Thani
-
-
brenda
3 isoenzymes: Mn2+-inducible MnP1 and MnP3, partly constitutive MnP2
-
-
brenda
Deuteromycotina sp.
fungi IZU-154, FERM BP-1859, hyperlignolytic fungus IZU-154, belongs to the family Deuteromycotina and is deposited as the strain name of NK-1148, 4 isoenzymes
-
-
brenda
white rot fungus, strains L-14807, L-15225, FP-104027, FP-90031-sp, FP-105752
-
-
brenda
dikaryotic strain TMI 800, protein complex containing MnP, laccase and beta-glucosidase activities
-
-
brenda
white rot fungus, syn. Corticium sordidum, strain HHB-8922-sp, 3 isoenzymes: MnPI, MnPII and MnPIII
-
-
brenda
-
394594, 394601, 439817, 439821, 439822, 439823, 439824, 439826, 439828, 439831, 439832, 439833, 439839, 439846, 439850, 439851, 439852, 439853, 439854
-
-
brenda
isozyme profile depends on type of nutrient limitation and growth phase: no H5 in C-limited cultures, manganese increases H3-production
-
-
brenda
MnP exists as several closely related isoenzymes
-
-
brenda
white rot basidomycete
394594, 394601, 439814, 439815, 439816, 439821, 439822, 439823, 439824, 439825, 439826, 439831, 439833, 439839, 439846, 439854
-
-
brenda
precursor. Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
UniProt
brenda
white rot fungus, strain CBS 613.91, 2 isoenzymes: MnP1 and MnP2
-
-
brenda
importance of media composition in the production of different isoenzymes
-
-
brenda
white rot basidomycete, 3 isoenzymes: MnP1, MnP2 and MnP3
-
-
brenda
3 isoenzymes: Mn2+-inducible MnP1 and MnP3, partly constitutive MnP2
-
-
brenda
syn. Coriolus versicolor, white rot basidomycete, strain PRL 572, 5 isoenzymes
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
higher concentrations of foam and lower levels of spore inoculums result in the formation of scattered mycelial pellets, increased autolysis of chlamydospore-like cells (a reservoir of MnP), and a higher activity of MnP. Even though MnP is a secondary metabolite, the addition of 5times more glucose and diammonium tartrate, as carbon and nitrogen sources, results in a 4fold increase in the dry cell mass. MnP activity decreases under these conditions to less than half, due to the formation of increasingly dense pellets and the inhibited lysis of chlamydospore-like cells
brenda
this fungus expresses three kinds of manganese peroxidase (MGMnP) isozymes, MGMnP1, MGMnP2, and MGMnP3 in low nitrogen medium (LNM) or LNM containing NaCl, but hardly produces native MnP in a high-nitrogen medium (HNM)
brenda
additional information
-
shallow stationary culture growing on N-limited medium
brenda
-
production of ligninolytic enzyme MnP in liquid fermentation medium of Phanerochaete chrysosporium strain BKMF-1767
brenda
Phanerodontia chrysosporium BKMF-1767
-
production of ligninolytic enzyme MnP in liquid fermentation medium of Phanerochaete chrysosporium strain BKMF-1767
-
brenda
Phanerodontia chrysosporium CCTCC AF96007
-
production of ligninolytic enzyme MnP in liquid fermentation medium of Phanerochaete chrysosporium strain BKMF-1767
-
brenda
-
strain Al-Dhabi 140 is grown in mineral salt medium containing 25, 50, 75, 100, 125, 150, 175 and 200 mg/l of tetracycline with 7% inoculum under shaking condition at 150 rpm.Tetracycline concentration in the culture medium is assayed after eight days. The degradation potential by strain Al-Dhabi 140 is 71 mg/l and 75.3 mg/l when the tetracycline concentration is 125 and 150 mg/l, respectively
brenda
Bacillus velezensis Al-Dhabi 140
-
strain Al-Dhabi 140 is grown in mineral salt medium containing 25, 50, 75, 100, 125, 150, 175 and 200 mg/l of tetracycline with 7% inoculum under shaking condition at 150 rpm.Tetracycline concentration in the culture medium is assayed after eight days. The degradation potential by strain Al-Dhabi 140 is 71 mg/l and 75.3 mg/l when the tetracycline concentration is 125 and 150 mg/l, respectively
-
brenda
-
grown on Japanese beech and cedar wood, Eucalyptus grandis wood, and Bamboo culms
brenda
grown on solid-state fermentation medium
brenda
grown on wheat straw, rice straw, agriculture byproducts, or agro-industrial wastes
brenda
additional information
-
the optimum temperatures for MnP production from NITW715076_2, NITW715076_1 and NITW715076 isolates are 50°C, 70°C, and 60°C, respectively. Fermentation is carried out using hydrolysate obtained after pre-treatment. The hydrolysate is mixed with 3 ml of pure MnP and 0.1% w/v Saccharomyces cerevisiae for 384 h at 35°C. The optimized conditions achieved for enzyme production are pH 6.5, temperature 35°C, agitation speed 130 rpm, carbon source sucrose (1%), nitrogen source yeast extract (0.5%) and inoculum volume 4 ml/100 ml
brenda
additional information
Pseudolagarobasidium sp. PP17-33
-
the white-rot fungus Pseudolagarobasidium sp. PP17-33 can be utilized for valuable manganese peroxidase (MnP) enzyme production from oil palm decanter cake. Optimization to enhance the production of enzymes through solid-state fermentation is performed using Plackett-Burman design and response surface methodology. The highest observed MnP is 5.156 U/gds, which enhanceds yield by 1.94fold from the non-optimization. The optimized medium (mg/g of OPDC) consists of 0.852 mg CuSO4/5H2O, 13.512 mg glucose, 2 mg yeast extract, 0.2 mg KH2PO4, 1.5 mg MgSO4/7H2O, 0.01 mg FeSO4/7H2O, 0.15 mg MnSO4/H2O, 0.01 mg ZnSO4/7H2O and 0.3 mg Tween 80, pH 5.0, when incubated at 30°C for 7 days. The most significant variables of MnP productions are CuSO4/5H2O and glucose concentrations
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
manganese peroxidase (MnP) is an extracellular glycosylated heme protein
-
brenda
Cerrena unicolor BBP6
-
manganese peroxidase (MnP) is an extracellular glycosylated heme protein
-
-
brenda
-
-
-
394601, 439814, 439815, 439816, 439817, 439820, 439821, 439822, 439823, 439824, 439825, 439826, 439828, 439831, 439832, 439833, 439839, 439846, 439850, 439851, 439852, 439854
brenda
-
appears to be closely related to mycelium
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
maganese peroxidases (MnPs) can be divided into groups of short, long, and extra-long MnPs. The length of long MnPs is 348-361 amino acids, extra-long MnPs are longer than 362 amino acids, and short MnPs are no longer than 348 amino acids. The long and extralong MnPs are characterized by a C-terminal tail that surrounds the main heme access channel, preventing oxidation of low-redox-potential substrates (e.g. ABTS, 2,6-DMP). MrMnP1 is 343 amino acids long and can be categorized as a short MnP
evolution
MnP124076 is the only short MnP found in Ceriporiopsis subvermispora, MnP157986 is an extralong MnP and has the longest amino acid sequence. MnP50297 and MnP117436 are an extralong MnP and a long MnP, respectively, and they are the most abundantly produced MnPs in each subfamily by Ceriporiopsis subvermispora grown in aspen wood-containing medium
evolution
the enzyme belongs to the ligninolytic peroxidase gene family, 13 MnP genes and five dye-decolorizing peroxidase (DyP) genes are present in the Irpex lacteus strain F17 genome, they represent two different families of heme peroxidases and are unrelated to the fungal class II peroxidases
evolution
MGMnPs may have evolved to adapt to chloride-rich environments, e.g. mangrove forests
evolution
-
DNA sequence comparisons and phylogenetic analysis and tree
evolution
-
MnP124076 is the only short MnP found in Ceriporiopsis subvermispora, MnP157986 is an extralong MnP and has the longest amino acid sequence. MnP50297 and MnP117436 are an extralong MnP and a long MnP, respectively, and they are the most abundantly produced MnPs in each subfamily by Ceriporiopsis subvermispora grown in aspen wood-containing medium
-
evolution
-
maganese peroxidases (MnPs) can be divided into groups of short, long, and extra-long MnPs. The length of long MnPs is 348-361 amino acids, extra-long MnPs are longer than 362 amino acids, and short MnPs are no longer than 348 amino acids. The long and extralong MnPs are characterized by a C-terminal tail that surrounds the main heme access channel, preventing oxidation of low-redox-potential substrates (e.g. ABTS, 2,6-DMP). MrMnP1 is 343 amino acids long and can be categorized as a short MnP
-
evolution
Irpex lacteus F17
-
