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Information on EC 1.11.1.16 - versatile peroxidase
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1.11.1.16 versatile peroxidaseIUBMB Comments
A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4].
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Word Map
- 1.11.1.16
- lignin
- pleurotus
- peroxidases
-
ligninolytic
- eryngii
- laccase
-
white-rot
- bjerkandera
- ostreatus
-
veratryl
- adusta
- chrysosporium
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phanerochaete
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lignin-degrading
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non-phenolic
- 2,6-dimethoxyphenol
-
delignification
-
aryl-alcohols
- degradation
- synthesis
- industry
- analysis
- paper production
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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Synonyms
myoglobin, versatile peroxidase, mb peroxidase, versatile peroxidase mnp2, metmb peroxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mb peroxidase
metMb peroxidase
myoglobin
VP1
Vpl2
VPS1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
NMR study of enzyme both in resting state and cyanide-inhibited form. Analysis of interaction with Mn2+
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1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
study of reaction of H2O2 with the enzyme in the absence of substrate suggests an amino acid radical in moderate distance from ferryl heme. A tryptophan radical is formed during the catalytic mechanism
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1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
the radical intermediate in the reaction of enzyme with H2O2 is a tryptophan neutral radical at W164
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(1)
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2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O
(2)
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2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O
at the ferric resting state, heme peroxidases are first activated by a single molecule of H2O2 to yield an oxidized catalytic intermediate called compound I (oxoferryl IV porphyrin p-cation radical), releasing one molecule of water as the only by-product. The enzyme then catalyzes two consecutive one-electron oxidations of two reducing substrates, regenerating the ground reduced state through a second catalytic intermediate called compound II (oxoferryl) and with the concomitant production of a second molecule of water. The main limiting step within this catalytic cycle is the low conversion rate from compound II to the ground state, which allows the former to accumulate and react with a new molecule of H2O2, either in the presence (with an excess of H2O2) or absence (at catalytic concentrations of H2O2) of the reducing substrate
2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O
the versatile peroxidase catalytic mechanism is similar to classic peroxidases, in which substrate oxidation is carried out by a two-electron multistep reaction at the expense of hydrogen peroxide. Versatile peroxidases oxidize Mn2+ (as MnP), degrade the lignin model dimer veratryl glycerol-guaiacylether to yield veratraldehyde, and oxidize veratryl alcohol and dimethoxybenzene to veratraldehyde and p-benzoquinone, respectively
2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O
the versatile peroxidase catalytic mechanism is similar to classic peroxidases, in which substrate oxidation is carried out by a two-electron multistep reaction at the expense of hydrogen peroxide. Versatile peroxidases oxidize Mn2+ (as MnP), degrade the lignin model dimer veratryl glycerol-guaiacylether to yield veratraldehyde, and oxidize veratryl alcohol and dimethoxybenzene to veratraldehyde and p-benzoquinone, respectively
Bjerkandera adusta UAMH8258
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
reactive-black-5:hydrogen-peroxide oxidoreductase
A hemoprotein. This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13, manganese peroxidase and EC 1.11.1.14, lignin peroxidase. Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates [2,4].
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CAS REGISTRY NUMBER
COMMENTARY
114995-15-2
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42613-30-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,4-dimethoxybenzene + H2O2
1,4-benzoquinone + formaldehyde + H2O
-
Mn2+-independent activity
-
-
?
1-methylanthracene + H2O2
1-methylanthraquinone + H2O
-
at 43% of the rate with 9-methylanthracene
-
-
?
1-phenyl-1,2-ethandiol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenyl-1-propanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenyl-2-propanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenylethanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
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-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
-
-
-
?
2,7-diaminofluorene + H2O2
? + H2O
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during oxidation of 2,7-diaminofluorene, both with and without Mn2+, biphasic kinetics with apparent saturation in both micromolar and millimolar ranges are obtained
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-
?
2-chloro-1,4-dimethoxybenzene + H2O2
2-chloro-1,4-benzoquinone + H2O
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Mn2+-independent activity
-
-
?
2-methylanthracene + H2O2
2-methylanthraquinone + H2O
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at 24% of the rate with 9-methylanthracene
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-
?
3-methyl-2-benzothiazolinone hydrazone + H2O2
? + H2O
-
enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+
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-
?
anthracene + H2O2
anthraquinone + H2O
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at 4.8% of the rate with 9-methylanthracene
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-
?
Azure B + 2 H+ + H2O2
oxidized Azure B + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
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?
bovine pancreatic RNase
oxidized bovine pancreatic RNase
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no redox mediators involved
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-
?
carbazole + H2O2
? + H2O
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at 4.8% of the rate with 9-methylanthracene
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?
guaiacylglycerol-beta-guaiacyl ether + H2O2
glycerol + guaiacol + 2 H2O
GGE, substrate of mutant enzyme N246A
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?
indigo carmine + 2 H+ + H2O2
oxidized indigo carmine + 2 H2O
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dye decolorization
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?
manganese(II)-substituted polyoxometalate + H2O2
manganese(III)-substituted polyoxometalate + H2O2
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-
-
-
?
methyl green + 2 H+ + H2O2
oxidized methyl green + 2 H2O
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dye decolorization
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-
?
Mn2+ + H2O2 + remazol black-5
?
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incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
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-
?
Mn2+ + H2O2 + remazol blue-19
?
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incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
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-
?
Mn2+ + H2O2 + remazol brilliant violet
?
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incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
?
Mn2+ + H2O2 + remazol orange-16
?
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incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
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?
Mn2+ + H2O2 + rose bengal
?
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incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
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?
p-dimethoxybenzene + H2O2
benzoquinone + H2O
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catalyzed by isoforms PS3, PS1
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?
phenol red + H2O2
oxidized phenol red + H2O
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Mn2+-dependent activity
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?
Remazol brilliant blue R + 2 H+ + H2O2
oxidized Remazol brilliant blue R + 2 H2O
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dye decolorization
-
-
?
remazol brilliant blue R + H2O2
? + 2 H2O
transformation of the bulky substrate remazol brilliant blue R (RBBR), is monitored at its maximum visible absorbance wavelength of 590 nm
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-
?
remazol brilliant blue R + H2O2
oxidized remazol brilliant blue R + 2 H2O
substrate of N246A mutant enzyme
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
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Mn2+-independent activity
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?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
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Mn2+-independent activity
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?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
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Mn2+-dependent and independent activity
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?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
oxidation of Mn2+ to Mn3+ (manganese peroxidase activity) is measured as the H2O2-dependent formation of the complex malonate-Mn3+
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?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
activity of EC 1.11.1.13
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?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
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-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
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Mn2+-independent activity
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
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?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
substrate 2,6-dimethoxyphenol (DMP) is transformed at the distal site of heme prosthetic group (lignin peroxidase activity)
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-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Lentinus squarrosulus TAMI004
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-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
lignin + H2O2
? + H2O
-
lignin fraction from straw pulpin, versatile peroxidase reacts with soluble lignin fragments in the absence of added mediators, most probably causing extensive polymerisation of high and intermediate fractions of lignin, and an increase of the small-molecular-mass lignin fraction
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-
?
lignin + H2O2
? + H2O
-
substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin
-
-
?
lignin + H2O2
? + H2O
-
substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
the Mn2+-binding site in versatile peroxidase is formed by the side-chains of Glu36, Glu40, and Asp175 located in front of the internal (i.e. more distant from the main haem access-channel) propionate of haem, and connected to the solvent by a narrow access-channel that presents a variable geometry during catalysis
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-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Lentinus squarrosulus 12292 ITS
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Lentinus squarrosulus TAMI004
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
dye decolorization
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
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dye decolorization
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
-
-
?
Reactive Black 5 + H2O2
?
versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
catalyzed by isoform PS1
-
-
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
substrate of N246A mutant enzyme
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Mn2+-independent activity
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
catalyzed by isoforms PS2, PS1
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Mn2+-independent activity
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
a solvent-exposed tryptophan is the catalytically-active residue in veratryl alcohol oxidation, initiating an electron transfer pathway to haem
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
additional information
?
-
-
enzyme is able to decolorize 27 out of 41 industrial dyes tested
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-
?
additional information
?
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-
manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity
-
-
?
additional information
?
-
ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
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-
additional information
?
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ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
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-
additional information
?
-
the oxidation of 2,6-dimethylphenol, Mn2+ and remazol brilliant blue R (RBBR) of the three different substrates occurs at different active sites of the enzyme molecule. Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a long-range electron t (LRET) pathway. The catalytic rate of the LRET mediated transformation shows a good correlation with the ionization energy of the additional amino acid on the protein surface
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-
additional information
?
-
-
the oxidation of 2,6-dimethylphenol, Mn2+ and remazol brilliant blue R (RBBR) of the three different substrates occurs at different active sites of the enzyme molecule. Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a long-range electron t (LRET) pathway. The catalytic rate of the LRET mediated transformation shows a good correlation with the ionization energy of the additional amino acid on the protein surface
-
-
-
additional information
?
-
versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower
-
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-
additional information
?
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versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower
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-
-
additional information
?
-
Bjerkandera adusta UAMH8258
ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
-
-
-
additional information
?
-
Bjerkandera adusta UAMH8258
versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower
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-
additional information
?
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oxidation of substrates may occur in two ways, either directly by the enzyme or by diffusible chelated Mn3+ as an oxidizing agent
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?
additional information
?
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enzyme is able to oxidize efficiently Mn2+ and phenolic and nonphenolic compounds in absence of this ion
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?
additional information
?
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substrate specificity analysis, overview
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-
additional information
?
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-
versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase
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-
-
additional information
?
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-
Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin
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-
-
additional information
?
-
Lentinus squarrosulus 12292 ITS
-
Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin
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-
-
additional information
?
-
Lentinus squarrosulus TAMI004
-
versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase
-
-
-
additional information
?
-
-
humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042')
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-
additional information
?
-
Lentinus tigrinus VKM F-160
-
humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042')
-
-
-
additional information
?
-
substrate specificity analysis, overview
-
-
-
additional information
?
-
-
in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F-1767
-
in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
-
-
?
additional information
?
-
-
highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
-
-
-
additional information
?
-
-
the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview
-
-
-
additional information
?
-
-
highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
-
-
-
additional information
?
-
-
the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview
-
-
-
additional information
?
-
-
in the absence of Mn2+, efficient hydroquinone oxidation is dependent on exogenous H2O2. In the presence of Mn2+, exogenous H2O2 is not required for complete oxidation of hydroquinones
-
-
?
additional information
?
-
versatile peroxidase is able to oxidize typical substrates of other peroxidases, these hybrid properties are due to the coexistence in a single protein of different catalytic sites reminiscent of those present in the other basidiomycete peroxidase families
-
-
?
additional information
?
-
presence of two independent catalytic sites for different phenols and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in native enzyme, characterizedby high and low specificity constants, i.e. Km in the micromolar range and Km in the millimolar range, respcetively
-
-
?
additional information
?
-
-
presence of two independent catalytic sites for different phenols and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in native enzyme, characterizedby high and low specificity constants, i.e. Km in the micromolar range and Km in the millimolar range, respcetively
-
-
?
additional information
?