the enzyme belongs to the ligninolytic peroxidase gene family, 13 MnP genes and five dye-decolorizing peroxidase (DyP) genes are present in the Irpex lacteus strain F17 genome, they represent two different families of heme peroxidases and are unrelated to the fungal class II peroxidases
-
evolution
Irpex lacteus CCTCC AF2014020
-
the enzyme belongs to the class II fungal peroxidases (PODs)
-
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides
physiological function
-
enzyme MnP generates Mn3+ (act as a diffusible charge transfer mediators) which can oxidize a large amount of phenolic substrates such as simple phenols, amines, dyes as well as phenolic lignin model compounds. In contrast to laccase, MnP is not capable of oxidizing the more recalcitrant nonphenolic compounds
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
the manganese peroxidase of Irpex lacteus strain 17 is able to degrade recalcitrant aromatic pollutants
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
the crude manganese peroxidase from Bacillus velezensis strain Al-Dhabi 140 shows an optimum degradation process and maximum removal efficacy of 87 mg/l at tetracycline concentration 143.75 mg/l, pH 6.9, and 8.04% inoculum
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
Irpex lacteus CD2
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
Irpex lacteus F17
-
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
-
physiological function
Irpex lacteus F17
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
Irpex lacteus F17
-
the manganese peroxidase of Irpex lacteus strain 17 is able to degrade recalcitrant aromatic pollutants
-
physiological function
Irpex lacteus CCTCC AF2014020
-
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
-
physiological function
Cerrena unicolor BBP6
-
manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides
-
physiological function
Cerrena unicolor BBP6
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
Ganoderma lucidum IBL-05
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
Irpex lacteus CCBAS238
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
Bacillus velezensis Al-Dhabi 140
-
the crude manganese peroxidase from Bacillus velezensis strain Al-Dhabi 140 shows an optimum degradation process and maximum removal efficacy of 87 mg/l at tetracycline concentration 143.75 mg/l, pH 6.9, and 8.04% inoculum
-
physiological function
Phanerodontia chrysosporium BKMF-1767
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
-
physiological function
Phanerodontia chrysosporium CCTCC AF96007
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
-
additional information
-
GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
-
GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
additional information
-
the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
additional information
-
screening and tetracycline degrading efficiency of the five bacteria isolated from the municipal soil sludge, overview. The strain termed Al-Dhabi 140 from Bacillus velezensis shows the highest activity
additional information
-
GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
-
GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
-
the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
-
additional information
Irpex lacteus CCTCC AF2014020
-
role of Glu166 in the Mn2+-independent activity
-
additional information
Bacillus velezensis Al-Dhabi 140
-
screening and tetracycline degrading efficiency of the five bacteria isolated from the municipal soil sludge, overview. The strain termed Al-Dhabi 140 from Bacillus velezensis shows the highest activity
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PEM3_PHLRA
362
0
37815
Swiss-Prot
other Location (Reliability: 3)
M2REM6_CERS8
Ceriporiopsis subvermispora (strain B)
386
0
40337
TrEMBL
-
S4W784_IRPLA
359
0
37829
TrEMBL
Secretory Pathway (Reliability: 1)
V2XS39_MONRO
Moniliophthora roreri (strain MCA 2997)
362
0
37718
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36600
-
x * 36600, MALDI-TOF mass spectrometric analysis, more accurate reflection of the true molecular weight than by SDS-PAGE
38000 - 45000
40000
40000 - 43000
41000
42000
43000
44000
44500
45000
46000
48000
49000
50500
660000
-
protein complex containing MnP, laccase and beta-glucosidase, gel filtration
44000
-
x * 44000, isozyme TvMP4, x * 44500, isozyme TvMP2 and TvMP5, 1 * 45000, isozyme TvMP1 and TvMP3, SDS-PAGE
44500
-
x * 44000, isozyme TvMP4, x * 44500, isozyme TvMP2 and TvMP5, 1 * 45000, isozyme TvMP1 and TvMP3, SDS-PAGE
45000
-
x * 44000, isozyme TvMP4, x * 44500, isozyme TvMP2 and TvMP5, 1 * 45000, isozyme TvMP1 and TvMP3, SDS-PAGE
46000
-
-
46000
-
x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 36600, MALDI-TOF mass spectrometric analysis, more accurate reflection of the true molecular weight than by SDS-PAGE
?
-
x * 36600, MALDI-TOF mass spectrometric analysis, more accurate reflection of the true molecular weight than by SDS-PAGE
-
?
x * 44600, recombinant refolded His6-tagged enzyme, SDS-PAGE, x * 38200, about, MnP6, sequence calculation
?
Irpex lacteus F17
-
x * 44600, recombinant refolded His6-tagged enzyme, SDS-PAGE, x * 38200, about, MnP6, sequence calculation
-
?
-
x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
?
Phanerodontia chrysosporium OGC101
-
x * 46000, wild-type and mutants R177D, R177E, R177N and R177Q, SDS-PAGE
-
?
-
x * 44000, isozyme TvMP4, x * 44500, isozyme TvMP2 and TvMP5, 1 * 45000, isozyme TvMP1 and TvMP3, SDS-PAGE
monomer
Phanerodontia chrysosporium VKM F-1767
-
1 * 45000, PCH4 and PCH6, 1 * 43000, PCH5, SDS-PAGE
-
additional information
products of the MnP isozyme genes MGmnp1, MGmnp2, and MGmnp3 are identified by peptide mass fingerprinting analysis as the MnP isozymes at 45, 50, and 47 kDa respectively
additional information
products of the MnP isozyme genes MGmnp1, MGmnp2, and MGmnp3 are identified by peptide mass fingerprinting analysis as the MnP isozymes at 45, 50, and 47 kDa respectively
additional information
products of the MnP isozyme genes MGmnp1, MGmnp2, and MGmnp3 are identified by peptide mass fingerprinting analysis as the MnP isozymes at 45, 50, and 47 kDa respectively
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
2 isoenzymes differ in glycosylation degree, anthrone analysis: 5-7% total carbohydrate, SDS-PAGE after Endo-H treatment: 4.5% N-linked carbohydrate content in BOS1 and 2.3% in BOS2
glycoprotein
-
2 isoenzymes differ in glycosylation degree, anthrone analysis: 5-7% total carbohydrate, SDS-PAGE after Endo-H treatment: 4.5% N-linked carbohydrate content in BOS1 and 2.3% in BOS2
-
glycoprotein
manganese peroxidase (MnP) is an extracellular glycosylated heme protein
glycoprotein
Cerrena unicolor BBP6
-
manganese peroxidase (MnP) is an extracellular glycosylated heme protein
-
glycoprotein
-
neutral carbohydrate content: MnP1: 8.5%, MnP2: 10.3%
-
glycoprotein
-
the enzyme displays an extent of N-glycosylation of about 5.3% of the high-mannose type
glycoprotein
-
the enzyme displays an extent of N-glycosylation of about 5.3% of the high-mannose type
-
glycoprotein
-
N-glycosylation of about 5.3% of the high-mannose type
-
glycoprotein
-
the enzyme displays an extent of N-glycosylation of about 5.3% of the high-mannose type
-
glycoprotein
-
-
glycoprotein
-
glycoprotein with one recognition sequence for N-linked carbohydrate at Asp-217, residue at position 10 is a potential site for O-glycosylation
glycoprotein
native MnP is glycosylated, but not recombinant MnP
glycoprotein
-
with 3 potential N-glycosylation sites, but only Asn-131 binds to carbohydrate
glycoprotein
-
the recombinant enzyme produced by ZBMNP16 is hyperglycosylated
glycoprotein
Phanerodontia chrysosporium BKM-F 1767
-
glycoprotein with one recognition sequence for N-linked carbohydrate at Asp-217, residue at position 10 is a potential site for O-glycosylation
-
glycoprotein
-
with 3 potential N-glycosylation sites, but only Asn-131 binds to carbohydrate
-
glycoprotein
-
native MnP is glycosylated, but not recombinant MnP
-
glycoprotein
-
TvMnP1: 6% w/w carbohydrates, 0.6 mol glucose, 9.8 mol mannose and 6.7 mol glucosamine per mol protein, TvMnP2: 4% w/w carbohydrates, 0.8 mol glucose, 6.4 mol mannose and 3.6 mol glucosamine per mol protein, glucose may be from gel filtration on Sephadex
proteolytic modification
Deuteromycotina sp.