-
the enzyme shows a broad substrate spectrum
-
-
-
additional information
?
-
-
the enzyme shows a broad substrate spectrum
-
-
-
additional information
?
-
no activity with Phenol Red and Remazol Brilliant Blue
-
-
?
additional information
?
-
-
no substrates: Fe2+, veratryl alcohol
-
-
?
additional information
?
-
enzyme DypB degrades solvent-obtained fractions of a Kraft lignin. The recombinant mutant enzyme Rh_DypB shows a classical peroxidase activity which is significantly increased by adding Mn2+ ions, kinetic parameters for H2O2, Mn2+, ABTS, and 2,6-DMP are determined. The enzyme shows broad dye-decolorization activity, especially in the presence of Mn2+, oxidizes various aromatic monomers from lignin, and cleaves the guaiacylglycerol-beta-guaiacyl ether (GGE), i.e., the Calpha-Cbeta bond of the dimeric lignin model molecule of beta-O-4 linkages. Under optimized conditions, 2 mM GGE is fully cleaved by recombinant Rh_DypB, generating guaiacol in only 10 min, at a rate of 12.5 micromol/min/mg enzyme. Screening of oxidation activity on monomeric lignin model compounds, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Lentinus squarrosulus TAMI004
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Lentinus squarrosulus TAMI004
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
-
-
?
additional information
?
-
ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
-
-
-
additional information
?
-
-
ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
-
-
-
additional information
?
-
Bjerkandera adusta UAMH8258
ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
-
-
-
additional information
?
-
substrate specificity analysis, overview
-
-
-
additional information
?
-
-
versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase
-
-
-
additional information
?
-
Lentinus squarrosulus TAMI004
-
versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase
-
-
-
additional information
?
-
-
humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042')
-
-
-
additional information
?
-
Lentinus tigrinus VKM F-160
-
humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042')
-
-
-
additional information
?
-
substrate specificity analysis, overview
-
-
-
additional information
?
-
-
highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
-
-
-
additional information
?
-
-
highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
enzyme shows the typical Soret band, heme content is 0.5 mol per mol of protein
heme
myoglobin (Mb) is the predominant oxygen-binding heme protein in vertebrate skeletal muscle and heart
heme
myoglobin (Mb) is the predominant oxygen-binding heme protein in vertebrate skeletal muscle and heart
heme
the predicted heme-binding residues are His66, Glu67, Leu69, Arg70, Phe73, Pro172, Glu173, Pro174, Ile181, Phe185, Leu199, Leu200, Ser202, His203, Ile205, Ala206, Ala207, Ala208, Asp209, His210, Val211, Phe220, Leu262, Ser264, Phe292, and Met296
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
-
though copper is not directly involved in the activity of versatile peroxidase, copper is an activator for multiple catabolic enzymes such as lytic polysaccharide monooxygenases (LPMO) and glyoxal oxidases that are indirectly involved with versatile peroxidase activity
Fe2+
Manganese
Mn2+
Ca2+
-
required, Ca2+-depleted enzyme is able to form the active intermediate compound I but its long range electron transfer has been disrupted
Ca2+
required, binding structure, three-dimensional modeling, overview
Manganese
-
oxidation of Mn(II) to Mn(III), presence of manganese in the reaction mixture with industrial dyes does not enhance the decoloration rate
Manganese
-
Km value 0.022 for wild-type, 0.021 for mutant W170A, 0.022 for mutant R263N, 0.026 for mutant Q266F, 0.027 for mutant V166/168L
Mn2+
-
activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10%
Mn2+
-
Mn(II) can promote the oxidation of low redox potential substrates and increase decolorization efficiency up to 70% for the recombinant enzyme VP1 (rVP1), binding site structure analysis
Mn2+
-
isoenzyme Pl, putative Mn-interaction site near E35, E39, D175. Isoenzyme Ps1, putative Mn-interaction site near E36, E40, D181
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
substrate inhibition
bovine pancreatic RNase
-
competitive to oxidation of veratryl alcohol, non-competitive to oxidation of Mn2+
-
N-bromosuccinimide
-
modification of tryptophan residues by N-bromosuccinimide drastically reduces the Mn(II)-independent activity and dye decoloration, while Mn(II)-dependent activity is maintained. Effect is not reversed by addition of mediators
NaOCl
the heme iron directly reacts with NaOCl. The heme reduces NaOCl toxicity towards Mb side-chains. The oxidized (Fe3+) form of Mb (metMB) peroxidase activity is significantly decreased after incubation with NaOCl and NaCN, but not with NaOCl alone
NaOCl
the heme iron directly reacts with NaOCl. The heme reduces NaOCl toxicity towards Mb side-chains. The oxidized (Fe3+) form of Mb (metMB) peroxidase activity is significantly decreased after incubation with NaOCl and NaCN, but not with NaOCl alone
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
veratryl alcohol, which increases the ability of LiP to oxidize high-redox-potential substrates, does not affect oxidation of these by versatile peroxidases of Bjerkandera adusta
-
additional information
-
veratryl alcohol, which increases the ability of LiP to oxidize high-redox-potential substrates, does not affect oxidation of these by versatile peroxidases of Bjerkandera adusta
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.4
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
0.0007
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C
0.0017
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant R257L
0.0023
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P76G, high efficiency site, pH 3.5, 25°C
0.0026
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant M247L
0.0028
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant S158E
0.003
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, wild-type
0.003
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, high efficiency site, pH 3.5, 25°C
0.0032
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant R257A/A260F
0.0035
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant M247F
0.0036
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant R257K
0.004
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant S158D
0.004
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176D, high efficiency site, pH 3.5, 25°C
0.0041
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant F142G, high efficiency site, pH 3.5, 25°C
0.0054
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176G, high efficiency site, pH 3.5, 25°C
0.0054
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, high efficiency site, pH 3.5, 25°C
0.0054
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P141G, high efficiency site, pH 3.5, 25°C
0.0065
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant K264A
0.008
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215Q, high efficiency site, pH 3.5, 25°C
0.009
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant A260F
0.0143
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G, high efficiency site, pH 3.5, 25°C
0.0194
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
0.0194
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
0.056
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.0836
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, low efficiency site, pH 3.5, 25°C
0.18
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at 30°C and pH 4.5
0.305
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G, low efficiency site, pH 3.5, 25°C
0.383
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176G, low efficiency site, pH 3.5, 25°C
0.461
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P141G, low efficiency site, pH 3.5, 25°C
0.48
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
0.54
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, pH 3.5, temperature not specified in the publication
0.54
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
0.828
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant F142G, low efficiency site, pH 3.5, 25°C
0.86
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of Mn2+, pH 3.0, temperature not specified in the publication
1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant W164S, low efficiency site, pH 3.5, 25°C
1.09
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, low efficiency site, pH 3.5, 25°C
1.66
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215Q, low efficiency site, pH 3.5, 25°C
2.23
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176D, low efficiency site, pH 3.5, 25°C
2.86
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P76G, low efficiency site, pH 3.5, 25°C
14.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
15.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
0.036
2,6-dimethoxyphenol
mutant P76G, high efficiency site, pH 3.5, 25°C
0.038
2,6-dimethoxyphenol
mutant K176D, high efficiency site, pH 3.5, 25°C
0.058
2,6-dimethoxyphenol
mutant K215G, high efficiency site, pH 3.5, 25°C
0.063
2,6-dimethoxyphenol
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
0.065
2,6-dimethoxyphenol
mutant F142G, high efficiency site, pH 3.5, 25°C
0.066
2,6-dimethoxyphenol
mutant E140G, high efficiency site, pH 3.5, 25°C
0.078
2,6-dimethoxyphenol
mutant K215Q, high efficiency site, pH 3.5, 25°C
0.078
2,6-dimethoxyphenol
wild-type, high efficiency site, pH 3.5, 25°C
0.1
2,6-dimethoxyphenol
mutant K176G, high efficiency site, pH 3.5, 25°C
0.104
2,6-dimethoxyphenol
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
0.119
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
0.155
2,6-dimethoxyphenol
mutant P141G, high efficiency site, pH 3.5, 25°C
0.189
2,6-dimethoxyphenol
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
0.345
2,6-dimethoxyphenol
-
absence of Mn2+, pH not specified in the publication, temperature not specified in the publication
2.38
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
2.56
2,6-dimethoxyphenol
mutant K215Q, low efficiency site, pH 3.5, 25°C
2.97
2,6-dimethoxyphenol
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
3.33
2,6-dimethoxyphenol
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
6.5
2,6-dimethoxyphenol
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
10.5
2,6-dimethoxyphenol
wild-type, low efficiency site, pH 3.5, 25°C
16
2,6-dimethoxyphenol
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
17.5
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
29.5
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
32
2,6-dimethoxyphenol
wild-type, pH 3.5, temperature not specified in the publication
36.2
2,6-dimethoxyphenol
mutant K176G, low efficiency site, pH 3.5, 25°C
37.4
2,6-dimethoxyphenol
mutant E140G, low efficiency site, pH 3.5, 25°C
37.6
2,6-dimethoxyphenol
mutant W164S, low efficiency site, pH 3.5, 25°C
76
2,6-dimethoxyphenol
mutant P141G, low efficiency site, pH 3.5, 25°C
0.009
2,7-diaminofluorene
-
absence of Mn2+, pH 4.5, temperature not specified in the publication
0.038
2,7-diaminofluorene
-
presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
0.0059
4-hydroquinone
mutant F142G, high efficiency site, pH 3.5, 25°C
0.0103
4-hydroquinone
mutant P76G, high efficiency site, pH 3.5, 25°C
0.0122
4-hydroquinone
mutant K215Q, high efficiency site, pH 3.5, 25°C
0.013
4-hydroquinone
mutant K176D, high efficiency site, pH 3.5, 25°C
0.0174
4-hydroquinone
mutant K215G, high efficiency site, pH 3.5, 25°C
0.0189
4-hydroquinone
mutant K176G, high efficiency site, pH 3.5, 25°C
0.0205
4-hydroquinone
mutant E140G, high efficiency site, pH 3.5, 25°C
0.0251
4-hydroquinone
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
0.0362
4-hydroquinone
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
0.0397
4-hydroquinone
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
0.04
4-hydroquinone
mutant P141G, high efficiency site, pH 3.5, 25°C
0.41
4-hydroquinone
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
0.618
4-hydroquinone
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
0.836
4-hydroquinone
mutant E140G, low efficiency site, pH 3.5, 25°C
0.884
4-hydroquinone
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
1.112
4-hydroquinone
mutant K215G, low efficiency site, pH 3.5, 25°C
1.114
4-hydroquinone
mutant P141G, low efficiency site, pH 3.5, 25°C
1.18
4-hydroquinone
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
0.03
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.04