-
leader sequence at the N-terminus: first 24 amino acids possess characteristics of signal peptides
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure
hanging drop vapor diffusion method, enzyme-Mn(II) structure at 1.45 A resolution, enzyme -Cd(II) structure, enzyme-Sm(III) structure, metal-free structure
manganese peroxidase crystallizes in the presence of Mn2+, where three homologous residues (Glu35, Glu39, and Asp179) participate in metal co-ordination, opening of the glutamate side-chains is not observed in manganese peroxidase crystals grown in the absence of Mn2+
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S168W
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
S168W
-
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
-
T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
-
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
-
E166D
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
E166G
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
E166Q
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
E166D
Irpex lacteus CCTCC AF2014020
-
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
-
E166G
Irpex lacteus CCTCC AF2014020
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
-
E166Q
Irpex lacteus CCTCC AF2014020
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
-
E166D
Irpex lacteus F17
-
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
-
E166G
Irpex lacteus F17
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
-
E166Q
Irpex lacteus F17
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
-
A172W
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/A269R
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant does not show altered kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/A273T
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/F259M
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/I171V
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/K168V
site-directed mutagenesis, the mutant shows increased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W
-
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A172W/F259M
-
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A172W/I171V
-
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A172W/K168V
-
site-directed mutagenesis, the mutant shows increased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A48C/A63C
-
A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
M273L
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
N131D
mutant displays a similar catalysis pattern to that of wild-type enzyme, Asn131 is the only potential glycosylation site
N81S
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177Q
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R42A
mutant displays a similar catalysis pattern to that of wild-type enzyme, Arg42 is forming the peroxide binding pocket
S168W
-
mutant can oxidize both Mn2+ and typical lignin peroxidase substrates such as veratryl alcohol
M273L
-
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
-
N81S
-
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
-
F190A
Phanerodontia chrysosporium OGC101
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
-
F190I
Phanerodontia chrysosporium OGC101
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190L
Phanerodontia chrysosporium OGC101
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
R177A
Phanerodontia chrysosporium OGC101
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177D
Phanerodontia chrysosporium OGC101
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177E
Phanerodontia chrysosporium OGC101
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177K
Phanerodontia chrysosporium OGC101
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177N
Phanerodontia chrysosporium OGC101
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
additional information
additional information
-
usage of a fibrous bed reactor to culture of Bacilllus velezensis strain Al-Dhabi 140 on fibrous matrix to transform tetracycline in synthetic wastewater. The transformed product of tetracycline from the fibrous bed reactor is evident by the activity of ligninolytic enzymes produced by Bacillus velezensis strain Al-Dhabi 140 in reactor. Decrease in antibacterial potency by tetracycline degradation is obtained after 10 days. The zone of inhibition is 24 mm at day 1 and 9 mm at day 10
additional information
Bacillus velezensis Al-Dhabi 140
-
usage of a fibrous bed reactor to culture of Bacilllus velezensis strain Al-Dhabi 140 on fibrous matrix to transform tetracycline in synthetic wastewater. The transformed product of tetracycline from the fibrous bed reactor is evident by the activity of ligninolytic enzymes produced by Bacillus velezensis strain Al-Dhabi 140 in reactor. Decrease in antibacterial potency by tetracycline degradation is obtained after 10 days. The zone of inhibition is 24 mm at day 1 and 9 mm at day 10
-
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
-
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
-
additional information
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
additional information
-
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
additional information
Irpex lacteus CCTCC AF2014020
-
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
additional information
Irpex lacteus F17
-
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
additional information
-
MnP production from NITW715076_2, NITW715076_1, and NITW715076 isolates
additional information
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
additional information
-
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
additional information
-
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7.5
purified enzyme, 30°C, full stability at pH 4.5, below 10% activity remaining at pH 3.0 and pH 7.5, 90% at pH 4.0, 80% at pH 5.0, and 30% at pH 6.0
3.5 - 4.7
over 50% of maximal activity remains, recombinant enzyme, pH stability profile, overview
3.5 - 5.5
-
the enzyme shows a half-life of 8.8 h at pH 3.5, the half-lives of MnP activity at pH 4.5, 5.0, and 5.5 are 89.5, 99, and 101 h, respectively
3.5 - 7.5
purified recombinant refolded His6-tagged enzyme retaining 75% of maximal activity within this range
4.5
8
-
recombinant MnP: inactivation within 1 min, native MnP: inactivation within 15 min, A48C/A63C double mutant MnP: 1 h, 80% loss of activity
additional information
3
recombinant wild-type enzyme retains 26% activity after 24 h, while mutant A172W/K168V shows increased stability and retains 54% activity after 24 h, measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4.5
-
recombinant MnP, native MnP and A48C/A63C double mutant MnP are stable
4.5
-
in supernatant from pH 4.5 fermentations, 25% of activity of the recombinant enzyme is lost during the first 6 h, and another 25% decrease occurrs in the following 18 h. A much higher rate of loss of recombinant enzyme activity is observed in whole pH 4.5 culture, from which the yeast cells are not removed via centrifugation, than in either of the cell-free supernatants. The rate of loss of rMnP activity in pH 4.5 bioreactor cultures and culture supernatant is higher in samples obtained after 72 h of fermentation than in samples taken after 48 h
6
recombinant wild-type enzyme retains 38% activity after 24 h, while mutant A172W/K168V shows increased stability and retains 72% activity after 24 h, measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
6
-
native and A48C/A63C double mutant MnP: 1 h, less than 40% loss of activity
6
-
recombinant MnP produced by Pichia pastoris alphaMnP1-1 in pH 6 fed-batch fermentations is not stable in pure pH 6.0 buffers. In 0.01 M potassium phosphate buffer, activity of the recombinant enzyme decreases by 25% in 4 h. Half-lives of 6.7, 3.4, and 0.4 h for 0.01 M phosphate, 0.1 M phosphate, and 0.01 M sodium citrate buffers, respectively. In culture supernatants obtained from pH 6.0 bioreactor fermentations, the recombinant enzyme is stable for up to 6 h before a measurable loss of activity occurrs, and only 25% of the initial activity is lost after 24 h incubation
7
-
native MnP: 1 h, 80% loss of activity, A48C/A63C double mutant MnP: 1 h, 60% loss of activity
additional information
-
polyethylene glycol-modified enzyme shows greater stability to lower pH than native enzyme
additional information
-
recombinant MnP is more sensitive than native MnP as a result of lack of glycosylation
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
20 - 55
over 80% of maximal activity remains, recombinant enzyme, temperature stability profile, overview
35
37
-
recombinant MnP: 5 min, 50% loss of activity, A48C/A63C double mutant MnP: relatively stable
40
40 - 60
45
45 - 50
purified isozyme MGMnP2 is stable up to 45°C while the activity decreases around 50°C and disappears completely at 60°C after 1 h
49
-
wild-type MnP, MnP F190Y and MnP F190L: 330 s, 50% loss of activity, MnP F190I: 30 s, 50% loss of activity, MnP F190A: 5 s, complete loss of activity
50
50 - 70
-
the enzyme is rather unstable at 50, 60, and 70°C, resulting in half-lives of 660, 105, and 41 s, respectively
52
-
recombinant MnP: 20 s, 50% loss of activity, A48C/A63C double mutant MnP: 2 min, 50% loss of activity
55
60
65
additional information
100
-
complete inactivation after 5 min, 20% of original activity recovered after storage of heat-inactivated protein for 1 h at 0°C, no reactivation possible after boiling for 20 min
40 - 60
stable up to 40°C, while activity decreases above. MGMnP1 keeps half of its activity at 60°C after 1 h
40 - 60
stable up to 40°C, while activity decreases rapidly above for MGMnP3 after 1 h incubation, inactivation at 50°C
45
purified recombinant refolded His6-tagged enzyme retaining over 90% of its enzymatic activity below 45°C for 12 h
50
-
20% decrease of activity after 20 min, no further loss of activity after 60 min
55
-
more thermostable than MnP from Phanerochaete chrysosporium with half-lives 15-40fold longer at 55°C, Mn2+, Cd2+ and Zn2+ enhances thermostability
55
-
pH 4.5, 1.4 min, 50% loss of activity, both Mn2+ and Cd2+ protect MnP from thermal denaturation more efficiently than Ca2+ at pH 4.5, extending the half-life more than 2fold at 1 mM, combination of 0.5 mM Mn2+ and 0.5 mM Cd2+ extends the half-life more than 10fold
55
-
pH 4.5, 3 min, wild-type enzyme loses about 75% of the initial activity, 50% loss of activity after 3 min in presence of 1 mM ferric chloride. pH 4.5, 2 min, recombinant enzyme loses about 90% of the initial activity, about 45% loss of activity in presence of 1 mM ferric chloride
60
-
80% loss of activity after 10 min, complete inactivation after 40 min
additional information
-
polyethylene glycol-modified enzyme shows greater stability to higher temperatures than native enzyme
additional information
-
Mn2+ protects against thermal inactivation, probably due to active site protection
additional information
very sensitive to thermal treatment
additional information
-
susceptible to thermal inactivation due to the loss of calcium, calcium content after thermal treatment at 37°C for 15 min: 1.5 mol per mol of native MnP, 1 mol per mol of recombinant MnP and 1.3 mol per mol of A48C/A63C double mutant MnP, biphasic inactivation kinetics, recombinant MnP is more sensitive than native MnP as a result of the lack of glycosylation, calcium decreases the rate of thermal inactivation and reactivates MnP up to 50% of its original activity, while EGTA increases the rate of inactivation
additional information
isozyme MGMnP1 shows relatively high thermotolerance compared with the other isozymes
additional information
isozyme MGMnP1 shows relatively high thermotolerance compared with the other isozymes
additional information
isozyme MGMnP1 shows relatively high thermotolerance compared with the other isozymes
additional information
isozyme MGMnP3 shows relatively low thermotolerance compared with isozyme MGMnP1
additional information
isozyme MGMnP3 shows relatively low thermotolerance compared with isozyme MGMnP1
additional information
isozyme MGMnP3 shows relatively low thermotolerance compared with isozyme MGMnP1
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is more stable in carbon-limited cultures than in nitrogen-limited cultures
-
enzyme is very stable when the molar concentration of H2O2 is 10times of the concentration of the enzyme. When the H2O2 concentration is 250fold and 1000fold of the MnP concentration, the MnP activity decreases by 14% and 45%, respectively, in the first 15 min and remains the same thereafter. When the H2O2 concentration is 5000times of the enzyme concentration, the enzyme activity rapidly decreases in 30 min and then continues to decrease, but at a slower rate
-
enzyme retains more than 60% of the initial activity after exposure to 10 mM hydrogen peroxide for 5 min at 37°C
-
heat-inactivated protein, 100°C for 5 min, regains 80% of original activity by storage at 0°C for 1 h
-
no inactivation after 5 h in 50 mM Na-tartrate buffer, pH 4.5, with 2 mM nitrilotriacetate, 0.5 mM iodoacetamide or 2 mM PMSF
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable
4°C, pH 4.5, purified enzyme in 50 mM Na-tartrate buffer is stable for 1 week
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on blue agarose: isozyme H4 95% pure, followed by preparative isoelectric focusing: isozymes H3 and H5 pure
-
enzymes are extracted with 50 mM citrate-phosphate buffer at pH 4.0, 5.0 and 6.0 at 10°C and 25°C
-
extract is loaded onto a HiPREP26/10 desalting column followd by chromatography on a DEAE-Sepharose and a MonoQ HR5/5 column, finally the active fractions are applied to CIM QA Disks
-
from Ceriporiopsis subvermispora by gel filtration and chromatography on a Mono-Q column
-
MnP1 and MnP2
native enzyme 2.73fold from strain NITW715076, 1.6fold from strain NITW715076_1, and 2.85fold from strain NITW715076_2, by ammonium sulfate fractionation, dialysis, and anion exchange chromatography
-
native enzyme from cell free supernatant of bacterial culture, followed by ultrafiltration and gel filtration
-
partial purification
protoplasts from mycelia, native and recombinant extracellular enzyme from mycelia by filtration, addition of PEG, and anion exchange chromatography (elution with succinate), and ultrafiltration
purification of a protein complex containing MnP, laccase and beta-glucosidase activities
-
purification of MnPs from the mutants F190Y, F190L, F190I and F190A
-
purification of recombinant A48C/A63C double mutant MnP, expressed in Escherichia coli
-
purification of recombinant MnP, expressed in Escherichia coli
purification of recombinant MnP, expressed in Phanerochaete chrysosporium
-
purification of the mutant enzymes R177D, R177E, R177N and R177Q
-
purification scheme involves ultrafiltration, affinity chromatography on concanavalin-A Sepharose and gel filtration
-
recombinant refolded His6-tagged enzyme expressed from Escherichia coli strain Rosetta (DE3) by dialysis and nickel affinity chromatography
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3) in presence of 1 mM CaCl2 by nickel affinity chromatography, dialysis, followed by anion exchange chromatography, ultrafiltration, and gel filtration. Heme incorporation into MnP after purification, and removal of excess heme by high speed centrifugation at 50000 x g
ultrafiltration, Concanavalin-A Sepharose column chromatography and Superdex 75 gel filtration
-
using a Toyopearl Butyl-650M, a Toyopearl DEAE-650 and a Superdex 75 HR 10/30 column
-
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding MnP2 is cloned and expressed in Escherichia coli BL21(DE3)LysS
cDNA sequences of several MnP-encoding genes, including mnp1, mnp2 and mnp3
-
cloning and sequencing of the gene encoding MnP2, promoter region is analyzed, nucleotide sequence of the cDNA encoding MnP1, mnp1 is located on chromosome IV, mnp2 on chromosome VI and mnp3 on chromosome V
-
cloning of a full MnP cDNA from Trametes versicolor, and introducing an extra copy of the MnP gene under the control of a glyceraldehyde-3-phosphate dehydrogenase gene promoter from Aspergillus nidulans, into the genome of the wild type strain using a genetic transformation procedure. The gene is cloned and transferred into an expression vector (pBARGPE1) carrying a phosphinothricin resistance gene (bar) as a selectable marker to yield the expression vector, pBARTvMnP2. Transformants are generated through genetic transformation using pBARTvMnP2
codon-optimized gene mrmnp1, high level recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain X-33 with proper heme incorporation in to the resulting enzyme proteins
expression in Escherichia coli
expression in Pichia pastoris alphaMnP-1. Production of recombinant manganese peroxidase is highest at pH 6, with rMnP concentrations in the medium declining rapidly at pH less than 5.5, although cell growth rates are similar from pH 4-7
-
expression of A48C/A63C double mutant mnp gene in Escherichia coli XL-1 Blue
-
gene Il-MnP6, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain Rosetta (DE3) in inclusion bodies
gene MGmnp1, DNA and amino acid sequence determination and analysis, recombinant expression of extracellular isozyme MGmnp1 in Phlebia sp. strain MG-60
gene MGmnp2, DNA and amino acid sequence determination and analysis
gene MGmnp3, DNA and amino acid sequence determination and analysis, recombinant expression of extracellular isozyme MGmnp3 in Phlebia sp. strain MG-60
gene MnP10, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) as soluble protein. Coexpression with disulfide bond isomerase C (DsbC)
gene MnP12, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) as soluble protein. Coexpression with disulfide bond isomerase C (DsbC)
gene MnP2, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) as soluble protein. Coexpression with disulfide bond isomerase C (DsbC)
gene mnp3, recombinant expression of isozyme MnP3 as soluble extracellular protein in Pichia pastoris using alpha-factor as the signal peptide the recombinant enzyme has a MnP activity of 154.5 U/l
into the vector pET-22b, used for in vitro transcription and translation in a wheat germ extract system
isoenzymes H3, H4 and H5 are encoded by different genes and differentially regulated
-
isolation of the cDNAs encoding MnP isoenzymes: coding sequences of IZ-MnP1 cDNA with 1152 bp and IZ-MnP2 cDNA with 1155 bp in length, 2 copies of DNA encoding MnP isoenzymes exist in genomic DNA, 4 isoenzymes are generated as products of 2 genes by the difference of posttranslational modification
Deuteromycotina sp.
-
lemnp2 is cloned by 3'-RACE using cDNA that is synthesized from mycelial RNA
mutant genes F190Y, F190L, F190I and F190A are subcloned and expressed in Escherichia coli XL-1 Blue and DH5alphaF
-
three differentexpression vectors are constructed: pZBMNP contains the native Phanerochaete chrysosporium fungal secretion signal, palphaAMNP contains an alpha-factor secretion signal derived from Saccharomyces cerevisiae, and pZBIMNP has no secretion signal and is used for intracellular expression
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
copper increases the transcript levels of the manganese peroxidase genes mnp1 and mnp2
MnP is produced in media with sawdust
the optimum temperature for MnP production is 37°C. The amount of MnP registered at this temperature is 2.4 and 2.1times higher than that obtained in the treatments incubated at 30°C
-
the presence of laccase activity in the medium with sawdust probably depresses the expression of MnP
copper increases the transcript levels of the manganese peroxidase genes mnp1 and mnp2
-
copper increases the transcript levels of the manganese peroxidase genes mnp1 and mnp2
-
-
the presence of laccase activity in the medium with sawdust probably depresses the expression of MnP
-
the presence of laccase activity in the medium with sawdust probably depresses the expression of MnP
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged isozyme MnP6 from Escherichia coli strain Rosetta(DE3) inclusion bodies, refolding conditions: 1.5 M urea, 150 mM CaCl2, 0.025 mM hemin, 10% glycerol, 0.5 mM GSSG, 0.05 mM MnSO4, 20 mM KCl, and 50 mM Tris-HCl, pH 8.5
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
biotechnology
-
biotechnological applications require large amounts of low-cost enzymes, one of the appropriate approaches for this is to utilize the potential of lignocellulosic wastes, some of which may contain significant concentrations of soluble carbohydrates and inducers of enzyme synthesis, ensuring efficient production of ligninolytic enzymes
degradation
environmental protection
industry
nutrition
paper production
synthesis
additional information
biofuel production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
bioethanol production, the enzymes laccase and manganese peroxidase from Klebsiella pneumoniae are employed for ethanol production from rice and wheat bran biomass which shows 39.29% improved production compared to control, evaluation
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
Irpex lacteus CD2
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microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
Irpex lacteus F17
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microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
Cerrena unicolor BBP6
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microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
Ganoderma lucidum IBL-05
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microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
Irpex lacteus CCBAS238
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
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degradation
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
degradation
-
biomimmetic decrosslinking with enzyme or metal complex-catalyzed reactions will enable the development of new devulcanizing strategies for the safe disposal and recycling of waste vulcanized rubber products
degradation
-
various aspects of the biotechnological uses of these fungi have been studied regarding the nonspecific ligninolytic system of white-red fungi such as the degradation of industrial textile dye effluents and various xenobiotics
degradation
Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations
degradation
-
enzyme is able to detoxify aflatoxin B1. Maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
degradation
-
crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest
degradation
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
degradation
-
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
-
degradation
Phanerodontia chrysosporium BKM-F-1767
-
crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest
-
degradation
-
enzyme is able to detoxify aflatoxin B1. Maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
degradation
Bacillus velezensis Al-Dhabi 140
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
-
environmental protection
-
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
environmental protection
-
key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins
environmental protection
Deuteromycotina sp.