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+
0.051
H2O2
wild-type, pH 3.5, temperature not specified in the publication
0.2
H2O2
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
3.1
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
11.2
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.045
Mn2+
wild-type, pH 3.5, temperature not specified in the publication
0.12
Mn2+
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.68
Mn2+
-
pH not specified in the publication, temperature not specified in the publication
0.0066
Reactive Black 5
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.007
Reactive Black 5
wild-type, pH 3.5, temperature not specified in the publication
0.035
syringaldazine
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
0.066
syringaldazine
-
absence of Mn2+, pH 7.0, temperature not specified in the publication
0.304
veratryl alcohol
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
0.53
veratryl alcohol
-
presence of Mn2+, pH 4.5, temperature not specified in the publication
additional information
fulvic acid
-
Hill coefficient 3.0, presence of Mn2+, Km value 0.009 g/l, pH 3.5, 25°C
additional information
fulvic acid
-
Hill coefficient 3.6, absence of Mn2+, Km value 0.044 g/l, pH 3.5, 25°C
additional information
humic acid
-
Hill coefficient 1.2, absence of Mn2+, Km value 0.08 g/l, pH 3.5, 25°C
additional information
humic acid
-
Hill coefficient 2.8, presence of Mn2+, Km value 0.005 g/l, pH 3.5, 25°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetic parameters for wild-type enzyme and five selected mutant variants with dye substrates, comparisons, overview
-
additional information
additional information
-
kinetic parameters for wild-type enzyme and five selected mutant variants with dye substrates, comparisons, overview
-
additional information
additional information
Michaelis-Menten kinetics by mutant enzyme N246A
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic analysis, recombinant enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
47
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
0.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant M247F
2.77
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
4.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant M247L
5.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C
5.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant A260F
6.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of Mn2+, pH 3.0, temperature not specified in the publication
6.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P76G, high efficiency site, pH 3.5, 25°C
7.7
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant S158D
7.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215Q, high efficiency site, pH 3.5, 25°C
8.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, wild-type
8.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, high efficiency site, pH 3.5, 25°C
8.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant K264A
9.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant S158E
10.9
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant F142G, high efficiency site, pH 3.5, 25°C
11.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant R257K
12.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G, high efficiency site, pH 3.5, 25°C
12.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
13.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176G, high efficiency site, pH 3.5, 25°C
13.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176D, high efficiency site, pH 3.5, 25°C
13.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, high efficiency site, pH 3.5, 25°C
15.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
16.1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P141G, high efficiency site, pH 3.5, 25°C
18.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant R257A/A260F
19.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
22.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.5, 25°C, mutant R257L
93
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P141G, low efficiency site, pH 3.5, 25°C
146
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P76G, low efficiency site, pH 3.5, 25°C
154
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant F142G, low efficiency site, pH 3.5, 25°C
162
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
165
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215Q, low efficiency site, pH 3.5, 25°C
186
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, low efficiency site, pH 3.5, 25°C
204
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, low efficiency site, pH 3.5, 25°C
205
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant W164S, low efficiency site, pH 3.5, 25°C
216
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G, low efficiency site, pH 3.5, 25°C
220
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, pH 3.5, temperature not specified in the publication
220
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
223
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176D, low efficiency site, pH 3.5, 25°C
227
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
235
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
259
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176G, low efficiency site, pH 3.5, 25°C
326
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
365
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
12300
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at 30°C and pH 4.5
0.45
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.5
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
4.6
2,6-dimethoxyphenol
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
4.8
2,6-dimethoxyphenol
mutant P141G, high efficiency site, pH 3.5, 25°C
5.6
2,6-dimethoxyphenol
wild-type, high efficiency site, pH 3.5, 25°C
6.2
2,6-dimethoxyphenol
mutant P76G, high efficiency site, pH 3.5, 25°C
7.6
2,6-dimethoxyphenol
mutant K215Q, high efficiency site, pH 3.5, 25°C
9.3
2,6-dimethoxyphenol
mutant K176G, high efficiency site, pH 3.5, 25°C
9.5
2,6-dimethoxyphenol
mutant K215G, high efficiency site, pH 3.5, 25°C
9.8
2,6-dimethoxyphenol
mutant F142G, high efficiency site, pH 3.5, 25°C
10
2,6-dimethoxyphenol
mutant E140G, high efficiency site, pH 3.5, 25°C
10.6
2,6-dimethoxyphenol
-
absence of Mn2+, pH not specified in the publication, temperature not specified in the publication
10.6
2,6-dimethoxyphenol
mutant K176D, high efficiency site, pH 3.5, 25°C
17.3
2,6-dimethoxyphenol
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
20.4
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
29.8
2,6-dimethoxyphenol
wild-type, low efficiency site, pH 3.5, 25°C
30
2,6-dimethoxyphenol
-
presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
47.6
2,6-dimethoxyphenol
mutant W164S, low efficiency site, pH 3.5, 25°C
50.2
2,6-dimethoxyphenol
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
56.6
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
58
2,6-dimethoxyphenol
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
61
2,6-dimethoxyphenol
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
67
2,6-dimethoxyphenol
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
74.5
2,6-dimethoxyphenol
mutant K215Q, low efficiency site, pH 3.5, 25°C
98
2,6-dimethoxyphenol
wild-type, pH 3.5, temperature not specified in the publication
141
2,6-dimethoxyphenol
mutant P141G, low efficiency site, pH 3.5, 25°C
231.6
2,6-dimethoxyphenol
mutant K176G, low efficiency site, pH 3.5, 25°C
293
2,6-dimethoxyphenol
mutant E140G, low efficiency site, pH 3.5, 25°C
0.19
2,7-diaminofluorene
-
absence of Mn2+, pH 4.5, temperature not specified in the publication
0.83
2,7-diaminofluorene
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
9.71
4-hydroquinone
mutant F142G, high efficiency site, pH 3.5, 25°C
11.4
4-hydroquinone
mutant K215Q, high efficiency site, pH 3.5, 25°C
11.6
4-hydroquinone
mutant K176G, high efficiency site, pH 3.5, 25°C
14.6
4-hydroquinone
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
15.6
4-hydroquinone
mutant P141G, high efficiency site, pH 3.5, 25°C
16.2
4-hydroquinone
mutant E140G, high efficiency site, pH 3.5, 25°C
20
4-hydroquinone
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
20.4
4-hydroquinone
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
65.5
4-hydroquinone
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
82.1
4-hydroquinone
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
82.2
4-hydroquinone
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
85.6
4-hydroquinone
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
21.3
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
34
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+
135
H2O2
wild-type, pH 3.5, temperature not specified in the publication
490
H2O2
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
19
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
21.4
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
3.9
Mn2+
-
pH not specified in the publication, temperature not specified in the publication
54
Mn2+
wild-type, pH 3.5, temperature not specified in the publication
75
Mn2+
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
298
Mn2+
-
0.000083 1/sec/mg, incubates 30 min at 37°C, pH 9.0, spectrophotometrically measured at 415 nm
5
Reactive Black 5
-
0.0 M NaCl, 55.6 IgG relative content, 5.5% relative DNase activity
10.6
Reactive Black 5
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
11.8
Reactive Black 5
wild-type, pH 3.5, temperature not specified in the publication
0.22
syringaldazine
-
absence of Mn2+, pH 7.0, temperature not specified in the publication
6.1
syringaldazine
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
7.08
veratryl alcohol
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
26.8
veratryl alcohol
-
presence of Mn2+, pH 4.5, temperature not specified in the publication
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
7.36
manganese(II)-substituted polyoxometalate
-
in 0.1 M sodium tartrate, pH 5.0, at 20°C
-
0.85
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.99
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
1
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215Q, high efficiency site, pH 3.5, 25°C
2.45
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176G, high efficiency site, pH 3.5, 25°C
2.53
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
2.6
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, high efficiency site, pH 3.5, 25°C
3.48
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176D, high efficiency site, pH 3.5, 25°C
5.8
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
7.2
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
presence of Mn2+, pH 3.0, temperature not specified in the publication
51
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P76G, low efficiency site, pH 3.5, 25°C
99
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215Q, low efficiency site, pH 3.5, 25°C
100
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176D, low efficiency site, pH 3.5, 25°C
171
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, low efficiency site, pH 3.5, 25°C
185
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant F142G, low efficiency site, pH 3.5, 25°C
200
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant W164S, low efficiency site, pH 3.5, 25°C
201
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P141G, low efficiency site, pH 3.5, 25°C
244
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K215G, low efficiency site, pH 3.5, 25°C
410
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, pH 3.5, temperature not specified in the publication
410
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
at pH 3.0 and 25°C
676
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant K176G, low efficiency site, pH 3.5, 25°C
710
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G, low efficiency site, pH 3.5, 25°C
882
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G, high efficiency site, pH 3.5, 25°C
1120
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
2640
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant F142G, high efficiency site, pH 3.5, 25°C
2700
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
wild-type, high efficiency site, pH 3.5, 25°C
2830
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P76G, high efficiency site, pH 3.5, 25°C
3010
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant P141G, high efficiency site, pH 3.5, 25°C
4090
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
5670
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