-
degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater
environmental protection
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
environmental protection
-
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
environmental protection
-
degradation of recalcitrant pollutants
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
environmental protection
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
environmental protection
-
polycyclic aromatic hydrocarbon degradation
-
environmental protection
-
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
-
environmental protection
Phanerodontia chrysosporium OGC101
-
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
-
environmental protection
Phanerodontia chrysosporium VKM F-1767
-
degradation of recalcitrant pollutants
-
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Irpex lacteus CD2
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Irpex lacteus F17
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Cerrena unicolor BBP6
-
as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation
-
environmental protection
Cerrena unicolor BBP6
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Ganoderma lucidum IBL-05
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Irpex lacteus CCBAS238
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Bacillus velezensis Al-Dhabi 140
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
-
environmental protection
Phanerodontia chrysosporium BKMF-1767
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
-
environmental protection
Phanerodontia chrysosporium CCTCC AF96007
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
-
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
nutrition
-
biotechnological applications related to animal feeding
-
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
paper production
mediated system of degradation is potentially valuable for pulp and paper industries
paper production
-
mediated system of degradation is potentially valuable for pulp and paper industries
paper production
-
manganese peroxidase produced by the white-rot fungus Bjerkandera sp. strain BOS55 is used for lignin oxidation and bleaching of eucalyptus oxygen delignified kraft pulp
paper production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
paper production
-
manganese peroxidase produced by the white-rot fungus Bjerkandera sp. strain BOS55 is used for lignin oxidation and bleaching of eucalyptus oxygen delignified kraft pulp
-
paper production
-
mediated system of degradation is potentially valuable for pulp and paper industries
-
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
-
synthesis
-
expression of active manganese peroxidase in an Escherichia coli cell-free protein synthesis system, and optimization of reaction conditions such as the concentrations of hemin, calcium ions, and disulfide bond isomerase. Cell-free synthesized manganese peroxidase purified using the hemagglutinin tag shows higher specific activity than the commercial wild-type enzyme
synthesis
-
the enzymes laccase and manganese peroxidase from Klebsiella pneumoniae are employed for ethanol production from rice and wheat bran biomass which shows 39.29% improved production compared to control, evaluation
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
the recombinant isotzyme MnP3 from Cerrena unicolor strain BBP6, rMnP3-BBP6, has promising biotechnological application potential in textile industries and polycyclic aromatic hydrocarbon bioremediation
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel,agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
Irpex lacteus CD2
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
Irpex lacteus F17
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
Cerrena unicolor BBP6
-
the recombinant isotzyme MnP3 from Cerrena unicolor strain BBP6, rMnP3-BBP6, has promising biotechnological application potential in textile industries and polycyclic aromatic hydrocarbon bioremediation
-
additional information
Cerrena unicolor BBP6
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
Ganoderma lucidum IBL-05
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
Irpex lacteus CCBAS238
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
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REF.
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TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
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Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
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1993
Trametes versicolor
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279
25-31
1990
Phlebia radiata
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Aitken, M.; Irvine, R.L.
Stability testing of ligninase and Mn-peroxidase from Phanerochaete chrysosporium
Biotechnol. Bioeng.
34
1251-1260
1989
Phanerodontia chrysosporium, Phanerodontia chrysosporium VKM F-1767
brenda
Johansson, T.; Nyman, P.O.
Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. I. Isolation of enzyme forms and characterization of physical and catalytic properties
Arch. Biochem. Biophys.
300
49-56
1993
Trametes versicolor
brenda
Glenn, J.K.; Akileswaran, L.; Gold, M.H.
Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium
Arch. Biochem. Biophys.
251
688-696
1986
Phanerodontia chrysosporium
brenda
Wariishi, H.; Akileswaran, L.; Gold, M.H.
Manganese peroxidase from the basidiomycete Phanerochaete chrysosporium: spectral characterization of the oxidized states and the catalytic cycle
Biochemistry
27
5365-5370
1988
Phanerodontia chrysosporium
brenda
Wariishi, H.; Dunford, H.B.; MacDonald, I.D.; Gold, M.H.
Manganese peroxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Transient state kinetics and reaction mechanism
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3335-3340
1989
Phanerodontia chrysosporium
brenda
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Characterization of extracellular peroxidases produced by acetate-buffered cultures of the lignin-degrading basidiomycete Phanerochaete chrysosporium
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69
221-224
1990
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Ruttimann, C.; Schwember, E.; Salas, L.; Cullen, D.; Vicuna, R.
Ligninolytic enzymes of the white rot basidiomycetes Phlebia brevispora and Ceriporiopsis subvermispora
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16
64-76
1992
Phlebia brevispora, Gelatoporia subvermispora
-
brenda
Banci, L.; Bertini, I.; Pease, E.A.; Tien, M.; Turano, P.
1H NMR investigation of manganese peroxidase from Phanerochaete chrysosporium. A comparison with other peroxidases
Biochemistry
31
10009-10017
1992
Phanerodontia chrysosporium
brenda
Wariishi, H.; Valli, K.; Gold, M.H.
Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators
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267
23688-23695
1992
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Tuor, U.; Wariishi, H.; Schoemaker, H.E.; Gold, M.H.
Oxidation of phenolic arylglycerol beta-aryl ether lignin model compounds by manganese peroxidase from Phanerochaete chrysosporium: oxidative cleavage of an alpha-carbonyl model compound
Biochemistry
31
4986-4995
1992
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Pease, E.A.; Tien, M.
Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium
J. Bacteriol.
174
3532-3540
1992
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Harris, R.Z.; Wariishi, H.; Gold, M.H.; Ortiz de Montellano, P.R.
The catalytic site of manganese peroxidase. Regiospecific addition of sodium azide and alkylhydrazines to the heme group
J. Biol. Chem.
266
8751-8758
1991
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Popp, J.L.; Kirk, T.K.
Oxidation of methoxybenzenes by manganese peroxidase and by Mn3+
Arch. Biochem. Biophys.
288
145-148
1991
Phanerodontia chrysosporium, Lentinula edodes
brenda
Aitken, M.; Irvine, R.L.
Characterization of reactions catalyzed by manganese peroxidase from Phanerochaete chrysosporium
Arch. Biochem. Biophys.
276
405-414
1990
Phanerodontia chrysosporium, Phanerodontia chrysosporium VKM F-1767
brenda
Datta, A.; Bettermann, A.; Kirk, T.K.
Identification of a specific manganese peroxidase among ligninolytic enzymes secreted by Phanerochaete chrysosporium during wood decay
Appl. Environ. Microbiol.
57
1453-1460
1991
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
brenda
Forrester, I.T.; Grabski, A.C.; Mishra, C.; Kelley, B.D.; Strickland, W.N.; Leatham, G.F.; Burgess, R.R.
Characteristics and N-terminal amino acid sequence of a manganese peroxidase purified from Lentinula edodes cultures grown on a commercial wood substrate
Appl. Microbiol. Biotechnol.
33
359-365
1990
Lentinula edodes
brenda
Wariishi, H.; Valli, K.; Renganathan, V.; Gold, M.H.
Thiol-mediated oxidation of nonphenolic lignin model compounds by manganese peroxidase of Phanerochaete chrysosporium
J. Biol. Chem.
264
14185-14191
1989
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Gold, M.H.; Glenn, J.K.
Manganese peroxidase from Phanerochaete chrysosporium
Methods Enzymol.
161
258-264
1988
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
-
brenda
Paszczynski, A.; Crawford, R.L.; Huynh, V.B.
Manganese peroxidase from Phanerochaete chrysosporium: Purification
Methods Enzymol.
161
264-270
1988
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F 1767
-
brenda
Dzedzyulya, E.I.; Becker, E.G.
Mn-peroxidase from Bjerkandera adusta 90-41. Purification and substrate specificity
Biochemistry
65
707-712
2000
Bjerkandera adusta, Bjerkandera adusta 90-41
brenda
Lankinen, V.P.; Bonnen, A.M.; Anton, L.H.; Wood, D.A.; Kalkkinen, N.; Hatakka, A.; Thurston, C.F.
Characteristics and N-terminal amino acid sequence of manganese peroxidase from solid substrate cultures of Agaricus bisporus
Appl. Microbiol. Biotechnol.
55
170-176
2001
Agaricus bisporus
brenda
Youngs, L.D.; Gold, M.H.
Heterologous expression of a thermostable manganese peroxidase from Dichomitus squalens in Phanerochaete chrysosporium
Arch. Biochem. Biophys.
385
348-356
2001
Dichomitus squalens
brenda
Makkar, R.S.; Tsuneda, A.; Tokuyasu, K.; Mori, Y
Lentinula edodes produces a multicomponent protein complex containing manganese (II)-dependent peroxidase, laccase and beta-glucosidase
FEMS Microbiol. Lett.
200
175-179
2001
Lentinula edodes
brenda
Gelpke, M.D.S.; Youngs, H.L.; Gold, M.H.
Role of arginine 177 in the MnII binding site of manganese peroxidase. Studies with R177D, R177E, R177N, and R177Q mutants
Eur. J. Biochem.
267
7038-7045
2000
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Giardina, P.; Palmieri, G.; Fontanella, B.; Rivieccio, V; Sannia, G.
Manganese peroxidase isoenzymes produced by Pleurotus ostreatus grown on wood sadwust
Arch. Biochem. Biophys.
376
171-179
2000
Pleurotus ostreatus
brenda
Wang, Y.; Vazquez-Duhalt, R.; Pickard, M.A.
Purification, characterization, and chemical modification of manganese peroxidase from Bjerkandera adusta UAMH 8258
Curr. Microbiol.
45
77-87
2002
Bjerkandera adusta, Pleurotus eryngii, Bjerkandera adusta UAMH 8258
brenda
Perie, F.H.; Sheng, D.; Gold, M.H.
Purification and characterization of two manganese peroxidase isoenzymes from the white-rot basidiomycete Dichomitus squalens
Biochim. Biophys. Acta
1297
139-148
1996
Dichomitus squalens, Dichomitus squalens CBS 432.34
brenda
Miyazaki, C.; Takahashi, H.
Engineering of the H2O2-binding pocket region of a recombinant manganese peroxidase to be resistant to H2O2
FEBS Lett.
509
111-114
2001
Phanerodontia chrysosporium (Q02567), Phanerodontia chrysosporium, Phanerodontia chrysosporium MnP2 (Q02567)
brenda
Sarkar, S.; Martinez, A.T.; Martinez, M.J.
Biochemical and molecular characterization of a manganese peroxidase isoenzyme from Pleurotus ostreatus
Biochim. Biophys. Acta
1339
23-30
1997
Phanerodontia chrysosporium, Pleurotus ostreatus, Pleurotus eryngii, Rigidoporus microporus, Lentinus tigrinus, Pleurotus ostreatus CBS 411.71
brenda
Ruttimann-Johnson, C.; Cullen, D.; Lamar, R.T.
Manganese peroxidases of the white rot fungus Phanerochaete sordida
Appl. Environ. Microbiol.
60
599-605
1994
Gelatoporia subvermispora, Phanerochaete sordida, Rigidoporus microporus, Lentinus tigrinus, Tomophagus colossus, Trametes versicolor
brenda
Matsubara, M.; Suzuki, J.; Deguchi, T.; Miura, M.; Kitaoka, Y.
Characterization of manganese peroxidases from the hyperlignolytic fungus IZU-154
Appl. Environ. Microbiol.
62
4066-4072
1996
Phanerodontia chrysosporium, Deuteromycotina sp., Phanerodontia chrysosporium ME446
brenda
Martinez, M.J.; Ruiz-Duenas, F.J.; Guillen, F.; Martinez, A.T.
Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii
Eur. J. Biochem.
237
424-432
1996
Pleurotus ostreatus, Pleurotus eryngii, Pleurotus pulmonarius, Lentinus sajor-caju, Pleurotus ostreatus CBS 411.71
brenda
Nuske, J.; Scheibner, K.; Dornberger, U.; Ullrich, R.; Hofrichter, M.
Large scale production of manganese-peroxidase using agaric white-rot fungi
Enzyme Microb. Technol.
30
556-561
2002
Hypholoma frowardii, Clitocybula dusenii, Clitocybula dusenii b11
-
brenda
Steffen, K.T.; Hofrichter, M.; Hatakka, A.
Purification and characterization of a manganese peroxidases from the litter-decomposing basidiomycetes Agrocybe praecox and Stropharia coronilla
Enzyme Microb. Technol.
30
550-555
2002
Agrocybe praecox, Stropharia coronilla, Agrocybe praecox TM 70.84, Stropharia coronilla TM 47-1
-
brenda
Palma, C.; Martinez, A.T.; Lema, J.M.; Martinez, M.J.
Different fungal manganese-oxidizing peroxidases: A comparison between Bjerkandera sp. and Phanerochaete chrysosporium
J. Biotechnol.
77
235-245
2000
Phanerodontia chrysosporium, Bjerkandera adusta, Pleurotus ostreatus, Pleurotus eryngii, Pleurotus pulmonarius, Bjerkandera sp., Bjerkandera sp. BOS55, Phanerodontia chrysosporium VKM F-1767
brenda
Hofrichter, M.
Review: Lignin conversion by manganese peroxidase (MnP)
Enzyme Microb. Technol.
30
454-466
2002
Abortiporus biennis, Agaricus bisporus, Agrocybe dura, Agrocybe praecox, Armillaria mellea, Armillaria ostoyae, Auricularia sp., Auricularia sp. M37, Bjerkandera adusta, Bjerkandera sp., Clitocybula dusenii, Collybiopsis quercophila, Coriolopsis trogii, Coriolus pruinosum, Cyathus stercoreus, Deuteromycotina sp., Dichomitus squalens, Ganoderma lucidum, Gelatoporia subvermispora, Gymnopus dryophilus, Heterobasidion annosum, Hypholoma fasciculare, Hypholoma frowardii, Irpex flavus, Irpex lacteus, Kuehneromyces mutabilis, Lentinula edodes, Lentinus sajor-caju, Lentinus tigrinus, Meripilus vitreus, Merulius sp., Merulius sp. M15, Panaeolus sphinctrinus, Phaeolus schweinitzii, Phallus impudicus, Phanerochaete laevis, Phanerochaete sordida, Phanerodontia chrysosporium, Phellinus trivialis, Phlebia brevispora, Phlebia radiata, Phlebia tremellosa, Phlebiopsis flavidoalba, Pleurotus eryngii, Pleurotus ostreatus, Pleurotus pulmonarius, Psilocybe cubensis, Rigidoporus microporus, Stropharia aeruginosa, Stropharia coronilla, Stropharia rugosoannulata, Trametes gibbosa, Trametes hirsuta, Trametes polyzona, Trametes versicolor, Truncospora tephropora
-
brenda
Kishi, K.; Hildebrand, D.P.; Kusters-van Someren, M.; Gettemy, J.; Mauk, A.G.; Gold, M.H.
Site-directed mutations at phenylalanine-190 of manganese peroxidase: Effects on stability, function, and coordination
Biochemistry
36
4268-4277
1997
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Reading, N.S.; Aust, S.D.
Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability
Biotechnol. Prog.
16
326-333
2000
Phanerodontia chrysosporium
brenda
Youngs, H.L.; Sundaramoorthy, M; Gold, M.H.
Effects of cadmium on manganese peroxidase. Competitive inhibition of MnII oxidation and thermal stabilization of the enzyme
Eur. J. Biochem.
267
1761-1769
2000
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
Steffen, K.T.; Hatakka, A.; Hofrichter, M.
Degradation of benzo[a]pyrene by the litter-decomposing basidiomycete Stropharia coronilla: role of manganese peroxidase
Appl. Environ. Microbiol.
69
3957-3964
2003
Stropharia coronilla
brenda
Kamitsuji, H.; Honda, Y.; Watanabe, T.; Kuwahara, M.
Production and induction of manganese peroxidase isozymes in a white-rot fungus Pleurotus ostreatus
Appl. Microbiol. Biotechnol.
65
287-294
2004
Pleurotus ostreatus
brenda
Kamitsuji, H.; Watanabe, T.; Honda, Y.; Kuwahara, M.
Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators
Biochem. J.
386
387-393
2005
Pleurotus ostreatus
brenda
Sundaramoorthy, M.; Youngs, H.L.; Gold, M.H.; Poulos, T.L.
High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes
Biochemistry
44
6463-6470
2005
Phanerodontia chrysosporium (Q02567)
brenda
Lisov, A.V.; Leontievsky, A.A.; Golovleva, L.A.
Hybrid Mn-peroxidase from the ligninolytic fungus Panus tigrinus 8/18. Isolation, substrate specificity, and catalytic cycle
Biochemistry
68
1027-1035
2003
Lentinus tigrinus, Lentinus tigrinus 8/18
brenda
Deguchi, T.; Matsubara, M.; Nishida, T.
NADH oxidation by manganese peroxidase with or without alpha-hydroxy acid
Biosci. Biotechnol. Biochem.
66
717-721
2002
Pleurotus ostreatus
brenda
Gu, L.; Lajoie, C.; Kelly, C.
Expression of a Phanerochaete chrysosporium manganese peroxidase gene in the yeast Pichia pastoris
Biotechnol. Prog.
19
1403-1409
2003
Phanerodontia chrysosporium
brenda
Bermek, H.; Yazici, H.; Ozturk, H.; Tamerler, C.; Jung, H.; Li, K.; Brown, K.M.; Ding, H.; Xu, F.
Purification and characterization of manganese peroxidase from wood-degrading fungus Trichophyton rubrum LSK-27
Enzyme Microb. Technol.
35
87-92
2004
Trichophyton rubrum, Trichophyton rubrum LSK-27
-
brenda
Hoshino, F.; Kajino, T.; Sugiyama, H.; Asami, O.; Takahashi, H.