5680
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
6480
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
0.015
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
0.29
2,6-dimethoxyphenol
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
1.3
2,6-dimethoxyphenol
mutant W164S, low efficiency site, pH 3.5, 25°C
1.9
2,6-dimethoxyphenol
mutant P141G, low efficiency site, pH 3.5, 25°C
2.8
2,6-dimethoxyphenol
wild-type, low efficiency site, pH 3.5, 25°C
2.9
2,6-dimethoxyphenol
mutant K215Q, low efficiency site, pH 3.5, 25°C
3.1
2,6-dimethoxyphenol
wild-type, pH 3.5, temperature not specified in the publication
3.8
2,6-dimethoxyphenol
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
6.4
2,6-dimethoxyphenol
mutant K176G, low efficiency site, pH 3.5, 25°C
7.8
2,6-dimethoxyphenol
mutant E140G, low efficiency site, pH 3.5, 25°C
9.1
2,6-dimethoxyphenol
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
15.1
2,6-dimethoxyphenol
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
22.6
2,6-dimethoxyphenol
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
23.8
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
30.7
2,6-dimethoxyphenol
-
absence of Mn2+, pH not specified in the publication, temperature not specified in the publication
31
2,6-dimethoxyphenol
mutant P141G, high efficiency site, pH 3.5, 25°C
44.6
2,6-dimethoxyphenol
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
71
2,6-dimethoxyphenol
wild-type, high efficiency site, pH 3.5, 25°C
91.3
2,6-dimethoxyphenol
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
93
2,6-dimethoxyphenol
mutant K176G, high efficiency site, pH 3.5, 25°C
97
2,6-dimethoxyphenol
mutant K215Q, high efficiency site, pH 3.5, 25°C
152
2,6-dimethoxyphenol
mutant F142G, high efficiency site, pH 3.5, 25°C
153
2,6-dimethoxyphenol
mutant E140G, high efficiency site, pH 3.5, 25°C
165
2,6-dimethoxyphenol
mutant K215G, high efficiency site, pH 3.5, 25°C
171
2,6-dimethoxyphenol
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
171
2,6-dimethoxyphenol
mutant P76G, high efficiency site, pH 3.5, 25°C
283
2,6-dimethoxyphenol
mutant K176D, high efficiency site, pH 3.5, 25°C
476.2
2,6-dimethoxyphenol
-
presence of Mn2+, pH not specified in the publication, temperature not specified in the publication
21.1
2,7-diaminofluorene
-
absence of Mn2+, pH 4.5, temperature not specified in the publication
21.8
2,7-diaminofluorene
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
55.6
4-hydroquinone
mutant E140G/P141G, low efficiency site, pH 3.5, 25°C
96.8
4-hydroquinone
mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C
132.8
4-hydroquinone
mutant E140G/K176G, low efficiency site, pH 3.5, 25°C
203.2
4-hydroquinone
mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C
368
4-hydroquinone
mutant E140G/P141G, high efficiency site, pH 3.5, 25°C
565
4-hydroquinone
mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C
800
4-hydroquinone
mutant E140G/K176G, high efficiency site, pH 3.5, 25°C
1600
4-hydroquinone
mutant F142G, high efficiency site, pH 3.5, 25°C
710
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
850
H2O2
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+
2400
H2O2
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
2650
H2O2
wild-type, pH 3.5, temperature not specified in the publication
1.7
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2
6.9
Mn(II)
pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2
5.7
Mn2+
-
pH not specified in the publication, temperature not specified in the publication
630
Mn2+
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
1190
Mn2+
wild-type, pH 3.5, temperature not specified in the publication
1600
Reactive Black 5
mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication
1670
Reactive Black 5
wild-type, pH 3.5, temperature not specified in the publication
3.3
syringaldazine
-
absence of Mn2+, pH 7.0, temperature not specified in the publication
174.3
syringaldazine
-
presence of Mn2+, pH 7.0, temperature not specified in the publication
2.3
veratryl alcohol
-
absence of Mn2+, pH 3.0, temperature not specified in the publication
50.6
veratryl alcohol
-
presence of Mn2+, pH 4.5, temperature not specified in the publication
additional information
fulvic acid
-
Hill coefficient 3.0, presence of Mn2+, kcat/Km value 300 g/l/min, pH 3.5, 25°C
additional information
fulvic acid
-
Hill coefficient 3.6, absence of Mn2+, kcat/Km value 25 g/l/min, pH 3.5, 25°C
additional information
humic acid
-
Hill coefficient 1.2, absence of Mn2+, kcat/Km value 15.5 g/l/min, pH 3.5, 25°C
additional information
humic acid
-
Hill coefficient 2.8, presence of Mn2+, kcat/Km value 240 g/l/min, pH 3.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as substrate, at 30°C and pH 4.5
10.8
-
substrate 2,6-dimthoxy-1,4-benzohydroquinone, pH 5.0, absence of Mn2+
23.1
-
purified refolded recombinant enzyme VP1, pH and temperature not specified in the publication
61.48
-
after 5.66fold purification, with Mn2+ as substrate, at pH 5.0 and 25°C
8.8
substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), pH 3.5, 25°C
additional information
additional information
-
manganese oxidizing activity is 12 U/ml in submerged and 131 U/ml in solid-state culture
additional information
activities of wild-type enzyme and five selected mutant variants with dye substrates, comparisons, overview
additional information
-
activities of wild-type enzyme and five selected mutant variants with dye substrates, comparisons, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4.2
-
and 3.0, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), presence of Mn2+
4.5
6.5
3
-
and 4.2, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), presence of Mn2+
3
-
substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), absence of Mn2+
3
-
Mn2+-independent oxidation of substituted phenols and aromatic molecules
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
metMb peroxidase activity is pH-dependent, increasing as pH decreases from 7.4 to 6.1, which is biologically relevant to anaerobic vertebrate muscle when incurring intracellular lactic acidosis
additional information
-
metMb peroxidase activity is pH-dependent, increasing as pH decreases from 7.4 to 6.1, which is biologically relevant to anaerobic vertebrate muscle when incurring intracellular lactic acidosis
additional information
metMb peroxidase activity is pH-dependent, increasing as pH decreases from 7.4 to 6.1, which is biologically relevant to anaerobic vertebrate muscle when incurring intracellular lactic acidosis
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.65
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
growth without Mn2+ added, stimulation of enzyme synthesis by addition of glycolate, glyoxylate, or oxalate to medium
-
-
brenda
growth without Mn2+ added, stimulation of enzyme synthesis by addition of glycolate, glyoxylate, or oxalate to medium
-
-
brenda
induction of enzyme transcripts and activity by growth on glucose-peptone medium, addition of more than 0.025 mM Mn2+ results in no detectable enzyme transkripts or activity. Enzyme expression is strongly induced by exogenous H2O2 or continuous H2O2 generation
-
-
brenda
isoenzymes MP-1 and MP-2, addition of Mn2+ to growth medium represses enzyme activity
-
-
brenda
induction of enzyme by rich peptone medium, addition of 0.5 mM Mn2+ decrease enzyme activity by 50%
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
cultured in different media with and without soil and humic acids
brenda
Lentinus tigrinus VKM F-160
-
cultured in different media with and without soil and humic acids
-
brenda
additional information
-
strains from solid-state and from submerged fermentations. The fungus produces high levels of versatile peroxidase at a C:N ratio of approximately 100, temperature of 35°C, and initial pH of 7.0. Evaluation and optimization of growth medium and production conditions, detailed overview. Versatile peroxidase production with Cu2+ exhibits the most remarkable effect followed by Zn2+. With all factors appropriate for production of versatile peroxidase, significant enzyme activity is detected in 3 days in the optimized culture medium
brenda
additional information
Lentinus squarrosulus 12292 ITS
-
strains from solid-state and from submerged fermentations. The fungus produces high levels of versatile peroxidase at a C:N ratio of approximately 100, temperature of 35°C, and initial pH of 7.0. Evaluation and optimization of growth medium and production conditions, detailed overview. Versatile peroxidase production with Cu2+ exhibits the most remarkable effect followed by Zn2+. With all factors appropriate for production of versatile peroxidase, significant enzyme activity is detected in 3 days in the optimized culture medium
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme contains a predicted signal peptide
-
brenda
-
the enzyme contains a predicted signal peptide
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the most important ligninolytic enzymes of white-rot fungi, which efficiently degrade lignin and a wide range of aromatic xenobiotics, including polychlorinated phenols, nitro- and amino-substituted phenols, synthetic dyes, and polycyclic aromatic hydrocarbons, are phenol oxidase laccase (EC 1.10.3.2) and three heme peroxidases: lignin peroxidase (LiP, EC 1.11.1.14), which catalyze the oxidative cleavage of carbon-carbon bonds and ether bonds (C-O-C) in non-phenolic aromatic substrates of high redox potential, and the manganese peroxidase (MnP, EC 1.11.1.13), which requires Mn2+ to complete its catalytic cycle and forms Mn3+ -chelates, acting as diffusing oxidizers, and also versatile peroxidase (VP, EC 1.11.1.16) that has both previous activities and is present in Pleurotus and Bjerkandera fungal species, and in some other fungi such as Lepista irina and Panus tigrinus. Evolutionary and phylogenetic analysis
evolution
versatile peroxidase (VP) is a lignin-degrading heme-containing oxidoreductase classified as a class II peroxidase, which is secreted by several species of basidiomycetes, mostly from the genera Pleurotus and Bjerkandera
evolution
-
versatile peroxidase is regarded as a hybrid of lignin peroxidase and manganese peroxidase. This enzyme possesses the catalytic features of oxidation of aromatic compounds through long-range electron transfer (LRET) and Mn (II) to Mn (III), analogous to the latter peroxidase
evolution
Bjerkandera adusta UAMH8258
-
the most important ligninolytic enzymes of white-rot fungi, which efficiently degrade lignin and a wide range of aromatic xenobiotics, including polychlorinated phenols, nitro- and amino-substituted phenols, synthetic dyes, and polycyclic aromatic hydrocarbons, are phenol oxidase laccase (EC 1.10.3.2) and three heme peroxidases: lignin peroxidase (LiP, EC 1.11.1.14), which catalyze the oxidative cleavage of carbon-carbon bonds and ether bonds (C-O-C) in non-phenolic aromatic substrates of high redox potential, and the manganese peroxidase (MnP, EC 1.11.1.13), which requires Mn2+ to complete its catalytic cycle and forms Mn3+ -chelates, acting as diffusing oxidizers, and also versatile peroxidase (VP, EC 1.11.1.16) that has both previous activities and is present in Pleurotus and Bjerkandera fungal species, and in some other fungi such as Lepista irina and Panus tigrinus. Evolutionary and phylogenetic analysis
-
evolution
Lentinus squarrosulus 12292 ITS
-
versatile peroxidase is regarded as a hybrid of lignin peroxidase and manganese peroxidase. This enzyme possesses the catalytic features of oxidation of aromatic compounds through long-range electron transfer (LRET) and Mn (II) to Mn (III), analogous to the latter peroxidase
-
malfunction
acetylation of tyrosine residues would inhibit peroxidase activity
malfunction
Tyr103 acetylation significantly reduces the rate of ferrylMb auto-reduction, indicating the role of tyrosine residues as intramolecular substrates
metabolism
-
ligninases, including laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase, are crucial components of the ligninolytic machinery. The white-rot fungi engage collective action of these enzymes in mineralization of the complex macromolecule
metabolism
-
versatile peroxidase of the white-rot fungus Lentinus tigrinus is involved in biotransformation of soil humic matter. Alkali-extractable and acid-insoluble constituents of SOM (HA) contain true macromolecular components, stable in the presence of 0.1% sodium dodecyl sulfate but degradable/resynthesizable by oxidative enzymes acting on covalent linkages. The humic acid degradation in the presence of laccase occurs at slower initial rate than in the presence of the enzyme. Each of the enzymes causes about 60% color loss and almost complete degradation of HA into smaller molecules within 2 weeks of cultivation. Depolymerization of HA in the culture liquid in the presence of laccase is accompanied by polymerization of degradation products on mycelium. Humus macromolecules are not stable to oxidative enzymes once desorbed from the mineral phase. Laccase of Lentinus tigrinus is comparable by its degradation potential to VP, and interfacial secondary synthesis reactions occur during humus decay in the presence of laccase. Comparison of versatile peroxidase and laccase activities, detailed overview
metabolism
Lentinus squarrosulus 12292 ITS
-
ligninases, including laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase, are crucial components of the ligninolytic machinery. The white-rot fungi engage collective action of these enzymes in mineralization of the complex macromolecule
-
metabolism
Lentinus tigrinus VKM F-160
-
versatile peroxidase of the white-rot fungus Lentinus tigrinus is involved in biotransformation of soil humic matter. Alkali-extractable and acid-insoluble constituents of SOM (HA) contain true macromolecular components, stable in the presence of 0.1% sodium dodecyl sulfate but degradable/resynthesizable by oxidative enzymes acting on covalent linkages. The humic acid degradation in the presence of laccase occurs at slower initial rate than in the presence of the enzyme. Each of the enzymes causes about 60% color loss and almost complete degradation of HA into smaller molecules within 2 weeks of cultivation. Depolymerization of HA in the culture liquid in the presence of laccase is accompanied by polymerization of degradation products on mycelium. Humus macromolecules are not stable to oxidative enzymes once desorbed from the mineral phase. Laccase of Lentinus tigrinus is comparable by its degradation potential to VP, and interfacial secondary synthesis reactions occur during humus decay in the presence of laccase. Comparison of versatile peroxidase and laccase activities, detailed overview
-
physiological function
despite the presence of Mn2+ in the medium, a transformant overexpressing the enzyme produces mnp4 transcripts as well as versatile peroxidase activity as early as 4 days after inoculation. The level of expression is constant throughout 10 days of incubation and the activity is comparable to the typical activity in Mn2+-deficient media
physiological function
although their function is most commonly associated with facilitating oxygen storage and diffusion, myoglobin (Mb) has also been implicated in cellular antioxidant defense. The oxidized (Fe3+) form of Mb (metMB) can react with hydrogen peroxide (H2O2) to produce ferrylmyoglobin (ferrylMb). FerrylMb can be reduced back to metMb for another round of reaction with H2O2. Horse skeletal muscle Mb displays peroxidase activity using 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) as reducing substrates, as well as the biologically-relevant substrates NADH/NADPH, ascorbate, caffeic acid, and resveratrol. FerrylMb can be reduced by both ethanol and acetaldehyde. MetMb reacts with hypochlorite in a heme-dependent fashion, indicating that Mb could play a role in hypochlorite detoxification. Mb peroxidase activity might be an important antioxidant mechanism in vertebrate cardiac and skeletal muscle under a variety of physiological conditions, such as those that might occur in contracting skeletal muscle or during hypoxia
physiological function
although their function is most commonly associated with facilitating oxygen storage and diffusion, myoglobin (Mb) has also been implicated in cellular antioxidant defense. The oxidized (Fe3+) form of Mb (metMB) can react with hydrogen peroxide (H2O2) to produce ferrylmyoglobin (ferrylMb). FerrylMb can be reduced back to metMb for another round of reaction with H2O2. Horse skeletal muscle Mb displays peroxidase activity using 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) as reducing substrates, as well as the biologically-relevant substrates NADH/NADPH, ascorbate, caffeic acid, and resveratrol. FerrylMb can be reduced by both ethanol and acetaldehyde. MetMb reacts with hypochlorite in a heme-dependent fashion, indicating that Mb could play a role in hypochlorite detoxification. Mb peroxidase activity might be an important antioxidant mechanism in vertebrate cardiac and skeletal muscle under a variety of physiological conditions, such as those that might occur in contracting skeletal muscle or during hypoxia
physiological function
-
Lentinus squarrosulus is a saprophytic white-rot producing novel versatile peroxidase that is capable of selectively degrading lignin of the crop residues. Treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification
physiological function
-
treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification. Screening of wild isolates for a versatile peroxidase having exceptional efficiency for aromatics and manganese oxidation
physiological function
versatile peroxidase (VP) from Pleurotus eryngii is a heme-containing peroxidase with a broad substrate spectrum that can break down many structurally distinct pollutants, including azo dyes. Versatile peroxidase is a hybrid enzyme that combines the catalytic characteristics of MnP (i.e., the ability to oxidase Mn2+ to Mn3+, which when complexed by organic acids can oxidize aromatic compounds, EC 1.11.1.13) with the LiP-like ability (EC 1.11.1.14) to use the long-range electron transfer (LRET) pathway based on surface-exposed catalytic tryptophan for the oxidation of compounds with a higher redox potential. Versatile peroxidase can directly oxidize many high-redox-potential dyes, whereas LiP requires various redox mediators to complete the same reaction. Verstaile peroxidase can also oxidize veratryl alcohol but has a much lower affinity for it as compared to lignin peroxidase (LiP)
physiological function
versatile peroxidase (VP) secreted by white-rot fungi is involved in the degradation of lignin within land ecosystems, with a broad substrate scope and minor requirements
physiological function
versatile peroxidases can directly attack lignin, cellulose, and hemicellulose in the plant cell wall to decompose it
physiological function
Lentinus squarrosulus TAMI004
-
treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification. Screening of wild isolates for a versatile peroxidase having exceptional efficiency for aromatics and manganese oxidation
-
physiological function
Bjerkandera adusta UAMH8258
-
versatile peroxidases can directly attack lignin, cellulose, and hemicellulose in the plant cell wall to decompose it
-
physiological function
Lentinus squarrosulus 12292 ITS
-
Lentinus squarrosulus is a saprophytic white-rot producing novel versatile peroxidase that is capable of selectively degrading lignin of the crop residues. Treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification
-
additional information
-
enzyme VP1 contains a Mn-binding site, a heme binding site and a substrate binding site according to the conserved domain database (CDD). VP1 demonstrates both MnP and LiP structural characterization, including Mn-binding site and an exposed tryptophan residue. The conserved Mn-binding site allows VP to obtain electrons from Mn(II) and oxidize Mn(II) to Mn(III). Three conserved amino acid residues, Glu63, Glu67, and Asp202, comprise the Mn-binding site of both VP and MnP. The chelated Mn(III) ions released from the Mn binding site act as diffusible charge transfer mediators attacking low redox potential phenolic substrates like 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol. According to multiple sequence alignment, the tryptophan residue is conserved in VP1 and other VPs and LiPs, but not in MnPs. Trp191 in VP1 is likely to have a direct oxidation capacity on high redox potential substrates, such as verytryl alcohol and Reactive Black 5 via long-range electron transfer (LRET) to heme. In addition, two conserved residues, His102 and His259, located on the proximal and the distal of heme binding region and conserved in VP and LiP, may also involve in LRET for high redox potential substrates oxidation
additional information
role of tyrosine residues in Mb peroxidase activity
additional information
role of tyrosine residues in Mb peroxidase activity, overview. Residue Y103 is important in orienting certain substrates in the heme pocket
additional information
versatile peroxidase (VP) from Bjerkandera adusta is able to oxidize bulky and high-redox substrates through a long-range electron transfer (LRET) pathway
additional information
-
versatile peroxidase (VP) from Bjerkandera adusta is able to oxidize bulky and high-redox substrates through a long-range electron transfer (LRET) pathway
additional information
versatile peroxidase (VP) has an access channel that is open to the solvent and where low-redox potential substrates are oxidized. In addition, VP has a superficial catalytic tryptophan that, in its active state, oxidizes both low-redox and more significantly, high redox potential substrates through a long-range electron transfer pathway to the heme, like lignin peroxidase. In the sagittal plane of the protein structure there is a small heme access channel where Mn2+ is oxidized to Mn3+, the latter acting as a diffusible oxidizer as also occurs in MnP (EC 1.11.1.13)
additional information
-
versatile peroxidase is endowed with polyvalent catalytic sites that render this protein with high redox potential
additional information
versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111
additional information
-
versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111
additional information
-
versatile peroxidase, an extracellular heme protein of the ligninolytic system, is endowed with polyvalent catalytic sites that render this protein with high redox potential
additional information
Lentinus squarrosulus TAMI004
-
versatile peroxidase, an extracellular heme protein of the ligninolytic system, is endowed with polyvalent catalytic sites that render this protein with high redox potential
-
additional information
Bjerkandera adusta UAMH8258
-
versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111
-
additional information
-
enzyme VP1 contains a Mn-binding site, a heme binding site and a substrate binding site according to the conserved domain database (CDD). VP1 demonstrates both MnP and LiP structural characterization, including Mn-binding site and an exposed tryptophan residue. The conserved Mn-binding site allows VP to obtain electrons from Mn(II) and oxidize Mn(II) to Mn(III). Three conserved amino acid residues, Glu63, Glu67, and Asp202, comprise the Mn-binding site of both VP and MnP. The chelated Mn(III) ions released from the Mn binding site act as diffusible charge transfer mediators attacking low redox potential phenolic substrates like 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol. According to multiple sequence alignment, the tryptophan residue is conserved in VP1 and other VPs and LiPs, but not in MnPs. Trp191 in VP1 is likely to have a direct oxidation capacity on high redox potential substrates, such as verytryl alcohol and Reactive Black 5 via long-range electron transfer (LRET) to heme. In addition, two conserved residues, His102 and His259, located on the proximal and the distal of heme binding region and conserved in VP and LiP, may also involve in LRET for high redox potential substrates oxidation
-
additional information
Lentinus squarrosulus 12292 ITS
-
versatile peroxidase is endowed with polyvalent catalytic sites that render this protein with high redox potential
-
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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). VPS1_PLEER
370
0
39046
Swiss-Prot
Secretory Pathway (Reliability: 2)
VPL1_PLEER
361
0
37596
Swiss-Prot
Secretory Pathway (Reliability: 2)
VPL2_PLEER
361
0
37624
Swiss-Prot
Secretory Pathway (Reliability: 1)
DYP2_AMYS7
Amycolatopsis sp. (strain ATCC 39116 / 75iv2)
464
0
50225
Swiss-Prot
-
A0A2U8JQ39_9PEZI
1031
0
108619
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2R8CGC7_9RHOB
476
0
52474
TrEMBL
-
A0A6J5H5A2_9BURK
508
0
54746
TrEMBL
-
A0A2R8BGE4_9RHOB
580
0
64979
TrEMBL
-
A0A2Z2NZ98_9GAMM
514
0
56927
TrEMBL
-
MYG_MOUSE
154
0
17070
Swiss-Prot
Mitochondrion (Reliability: 1)
Q96V56_PLEOS
131
0
13510
TrEMBL
Secretory Pathway (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
x * 43000, SDS-PAGE, x * 41000, SDS-PAGE of deglycosylated enzyme
43000
43000
x * 43000, SDS-PAGE, x * 41000, SDS-PAGE of deglycosylated enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
?