Thermally stable and hydrogen peroxide tolerant manganese peroxidase (MnP) from Lenzites betulinus
FEBS Lett.
530
249-252
2002
Lenzites betulinus
brenda
Christian, V.V.; Shrivastava, R.; Novotny, C.; Vyas, B.R.
Decolorization of sulfonphthalein dyes by manganese peroxidase activity of the white-rot fungus Phanerochaete chrysosporium
FEMS Microbiol. Rev.
48
771-774
2003
Phanerodontia chrysosporium
brenda
Podgornik, H.; Podgornik, A.
Separation of manganese peroxidase isoenzymes on strong anion-exchange monolithic column using pH-salt gradient
J. Chromatogr. B
799
343-347
2004
Phanerodontia chrysosporium, Phanerodontia chrysosporium MZKI B-223
brenda
Urek, R.O.; Pazarlioglu, N.K.
Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium
Proc. Biochem.
39
2061-2068
2004
Phanerodontia chrysosporium
-
brenda
de la Rubia, T.; Linares, A.; Perez, J.; Munoz-Dorado, J.; Romera, J.; Martinez, J.
Characterization of manganese-dependent peroxidase isoenzymes from the ligninolytic fungus Phanerochaete flavido-alba
Res. Microbiol.
153
547-554
2002
Phlebiopsis flavidoalba
brenda
Jiang, F.; Kongsaeree, P.; Schilke, K.; Lajoie, C.; Kelly, C.
Effects of pH and temperature on recombinant manganese peroxidase production and stability
Appl. Biochem. Biotechnol.
146
15-27
2008
Phanerodontia chrysosporium
brenda
Jiang, F.; Kongsaeree, P.; Charron, R.; Lajoie, C.; Xu, H.; Scott, G.; Kelly, C.
Production and separation of manganese peroxidase from heme amended yeast cultures
Biotechnol. Bioeng.
99
540-549
2008
Phanerodontia chrysosporium
brenda
Kwon, H.; Chung, E.; Oh, J.; Lee, C.; Ahn, I.
Optimized production of lignolytic manganese peroxidase in immobilized cultures of Phanerochaete chrysosporium
Biotechnol. Bioprocess Eng.
13
108-114
2008
Phanerodontia chrysosporium
-
brenda
Hwang, S.; Lee, C.H.; Ahn, I.S.; Park, K.
Manganese peroxidase-catalyzed oxidative degradation of vanillylacetone
Chemosphere
72
572-577
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Cheng, X.; Jia, R.; Li, P.; Tu, S.; Zhu, Q.; Tang, W.; Li, X.
Purification of a new manganese peroxidase of the white-rot fungus Schizophyllum sp. F17, and decolorization of azo dyes by the enzyme
Enzyme Microb. Technol.
41
258-264
2007
Schizophyllum sp., Schizophyllum sp. F17
-
brenda
Songulashvili, G.; Elisashvili, V.; Wasser, S.P.; Nevo, E.; Hadar, Y.
Basidiomycetes laccase and manganese peroxidase activity in submerged fermentation of food industry wastes
Enzyme Microb. Technol.
41
57-61
2007
Ganoderma adspersum, Ganoderma lucidum, Phlebia radiata, Phellinus robustus, Trametes versicolor, Trametes zonata, Omphalotus olearius, Trametes maxima, Fomes fomentarius, Coriolopsis trogii, Ganoderma adspersum 845, Ganoderma lucidum 447, Phellinus robustus 250, Omphalotus olearius 174, Phlebia radiata 511, Trametes maxima 681, Coriolopsis trogii 146, Trametes zonata 540
-
brenda
Feijoo, G.; Moreira, M.T.; Alvarez, P.; Lu-Chau, T.A.; Lema, J.M.
Evaluation of the enzyme manganese peroxidase in an industrial sequence for the lignin oxidation and bleaching of eucalyptus kraft pulp
J. Appl. Polym. Sci.
109
1319-1327
2008
Bjerkandera sp., Bjerkandera sp. BOS55
-
brenda
Yeo, S.; Park, N.; Song, H.; Choi, H.T.
Generation of a transformant showing higher manganese peroxidase (Mnp) activity by overexpression of Mnp gene in Trametes versicolor
J. Microbiol.
45
213-218
2007
Trametes versicolor (Q6KB19), Trametes versicolor
brenda
Hilden, K.S.; Bortfeldt, R.; Hofrichter, M.; Hatakka, A.; Lundell, T.K.
Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
Microbiology
154
2371-2379
2008
Phlebia sp. b19 (B2BF37), Phlebia sp. b19 (B2BF38)
brenda
Catal, T.; Liu, H.; Bermek, H.
Selenium induces manganese-dependent peroxidase production by the white-rot fungus Bjerkandera adusta (Willdenow) P. Karsten
Biol. Trace Elem. Res.
123
211-217
2008
Bjerkandera adusta
brenda
Silva, E.; Martins, S.; Milagres, A.
Extraction of manganese peroxidase produced by Lentinula edodes
Biores. Technol.
99
2471-2475
2008
Lentinula edodes
brenda
Sato, S.; Ohashi, Y.; Kojima, M.; Watanabe, T.; Honda, Y.; Watanabe, T.
Degradation of sulfide linkages between isoprenes by lipid peroxidation catalyzed by manganese peroxidase
Chemosphere
77
798-804
2009
Gelatoporia subvermispora
brenda
Erdem, E.; Ucar, M.; Kaymaz, Y.; Pazarlioglu, N.
New and different lignocellulosic materials from Turkey for laccase and manganese peroxidase production by Trametes versicolor
Eng. Life Sci.
9
60-65
2009
Trametes versicolor
-
brenda
Susla, M.; Novotny, C.; Erbanova, P.; Svobodova, K.
Implication of Dichomitus squalens manganese-dependent peroxidase in dye decolorization and cooperation of the enzyme with laccase
Folia Microbiol. (Praha)
53
479-485
2008
Dichomitus squalens
brenda
Alvarez, J.M.; Canessa, P.; Mancilla, R.A.; Polanco, R.; Santibanez, P.A.; Vicuna, R.
Expression of genes encoding laccase and manganese-dependent peroxidase in the fungus Ceriporiopsis subvermispora is mediated by an ACE1-like copper-fist transcription factor
Fungal Genet. Biol.
46
104-111
2009
Gelatoporia subvermispora, Gelatoporia subvermispora FP-105752
brenda
Kenkebashvili, N.; Elisashvili, V.; Hadar, Y.
Effect of nutrient medium composition on laccase and manganese peroxidase activity in medicinal mushrooms
Int. J. Med. Mushr.
11
191-198
2009
Basidiomycota, Pallidohirschioporus biformis, Trametes ochracea, Trametes ochracea 1215, Pallidohirschioporus biformis 117
-
brenda
Petruccioli, M.; Frasconi, M.; Quaratino, D.; Covino, S.; Favero, G.; Mazzei, F.; Federici, F.; DAnnibale, A.
Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79
J. Biol. Inorg. Chem.
14
1153-1163
2009
Lentinus tigrinus, Lentinus tigrinus 577.79, Lentinus tigrinus CBS 577.79
brenda
Zhang, X.; Wang, Y.; Wang, L.; Chen, G.; Liu, W.; Gao, P.
Site-directed mutagenesis of manganese peroxidase from Phanerochaete chrysosporium in an in vitro expression system
J. Biotechnol.
139
176-178
2009
Phanerodontia chrysosporium (Q02567), Phanerodontia chrysosporium
brenda
Elisashvili, V.; Kachlishvili, E.
Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes
J. Biotechnol.
144
37-42
2009
Basidiomycota, Bjerkandera adusta, Cerrena unicolor, Fomes fomentarius, Pallidohirschioporus biformis, Trametes maxima, Trametes ochracea, Trametes pubescens, Trametes versicolor
brenda
Sakamoto, Y.; Nakade, K.; Nagai, M.; Uchimiya, H.; Sato, T.
Cloning of Lentinula edodes lemnp2, a manganese peroxidase that is secreted abundantly in sawdust medium
Mycoscience
50
116-122
2009
Lentinula edodes (B5U990), Lentinula edodes SR-1 (B5U990)
-
brenda
Erden, E.; Cigdem Ucar, M.; Gezer, T.; Pazarlioglu, N.
Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue
Braz. J. Microbiol.
40
346-353
2009
Abortiporus biennis, Abortiporus biennis ECN 100601, Agaricus sp., Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Collybia nuda, Collybia nuda ECN 100605, Coprinopsis atramentaria, Cortinarius sp. 1, Cortinarius sp. 2, Cortinarius sp. 2 ECN 100602, Cyclocybe aegerita, Ganoderma carnosum, Ganoderma carnosum ECN 100603, Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lactarius deliciosus ECN 100604, Lepiota naucina, Lepiota sp. 1, Lepiota sp. 2, Leptonia lazunila, Lyophyllum subglobisporium, Lyophyllum subglobisporium ECN 100606, Parasola plicatilis, Pleurotus ostreatus, Pleurotus ostreatus ECN 100607, Ramaria stricta, Ramaria stricta ECN 100608, Rhizopogon luteolus, Russula rosacea, Russula sp., Trametes hirsuta, Trametes versicolor, Trametes versicolor ECN 100609, Volvariella sp.
brenda
Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
J. Exp. Bot.
60
441-452
2009
Phanerodontia chrysosporium (Q02567)
brenda
Hu, M.; Zhang, W.; Wu, Y.; Gao, P.; Lu, X.