x * 42000, wild-type enzyme, sequence calculation x * 51500, Aga2-fusion enzyme, sequence calculation, x * 50000-65000, recombinant hyperglycosylated Aga2-fusion enzyme, SDS-PAGE
additional information
the enzyme structure includes 12 alpha-helices (Phe3-Gln20, Leu44-Phe57, Glu63-His74, Val114-Val125, Ala131-Cys147, Val178-Ala188, Thr193-Ala207, Thr229-Leu237, Gln263-Ala269, Ser271-Asn283, Gln285-Ile301, Ile338-Ala341), and two short beta-sheets (Gly-Ile100, Glu51-Val52)
additional information
-
the enzyme structure includes 12 alpha-helices (Phe3-Gln20, Leu44-Phe57, Glu63-His74, Val114-Val125, Ala131-Cys147, Val178-Ala188, Thr193-Ala207, Thr229-Leu237, Gln263-Ala269, Ser271-Asn283, Gln285-Ile301, Ile338-Ala341), and two short beta-sheets (Gly-Ile100, Glu51-Val52)
additional information
Bjerkandera adusta UAMH8258
-
the enzyme structure includes 12 alpha-helices (Phe3-Gln20, Leu44-Phe57, Glu63-His74, Val114-Val125, Ala131-Cys147, Val178-Ala188, Thr193-Ala207, Thr229-Leu237, Gln263-Ala269, Ser271-Asn283, Gln285-Ile301, Ile338-Ala341), and two short beta-sheets (Gly-Ile100, Glu51-Val52)
-
additional information
-
W170 exposed on enzyme surface is a substrate-binding site both for veratryl alcohol and for polymeric substrates
additional information
determination of the secondary structure of the N246Avariant with alpha-helix and beta-strand content of about 29% and about 19%, respectively
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
sequence has one potential N-glycosylation site at Asn109
glycoprotein
-
MP-1, up to 5% carbohydrate content, MP-2, up to 7% carbohydrate
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of enzyme model and identification of active sites for oxidation of Mn2+ and of aromatic substrates
hanging drop vapor diffusion method, crystal structures of untreated versatile peroxidase (immediately after expression in Escherichia coli and in vitro reconstitution), native versatile peroxidase (treated with Mn2+), D175A variant, and wild-type verstile peroxidase (from Pleurotus eryngii culture)
mutant enzyme W164Y, sitting-drop vapor diffusion method, resolution 1.94 A
mutants E140G, P141G, K176G, and E140G/K176G, to 1.6, 2.0, 1.5, 1.7 and 2.35 A resolution, respectively
sitting drop vapor diffusion method, using 0.1 M sodium MES buffer at pH 6.5, 25% (w/v) PEG 4000 and 0.2 M MgCl2
resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the five-coordinated quantum mechanically mixed-spin state being the most populated in the latter. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -260 mV
-
structural changes in the mutants D153H, D153A, R244L, N246H, N246A, D153A/N246A are confined to the distal heme environment
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A173R
kcat/KM for Mn2+ is 1.4fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.4fold higher than wild-type value, kcat/Km for Reactive Black 5 is 1.3fold higher than wild-type value
D175A
kcat/KM for Mn2+ is 842fold lower than wild-type value, kcat/Km for veratryl alcohol is3.2 fold higher than wild-type value, kcat/Km for Reactive Black 5 is 1.8fold higher than wild-type value
E140G
substitution of bulky residue at the main heme access channel, kinetic analysis
E140G/K176G
variant attains catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site W164
E140G/P141G
substitution of bulky residue at the main heme access channel, kinetic analysis
E140G/P141G/K176G
variant attains catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site W164
E140G/P182S/Q229P
site-directed mutagenesis, the mutant BB-8 is active over an enhanced pH range compared to wild-type and displays strong hyperactivation after incubation at alkaline pH with a 3fold increase in activity, The active pH range for mutant BB-8 is expanded considerably for several substrates, including ABTS, sinapic acid and guaiacol. Consequently, BB-8 is active in the acid range (pH 3-4) and remarkably, in the pH interval from 5 to 9 in which the activity of the parental VP is negligible. The kinetic parameters measured for ABTS reveals enhanced catalytic efficiency at acid pH as result of increased affinity, which permits BB-8 to remain active at basic pHs. This effect is mostly attributed to the E140G mutation that enables the mutant to work with similar catalytic efficiency at pH 6 as the parental type at pH 3.5, due to the widening of the heme channel. Whilst the activity against Mn2+ is diminished due to the P182S mutation introduced close to this catalytic site, this mutation offers the first experimental insight into the role of the Mn2+ site for the direct (non-mediated) oxidation of ABTS at neutral/basic pH
E140G/W164S/K176G
variant attains catalytic efficiencies for oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) at the heme channel similar to those of the exposed tryptophan site W164
E36A
kcat/KM for Mn2+ is 258fold lower than wild-type value, kcat/Km for veratryl alcohol is identical to wild-type value, kcat/Km for Reactive Black 5 is 1.2fold higher than wild-type value
E36A/E40A
kcat/KM for Mn2+ is 16000fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.3fold higher than wild-type value, kcat/Km for Reactive Black 5 is 1.1fold higher than wild-type value
E36A/E40A/D175A
kcat for Mn2+ is 149fold lower than wild-type value, kcat/Km for veratryl alcohol is nearly identical to wild-type value, kcat/Km for Reactive Black 5 is 2fold higher than wild-type value
E36A/E40A/D175A/P327ter
kcat for Mn2+ is 149fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.6fold lower than wild-type value, kcat/Km for Reactive Black 5 is 2.4fold higher than wild-type value
E36D
kcat/KM for Mn2+ is 77fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.3fold higher than wild-type value, kcat/Km for Reactive Black 5 is 3.5fold higher than wild-type value
E37K/H39R/V160A/T184M/Q202L/D213A/G330R
site-directed mutagenesis of enzyme mutant E37K/V160A/T184M/Q202L introducing three additional stabilizing point mutations, the final mutant (2-1B) shows an overall enhancement of 8°C in kinetic thermostability compared to wild-type enzyme, the specific activity increases 2.5fold, and the expression rate is enhanced by 52 fold. The thermostability mutant 2-1B displays remarkable stability at alkaline pH (with a residual activity above 60% at pH 9 after 120 h of incubation), which is rather unusual in fungal peroxidases. Although 2-1B is stable at alkaline conditions, there is hardly any activity at its three catalytic sites at basic pH
E37K/V160A/T184M/Q202L
E40A
kcat/KM for Mn2+ is 1231fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.2fold lower than wild-type value, kcat/Km for Reactive Black 5 is nearly identical to wild-type value
E40D
kcat/KM for Mn2+ is 54fold lower than wild-type value, kcat/Km for veratryl alcohol is 1.3fold lower than wild-type value, kcat/Km for Reactive Black 5 is 2.4fold higher than wild-type value
F142G
substitution of bulky residue at the main heme access channel, kinetic analysis
K176D
substitution of bulky residue at the main heme access channel, kinetic analysis
K176G
substitution of bulky residue at the main heme access channel, kinetic analysis
K215G
substitution of bulky residue at the main heme access channel, kinetic analysis
K215Q
substitution of bulky residue at the main heme access channel, kinetic analysis
N11D/G35K/E40K/T45A/S86R/P141A/F186L/T323I
site-directed mutagenesis
P141G
substitution of bulky residue at the main heme access channel, kinetic analysis
P76G
substitution of bulky residue at the main heme access channel, kinetic analysis
R257A/A260F
R257D
V160I/A260G
site-directed mutagenesis, the mutant MV4 shows increased dye degradation activity compared to the wild-type enzymen with Evans blue, Amido black 10B, and especially with Guinea green B
V160I/A260V
site-directed mutagenesis, the mutant MV5 shows increased dye degradation activity compared to the wild-type enzyme with Evans blue, and Guinea green B, but not with Amido black 10B
V160L/A260S
site-directed mutagenesis, the mutant MV1 shows increased dye degradation activity compared to the wild-type enzyme
V160Y
site-directed mutagenesis, the mutant MV2 shows increased dye degradation activity compared to the wild-type enzyme with Evans blue and Amido black 10B, but not with Guinea green B
V160Y/A260R
site-directed mutagenesis, the mutant MV3 shows increased dye degradation activity compared to the wild-type enzyme with Evans blue and Amido black 10B, but not with Guinea green B
W164H
W164S
W164X
site-directed mutagenesis, no activity at the catalytic Trp164 at basic pH due to the fact that the reduction potential of the Trp164 radical decreases as the pH increases, hindering the oxidation of high-redox potential substrates at neutral/basic pH. The long-range electron transfer pathway from Trp164 to the heme is permanently cancelled out at pHs above pH 5.0, thereby diverting the oxidative route for the oxidation of low-redox potential substrates to the other two catalytic sites at the time that the oxidation of high-redox potential compounds is supressed
W164Y
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
W164Y/R257A/A260F
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
Q266F
-
kinetic properties for H2O2 almost identical to those of wild-type, less than half the RNase A-oxidizing activity of wild-type
R263N
-
kinetic properties for H2O2 almost identical to those of wild-type, additional N-glycosylation
V166/168L
-
kinetic properties for H2O2 almost identical to those of wild-type
W170A
-
kinetic properties for H2O2 almost identical to those of wild-type, no oxidation of veratryl alcohol, decrease in oxodation of RNase A
D153A
mutation minimally affects the second order rate constant for Compound I formation and the specificity constant for H2O2, but substitution dramatically reduces the stability of Compound I
D153A/N246A
mutation reduces the second order rate constant for Compound I formation and the specificity constant for H2O2 less than 30fold, substitution dramatically reduces the stability of Compound I
D153H
mutant is more than an order of magnitude less reactive with H2O2 than wild-type
N246A
R244L
mutation abolishes the peroxidase activity, and heme iron of the mutant shows a pH-dependent transition from high spin pH 5 to low spin pH 8.5
additional information
E37K/V160A/T184M/Q202L
mutant obtained by directed evolution, increase in activity and temperature stability
E37K/V160A/T184M/Q202L
site-directed mutagenesis, the secretion of the mutant enzyme from recombinant Saccharomyces cerevisiae improves 129fold compared to wild-type, yielding 22 mg/l of active, soluble and stable enzyme, overexpression in Pichia pastoris, the enzyme is secreted
R257A/A260F
43% decrease in efficiency for oxidizing veratryl alcohol
R257D
versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation
W164H
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
W164S
site-directed mutagenesis, substitution of Trp-164 by a histidine, serine, or tyrosine residues causes a complete loss of activity on veratryl alcohol and Reactive Black 5
W164S
loss activity. Residue is responsible for high redox potential substrate oxidation
N246A
mutation inimally affects the second order rate constant for Compound I formation and the specificity constant for H2O2, but substitution dramatically reduces the stability of Compound I
additional information
introduction of radical-forming aromatic amino acids by chemical modification of the protein surface is performed using carbodiimide and succiniimide as carboxyl group activators, and the catalytic implications of these additional surface active-sites on the oxidation of 2,6-dimethylphenol, Mn2+, and remazol brilliant blue R (RBBR) are determined. These three different substrates are oxidized in different active sites of the enzyme molecule, of which the high redox RBBR is the only one that is transformed by an external radical formed in the protein surface. Both catalytic constants kcat and KM are significantly affected by the chemical modifications. Tryptophan- and tyrosine-modified versatile peroxidase shows higher catalytic transformation than the unmodified enzyme for RBBR, while the Mn2+ oxidation is significantly reduced by all chemical modifications. Formation of additional protein-based radicals after the chemical modification with radical-forming amino acids is determined by electron paramagnetic resonance studies. The chemical modification could modify any free amino or free carboxylic groups. The access channel to the heme edge is formed by two lysines (K212 and K275) and a glutamic acid (E169) that are prone to be modified. Method overview
additional information
-
introduction of radical-forming aromatic amino acids by chemical modification of the protein surface is performed using carbodiimide and succiniimide as carboxyl group activators, and the catalytic implications of these additional surface active-sites on the oxidation of 2,6-dimethylphenol, Mn2+, and remazol brilliant blue R (RBBR) are determined. These three different substrates are oxidized in different active sites of the enzyme molecule, of which the high redox RBBR is the only one that is transformed by an external radical formed in the protein surface. Both catalytic constants kcat and KM are significantly affected by the chemical modifications. Tryptophan- and tyrosine-modified versatile peroxidase shows higher catalytic transformation than the unmodified enzyme for RBBR, while the Mn2+ oxidation is significantly reduced by all chemical modifications. Formation of additional protein-based radicals after the chemical modification with radical-forming amino acids is determined by electron paramagnetic resonance studies. The chemical modification could modify any free amino or free carboxylic groups. The access channel to the heme edge is formed by two lysines (K212 and K275) and a glutamic acid (E169) that are prone to be modified. Method overview
additional information
versatile peroxidase from the fungus Bjerkandera adusta confers abiotic stress tolerance in transgenic tobacco plants. Thirty independent T2 transgenic VP lines overexpressing the fungal Bjerkandera adusta VP gene are selected on kanamycin. The VP22, VP24, and VP27 lines show significant manganese peroxidase (MnP) activity. The highest is VP22, which shows 10.87fold more manganese peroxidase activity than the wild-type plants and leads to a 34% increase in plant height and 28% more biomass. The VP22, VP24, and VP27 lines show enhanced tolerance to drought, 200 mM NaCl, and 400 mM sorbitol. Also, these transgenics display significant tolerance to methyl viologen, an active oxygen-generating compound. The average stem length of transgenic tobacco plants expressing the VP gene is approximately 34% taller than the wild-type plants, and there is a 28% average increase in fresh weight after three months in greenhouse conditions. Phenotypes, detailed overview
additional information
-
versatile peroxidase from the fungus Bjerkandera adusta confers abiotic stress tolerance in transgenic tobacco plants. Thirty independent T2 transgenic VP lines overexpressing the fungal Bjerkandera adusta VP gene are selected on kanamycin. The VP22, VP24, and VP27 lines show significant manganese peroxidase (MnP) activity. The highest is VP22, which shows 10.87fold more manganese peroxidase activity than the wild-type plants and leads to a 34% increase in plant height and 28% more biomass. The VP22, VP24, and VP27 lines show enhanced tolerance to drought, 200 mM NaCl, and 400 mM sorbitol. Also, these transgenics display significant tolerance to methyl viologen, an active oxygen-generating compound. The average stem length of transgenic tobacco plants expressing the VP gene is approximately 34% taller than the wild-type plants, and there is a 28% average increase in fresh weight after three months in greenhouse conditions. Phenotypes, detailed overview
additional information
Bjerkandera adusta UAMH8258
-
versatile peroxidase from the fungus Bjerkandera adusta confers abiotic stress tolerance in transgenic tobacco plants. Thirty independent T2 transgenic VP lines overexpressing the fungal Bjerkandera adusta VP gene are selected on kanamycin. The VP22, VP24, and VP27 lines show significant manganese peroxidase (MnP) activity. The highest is VP22, which shows 10.87fold more manganese peroxidase activity than the wild-type plants and leads to a 34% increase in plant height and 28% more biomass. The VP22, VP24, and VP27 lines show enhanced tolerance to drought, 200 mM NaCl, and 400 mM sorbitol. Also, these transgenics display significant tolerance to methyl viologen, an active oxygen-generating compound. The average stem length of transgenic tobacco plants expressing the VP gene is approximately 34% taller than the wild-type plants, and there is a 28% average increase in fresh weight after three months in greenhouse conditions. Phenotypes, detailed overview
-
additional information
-
immobilization of Lentinus squarrosulus on inert polyurethane foam (PUF) with optimized medium for production enhances the versatile peroxidase yield multifold. Maximal yield of versatile peroxidase achieved through optimization and immobilization strategies is 116 U/ml
additional information
Lentinus squarrosulus 12292 ITS
-
immobilization of Lentinus squarrosulus on inert polyurethane foam (PUF) with optimized medium for production enhances the versatile peroxidase yield multifold. Maximal yield of versatile peroxidase achieved through optimization and immobilization strategies is 116 U/ml
-
additional information
-
generation of a recombinant enzyme rVP1 expressed from Escherichia coli in inclusion bodies, renaturation of the recombinant enzyme. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. The ratio of guaiacyl-type to syringyl-type derivatives (G/S) after rVP1 treatment is 5.4times higher than that of the control. The polymerization of alkali lignin may be attributed to the transformation of S-type into G-type lignin by demethoxylation
additional information
-
generation of a recombinant enzyme rVP1 expressed from Escherichia coli in inclusion bodies, renaturation of the recombinant enzyme. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. The ratio of guaiacyl-type to syringyl-type derivatives (G/S) after rVP1 treatment is 5.4times higher than that of the control. The polymerization of alkali lignin may be attributed to the transformation of S-type into G-type lignin by demethoxylation
-
additional information
an engineered N-terminally truncated variant of mutant E37K/V160A/T184M/Q202L displays similar biochemical properties to those of the non-truncated counterpart in terms of kinetics, stability and spectroscopic features. Additional cycles of evolution raised the melting temperature by 8 degrees and significantly increased the enzyme's stability at alkaline pHs. In addition, the Km for H2O2 is enhanced up to 15fold while the catalytic efficiency is maintained, and there is an improvement in peroxide stability
additional information
-
an engineered N-terminally truncated variant of mutant E37K/V160A/T184M/Q202L displays similar biochemical properties to those of the non-truncated counterpart in terms of kinetics, stability and spectroscopic features. Additional cycles of evolution raised the melting temperature by 8 degrees and significantly increased the enzyme's stability at alkaline pHs. In addition, the Km for H2O2 is enhanced up to 15fold while the catalytic efficiency is maintained, and there is an improvement in peroxide stability
additional information
due to its broad substrate scope and minor requirements, versatile peroxidase is an extremely attractive blueprint to be designed by the directed evolution tool-box, directed evolution for functional expression in Saccharomyces cerevisiae, directed evolution for activity at alkaline pH, overview
additional information
improvement of degradation of azo dyes by versatile peroxidase through saturation mutagenesis and application in form of VP-coated yeast cell walls. Via saturation mutagenesis, two amino acids in the catalytic tryptophan environment of the enzyme are altered (V160 and A260). Library screening with three azo dyes reveals that these two positions have a significant influence on substrate specificity. Enzyme variants with up to 16fold higher catalytic efficiency for different azo dyes are isolated and sequenced. Immobilization of versatile peroxidase on the surface of yeast cells in purified cell wall fragments after lysis, the enzyme VP embedded in the cell wall retains about 70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h
additional information
-
improvement of degradation of azo dyes by versatile peroxidase through saturation mutagenesis and application in form of VP-coated yeast cell walls. Via saturation mutagenesis, two amino acids in the catalytic tryptophan environment of the enzyme are altered (V160 and A260). Library screening with three azo dyes reveals that these two positions have a significant influence on substrate specificity. Enzyme variants with up to 16fold higher catalytic efficiency for different azo dyes are isolated and sequenced. Immobilization of versatile peroxidase on the surface of yeast cells in purified cell wall fragments after lysis, the enzyme VP embedded in the cell wall retains about 70 % of its initial activity after 10 cycles of dye degradation each lasting 12 h
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
the recombinant enzyme maintains a large part of the starting activity following incubation for 24 h in this temperature range
25 - 55
-
Residual activity of roughly 100% is found after incubation at 25 to 55°C with all three substrates. Stability decreases gradually at temperatures from 60 to 70°C
63 - 65
the recombinant enzyme shows a good thermostability with a melting temperature of 63-65°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap Q column chromatography, and Mono Q column chromatography
-
extraction and purification of Aga2-VP fusion enzyme proteins from Saccharomyces cerevisiae strain EBY100 cell walls by dialysis, and ultrafiltration, followed by ion exchange chromatography
recombinant His-tagged N246A mutant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant protein
recombinant refolded His-tagged enzyme VP1 from Escherichia coli BL21(DE3) by nickel affinity chromatography
-
Resource-Q column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a recombinant mnp2 construct under the control of Pleurotus ostreatus sdi1 expression signals is introduced into the wild-type Pleurotus ostreatus strain by cotransformation with a carboxin-resistant marker plasmid. Recombinant Pleurotus ostreatus strains with elevated manganese peroxidase (MnP) productivity are successfully isolated. The productivity of the recombinant MnP2 in the present system is not high enough to meet the requirements for industrial applications
-
all attempts to express a functional versatile peroxidase as soluble protein in Escherichia coli fail, recombinant enzyme expression and secretion from Saccharomyces cerevisiae, overexpression of enzyme mutant E37K/V160A/T184M/Q202L in Pichia pastoris
design of a synthetic gene encoding the N246Avariant of DypB from Rhodococcus jostii strain RHA1 (Rh_DypB) is designed by back translation of the protein sequence, recombinant overexpression of His-tagged N246A mutant enzyme in Escherichia coli strain BL21(DE3), the enzyme is fully produced as folded holoenzyme, thus without the need for a further reconstitution step
DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant enzyme expression in Nicotiana tabacum cv. Petite Havana via an Agrobacterium tumefaciens strain LBA4404 transformation procedure, expression under control of the CaMV 35S promoter. Selection of the VP lines VP22, VP24, and VP27 with higher MnP (EC 1.11.1.13) activities
expression in Escherichia coli
expression in Escherichia coli fused to a thioredoxin-hexahistidine tag. Activity of the enzyme increases after removing the tag
gene vp1, DNA and amino acid sequence determination and analysis, recombinant overexpression of His-tagged enzyme VP1 in inclusion body in Escherichia coli strain BL21(DE3), most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. The ratio of guaiacyl-type to syringyl-type derivatives (G/S) after rVP1 treatment is 5.4times higher than that of the control
-
generation of an enzyme saturation mutagenesis library by site-directed muztagenesis, recombinant expression of enzyme mutants in Saccharomyces cerevisiae strain EBY100, DNA and amino acid sequence determination and analysis.The recombinant enzyme shows microheterogeneity due to hyperglycosylation in Saccharomyces cerevisiae
recombinant MnP2 is exclusively expressed and no endogenous MnP isozymes are secreted by the recombinant Pleurotus oseatus srain TM2-18
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme is the predominantly expressed manganese peroxidase in Mn2+-deficient media, whereas strongly repressed to approximately 1% in Mn2+-supplemented media