Characteristics and function of a low-molecular-weight compound with reductive activity from Phanerochaete chrysosporium in lignin biodegradation
Biores. Technol.
100
2077-2081
2009
Phanerodontia chrysosporium
brenda
Lupo, S.; Perez, A.; Martinez, S.; Simeto, S.; Rivas, F.; Bettucci, L.
In vitro characterization of Inocutis jamaicensis and experimental inoculation of Eucalyptus globulus standing trees
Forest Pathol.
39
293-303
2009
Inocutis jamaicensis, Inocutis jamaicensis MVHC11379
-
brenda
Vassilev, N.; Requena, A.; Nieto, L.; Nikolaeva, I.; Vassileva, M.
Production of manganese peroxidase by Phanerochaete chrisosporium grown on medium containing agro-wastes/rock phosphate and biocontrol properties of the final product
Ind. Crops Prod.
30
28-32
2009
Phanerodontia chrysosporium
-
brenda
Wang, J.; Ogata, M.; Hirai, H.; Kawagishi, H.
Detoxification of aflatoxin B1 by manganese peroxidase from the white-rot fungus Phanerochaete sordida YK-624
FEMS Microbiol. Lett.
314
164-169
2011
Phanerochaete sordida, Phanerochaete sordida YK-624
brenda
Yadav, P.; Singh, V.K.; Yadav, M.; Singh, S.K.; Yadava, S.; Yadav, K.D.
Purification and characterization of Mn-peroxidase from Musa paradisiaca (banana) stem juice
Indian J. Biochem. Biophys.
49
42-48
2012
Musa x paradisiaca
brenda
Asgher, M.; Irshad, M.; Iqbal, H.
Purification and characterization of novel manganese peroxidase from Schizophyllum commune IBL-06
Int. J. Agric. Biol.
15
749-754
2013
Schizophyllum commune, Schizophyllum commune IBL-06
-
brenda
Fernandez-Fueyo, E.; Ruiz-Duenas, F.J.; Martinez, A.T.
Engineering a fungal peroxidase that degrades lignin at very acidic pH
Biotechnol. Biofuels
7
114
2014
Gelatoporia subvermispora (M2REM6), Gelatoporia subvermispora B (M2REM6)
brenda
Ninomiya, R.; Zhu, B.; Kojima, T.; Iwasaki, Y.; Nakano, H.
Role of disulfide bond isomerase DsbC, calcium ions, and hemin in cell-free protein synthesis of active manganese peroxidase isolated from Phanerochaete chrysosporium
J. Biosci. Bioeng.
117
652-657
2014
Phanerodontia chrysosporium
brenda
Wen, X.; Jia, Y.; Li, J.
Enzymatic degradation of tetracycline and oxytetracycline by crude manganese peroxidase prepared from Phanerochaete chrysosporium
J. Hazard. Mater.
177
924-928
2010
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Thamvithayakorn, P.; Phosri, C.; Pisutpaisal, N.; Krajangsang, S.; Whalley, A.J.S.; Suwannasai, N.
Utilization of oil palm decanter cake for valuable laccase and manganese peroxidase enzyme production from a novel white-rot fungus, Pseudolagarobasidium sp. PP17-33
3 Biotech
9
417
2019
Pseudolagarobasidium sp. PP17-33
brenda
Duan, Z.; Shen, R.; Liu, B.; Yao, M.; Jia, R.
Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete
AMB Express
8
119
2018
Irpex lacteus (A0A2P1C6N7), Irpex lacteus, Irpex lacteus F17 (A0A2P1C6N7)
brenda
Zhang, H.; Zhang, X.; Geng, A.
Expression of a novel manganese peroxidase from Cerrena unicolor BBP6 in Pichia pastoris and its application in dye decolorization and PAH degradation
Biochem. Eng. J.
153
107402
2020
Cerrena unicolor (A0A7D5FUQ6), Cerrena unicolor BBP6 (A0A7D5FUQ6)
-
brenda
Bronikowski, A.; Koschorreck, K.; Urlacher, V.B.
Redesign of a new manganese peroxidase highly expressed in Pichia pastoris towards a lignin-degrading versatile peroxidase
ChemBioChem
19
2481-2489
2018
Moniliophthora roreri (V2XS39), Moniliophthora roreri, Moniliophthora roreri MCA 2997 (V2XS39)
brenda
Al-Dhabi, N.A.; Esmail, G.A.; Valan Arasu, M.
Effective degradation of tetracycline by manganese peroxidase producing Bacillus velezensis strain Al-Dhabi 140 from Saudi Arabia using fibrous-bed reactor
Chemosphere
268
128726
2021
Bacillus velezensis, Bacillus velezensis Al-Dhabi 140
brenda
Li, L.; Liu, B.; Yang, J.; Zhang, Q.; He, C.; Jia, R.
Catalytic properties of a short manganese peroxidase from Irpex lacteus F17 and the role of Glu166 in the Mn2+-independent activity
Int. J. Biol. Macromol.
136
859-869
2019
Irpex lacteus (S4W784), Irpex lacteus, Irpex lacteus CCTCC AF2014020 (S4W784), Irpex lacteus F17 (S4W784)
brenda
Ding, Y.; Cui, K.; Guo, Z.; Cui, M.; Chen, Y.
Manganese peroxidase mediated oxidation of sulfamethoxazole integrating the computational analysis to reveal the reaction kinetics, mechanistic insights, and oxidation pathway
J. Hazard. Mater.
415
125719
2021
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKMF-1767, Phanerodontia chrysosporium CCTCC AF96007
brenda
Kamei, I.; Tomitaka, N.; Motoda, T.; Yamasaki, Y.
Isozyme selective homologous expression of recombinant manganese peroxidase of salt-tolerant white-rot fungus Phlebia sp. MG-60, and its salt-tolerance and thermostability
J. Microbiol. Biotechnol.
32
248-255
2021
Phlebia sp. MG60 (B1B554), Phlebia sp. MG60 (A0A068PC52), Phlebia sp. MG60 (A0A068PCH3)
brenda
Zhang, H.; Zhang, J.; Zhang, X.; Geng, A.
Purification and characterization of a novel manganese peroxidase from white-rot fungus Cerrena unicolor BBP6 and its application in dye decolorization and denim bleaching
Process Biochem.
66
222-229
2018
Cerrena unicolor (A0A7D5FUQ6), Cerrena unicolor BBP6 (A0A7D5FUQ6)
-
brenda
Lin, M.I.; Nagata, T.; Katahira, M.
High yield production of fungal manganese peroxidases by E. coli through soluble expression, and examination of the activities
Protein Expr. Purif.
145
45-52
2018
Gelatoporia subvermispora (A0A2I7M8U2), Gelatoporia subvermispora (O42736), Gelatoporia subvermispora (A0A2I7M8W6), Gelatoporia subvermispora B (A0A2I7M8U2), Gelatoporia subvermispora B (O42736), Gelatoporia subvermispora B (A0A2I7M8W6)
brenda
Gaur, N.; Narasimhulu, K.; Pydisetty, Y.
Biochemical and kinetic characterization of laccase and manganese peroxidase from novel Klebsiella pneumoniae strains and their application in bioethanol production
RSC Adv.
8
15044-15055
2018
Klebsiella pneumoniae
-
brenda
Chowdhary, P.; Shukla, G.; Raj, G.; Ferreira, L.; Bharagava, R.
Microbial manganese peroxidase a ligninolytic enzyme and its ample opportunities in research
SN Appl. Sci.
1
45
2019
Acinetobacter baumannii, Agrocybe praecox (G4WG41), Alcaligenes faecalis, Bacillus cereus, Bacillus subtilis, Cerrena unicolor (A0A7D5FUQ6), Cerrena unicolor BBP6 (A0A7D5FUQ6), Ganoderma lucidum, Ganoderma lucidum (A0A1I9KRQ0), Ganoderma lucidum IBL-05, Gelatoporia subvermispora, Irpex lacteus, Irpex lacteus (S4W784), Irpex lacteus (A0A1S6KK55), Irpex lacteus CCBAS238, Irpex lacteus CD2 (A0A1S6KK55), Irpex lacteus F17 (S4W784), Phanerodontia chrysosporium (Q02567), Phlebia radiata (Q70LM3), Schizophyllum commune, Schizophyllum commune IBL-06, Trametes sp. 48424, Trametes villosa
-
brenda
Kumar, V.; Chandra, R.
Characterisation of manganese peroxidase and laccase producing bacteria capable for degradation of sucrose glutamic acid-Maillard reaction products at different nutritional and environmental conditions
World J. Microbiol. Biotechnol.
34
32
2018
Klebsiella aerogenes, Enterobacter cloacae, Klebsiella pneumoniae, Salmonella enterica
brenda
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