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme VP1 from inclusion body from Escherichia coli BL21(DE3)
-
using 0.15 M urea, 5 mM Ca2+, 0.02 mM hemin, a 4:1 oxidized-glutathione/reduced-glutathione ratio and 0.1 mg/ml protein at pH 9.5
-
using 0.16 M urea, 0.02 mM hemin, 5 mM CaCl2, 0.5 mM GSSG, 0.1 mM dithiothreitol, and 0.1 mg/ml protein in 20 mM Tris-HCl at pH 9.5
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
degradation
environmental protection
industry
paper production
-
versatile peroxidase reacts with soluble lignin fragments in the absence of added mediators, most probably causing extensive polymerisation of high and intermediate fractions of lignin, and an increase of the small-molecular-mass lignin fraction
synthesis
additional information
peroxidases are well-known biocatalysts produced by all organisms, especially microorganisms, and used in a number of biotechnological applications
agriculture
overproducing the VP gene in plants increases significantly their biomass and the abiotic stress tolerance. The versatile peroxidase enzyme is an effective biotechnological tool to protect organisms against ROS. In transgenic tobacco plants, it improves drought, salt, and oxidative stress tolerance. Thus, the versatile peroxidase gene represents a great potential for obtaining stress-tolerant crops. The enzyme from Bjerkandera adusta can mitigate oxidative stress induced by paraquat, salt- (NaCl), drought- and osmotic-stress (sorbitol)
agriculture
-
use of versatile peroxidase in enhancing the digestibility of straws is substantiated through proximate and in vitro digestibility analysis, use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants. Usage of commonly available crop residues such as paddy straw, finger millet straw, foxtail millet straw, little millet straw, and barnyard millet straw (milled to 1 to 2 cm length and dried at a constant temperature of 70°C) in biodegradation studies
agriculture
-
use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants
agriculture
Lentinus squarrosulus TAMI004
-
use of versatile peroxidase in enhancing the digestibility of straws is substantiated through proximate and in vitro digestibility analysis, use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants. Usage of commonly available crop residues such as paddy straw, finger millet straw, foxtail millet straw, little millet straw, and barnyard millet straw (milled to 1 to 2 cm length and dried at a constant temperature of 70°C) in biodegradation studies
-
agriculture
Bjerkandera adusta UAMH8258
-
overproducing the VP gene in plants increases significantly their biomass and the abiotic stress tolerance. The versatile peroxidase enzyme is an effective biotechnological tool to protect organisms against ROS. In transgenic tobacco plants, it improves drought, salt, and oxidative stress tolerance. Thus, the versatile peroxidase gene represents a great potential for obtaining stress-tolerant crops. The enzyme from Bjerkandera adusta can mitigate oxidative stress induced by paraquat, salt- (NaCl), drought- and osmotic-stress (sorbitol)
-
agriculture
Lentinus squarrosulus 12292 ITS
-
use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants
-
analysis
-
detection and quantification of soluble lignin transformation by measuring changes in the true colour of the system solution
analysis
-
evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
analysis
-
evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
-
degradation
versatile peroxidase presents particular interest due to its catalytic versatility including the degradation of compounds that other peroxidases are not able to oxidize directly, versatile peroxidase versatility permits its application in Mn3+-mediated or Mn-independent reactions on both low and high redox-potential aromatic substrates and dyes, versatile peroxidase can be used to reoxidize Mn-containing polyoxometalates, which are efficient oxidizers in paper pulp delignification
degradation
-
in presence of H2O2 and Mn2+, a cell-free subpernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
degradation
-
the allosteric behaviour of the VP enzyme promotes a high level of regulation of activity during the breakdown of model and industrial ligninolytic substrates, such as effluent from a pulp and paper plant, and fouled membrane solids extracted from a ground water treatment membrane
degradation
Phanerodontia chrysosporium BKM-F-1767
-
in presence of H2O2 and Mn2+, a cell-free subpernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
-
environmental protection
the enzyme immobilized on yeast cell wall fragments can be used for longterm bioremediation of environments contaminated with azo dyes
environmental protection
versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation
environmental protection
Bjerkandera adusta UAMH8258
-
versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation
-
industry
-
the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
industry
-
the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
industry
-
the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
industry
-
the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
synthesis
-
expression of enzyme under control of the alcohol dehydrogenase promoter of Aspergillus nidulans in this host. Culture temperature of 19°C enhances the level of peroxidase 5.8-fold and reduces the effective proteolytic activity twofold giving a peroxidase activity of 466 units per l. Application of the same conditions to expression in Aspergillus niger does not result in improved peroxidase activity, while the effective proteolytic activity is increased
synthesis
production of the oxidase in strain BL21(DE3)pLysS, cultivated at 25°C in auto-induction medium and presence of heme
synthesis
-
evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
synthesis
-
enzyme is produced by solid-state fermentation, using the agricultural residue banana peel as growth medium. An enzymatic activity of 10800 U/l i.e. 36 U/g of substrate is detected after 18 days, whereas only 1800 U/l are reached by conventional submerged fermentation with glucose-based medium
synthesis
-
evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mester, T.; Field, J.A.
Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese
J. Biol. Chem.
273
15412-15417
1998
Bjerkandera sp., Bjerkandera sp. BOS55
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 eryngii
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
Cohen, R.; Persky, L.; Hazan-Eitan, Z.; Yarden, O.; Hadar, Y.
Mn2+ alters peroxidase profiles and lignin degradation by the white-rot fungus Pleurotus ostreatus under different nutritional and growth conditions
Appl. Biochem. Biotechnol.
102-103
415-429
2002
Pleurotus ostreatus
brenda
Ruiz-Duenas, F.J.; Guillen, F.; Camarero, S.; Perez-Boada, M.; Martinez, M.J.; Martinez, A.T.
Regulation of peroxidase transcript levels in liquid cultures of the ligninolytic fungus Pleurotus eryngii
Appl. Environ. Microbiol.
65
4458-4463
1999
Pleurotus eryngii
brenda
Ruiz-Duenas, F.J.; Martinez, M.J.; Martinez, A.T.
Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates
Appl. Environ. Microbiol.
65
4705-4707
1999
Pleurotus eryngii (O94753)
brenda
Ruiz-Duenas, F.J.; Camarero, S.; Perez-Boada, M.; Martinez, M.J.; Martinez, A.T.
A new versatile peroxidase from Pleurotus
Biochem. Soc. Trans.
29
116-122
2001
Pleurotus eryngii
brenda
Pogni, R.; Baratto, M.C.; Giansanti, S.; Teutloff, C.; Verdin, J.; Valderrama, B.; Lendzian, F.; Lubitz, W.; Vazquez-Duhalt, R.; Basosi, R.
Tryptophan-based radical in the catalytic mechanism of versatile peroxidase from Bjerkandera adusta
Biochemistry
44
4267-4274
2005
Bjerkandera adusta
brenda
Verdin, J.; Pogni, R.; Baeza, A.; Baratto, M.C.; Basosi, R.; Vazquez-Duhalt, R.
Mechanism of versatile peroxidase inactivation by Ca(2+) depletion
Biophys. Chem.
121
163-170
2006
Bjerkandera adusta
brenda
Wang, Y.; Vazquez-Duhalt, R.; Pickard, M.A.
Manganese-lignin peroxidase hybrid from Bjerkandera adusta oxidizes polycyclic aromatic hydrocarbons more actively in the absence of manganese
Can. J. Microbiol.
49
675-682
2003
Bjerkandera adusta
brenda
Gomez-Toribio, V.; Martinez, A.T.; Martinez, M.J.; Guillen, F.
Oxidation of hydroquinones by the versatile ligninolytic peroxidase from Pleurotus eryngii. H2O2 generation and the influence of Mn2+
Eur. J. Biochem.
268
4787-4793
2001
Pleurotus eryngii
brenda
Camarero, S.; Ruiz-Duenas, F.J.; Sarkar, S.; Martinez, M.J.; Martinez, A.T.
The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases
FEMS Microbiol. Lett.
191
37-43
2000
Pleurotus eryngii (Q9UVP6), Pleurotus eryngii
brenda
Camarero, S.; Sarkar, S.; Ruiz-Duenas, F.J.; Martinez, M.J.; Martinez, A.T.
Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
J. Biol. Chem.
274
10324-10330
1999
Pleurotus eryngii
brenda
Pogni, R.; Baratto, M.C.; Teutloff, C.; Giansanti, S.; Ruiz-Duenas, F.J.; Choinowski, T.; Piontek, K.; Martinez, A.T.; Lendzian, F.; Basosi, R.
A tryptophan neutral radical in the oxidized state of versatile peroxidase from Pleurotus eryngii: a combined multifrequency EPR and density functional theory study
J. Biol. Chem.
281
9517-9526
2006
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Banci, L.; Camarero, S.; Martinez, A.T.; Martinez, M.J.; Perez-Boada, M.; Pierattelli, R.; Ruiz-Duenas, F.J.
NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii
J. Biol. Inorg. Chem.
8
751-760
2003
Pleurotus eryngii
brenda
Perez-Boada, M.; Ruiz-Duenas, F.J.; Pogni, R.; Basosi, R.; Choinowski, T.; Martinez, M.J.; Piontek, K.; Martinez, A.T.
Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways
J. Mol. Biol.
354
385-402
2005
Pleurotus eryngii
brenda
Tsukihara, T.; Honda, Y.; Watanabe, T.
Molecular breeding of white rot fungus Pleurotus ostreatus by homologous expression of its versatile peroxidase MnP2
Appl. Microbiol. Biotechnol.
71
114-120
2006
Pleurotus ostreatus
brenda
Ruiz-Duenas, F.J.; Morales, M.; Perez-Boada, M.; Choinowski, T.; Martinez, M.J.; Piontek, K.; Martinez, A.T.
Manganese oxidation site in Pleurotus eryngii versatile peroxidase: a site-directed mutagenesis, kinetic, and crystallographic study
Biochemistry
46
66-77
2007
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Tsukihara, T.; Honda, Y.; Sakai, R.; Watanabe, T.; Watanabe, T.
Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus
J. Biotechnol.
126
431-439
2006
Pleurotus ostreatus
brenda
Tsukihara, T.; Honda, Y.; Sakai, R.; Watanabe, T.; Watanabe, T.
Mechanism for oxidation of high-molecular-weight substrates by a fungal versatile peroxidase, MnP2
Appl. Environ. Microbiol.
74
2873-2881
2008
Pleurotus ostreatus
brenda
Ruiz-Duenas, F.J.; Morales, M.; Mate, M.J.; Romero, A.; Martinez, M.J.; Smith, A.T.; Martinez, A.T.
Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase
Biochemistry
47
1685-1695
2008
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Eibes, G.M.; Lu-Chau, T.A.; Ruiz-Duenas, F.J.; Feijoo, G.; Martinez, M.J.; Martinez, A.T.; Lema, J.M.
Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts
Bioprocess Biosyst. Eng.
32
129-134
2009
Pleurotus eryngii
brenda
Mohorcic, M.; Bencina, M.; Friedrich, J.; Jerala, R.
Expression of soluble versatile peroxidase of Bjerkandera adusta in Escherichia coli
Biores. Technol.
100
851-858
2009
Bjerkandera adusta (A5JTV4), Bjerkandera adusta
brenda
Moreira, P.R.; Almeida-Vara, E.; Malcata, F.X.; Duarte, J.C.
Lignin transformation by a versatile peroxidase from a novel Bjerkandera sp. strain
Int. Biodeter. Biodegrad.
59
234-238
2007
Bjerkandera sp.
-
brenda
Tinoco, R.; Verdin, J.; Vazquez-Duhalt, R.
Role of oxidizing mediators and tryptophan 172 in the decoloration of industrial dyes by the versatile peroxidase from Bjerkandera adusta
J. Mol. Catal. B
46
1-7
2007
Bjerkandera adusta
-
brenda
Ruiz-Duenas, F.J.; Pogni, R.; Morales, M.; Giansanti, S.; Mate, M.J.; Romero, A.; Martinez, M.J.; Basosi, R.; Martinez, A.T.
Protein radicals in fungal versatile peroxidase: catalytic tryptophan radical in both compound I and compound II and studies on W164Y, W164H, and W164S variants
J. Biol. Chem.
284
7986-7994
2009
Pleurotus eryngii (O94753), Pleurotus eryngii
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
Pleurotus eryngii (O94753)
brenda
Marques, G.; Gamelas, J.A.; Ruiz-Duenas, F.J.; del Rio, J.C.; Evtuguin, D.V.; Martinez, A.T.; Gutierrez, A.
Delignification of eucalypt kraft pulp with manganese-substituted polyoxometalate assisted by fungal versatile peroxidase
Biores. Technol.
101
5935-5940
2010
Pleurotus eryngii
brenda
Taboada-Puig, R.; Lu-Chau, T.A.; Moreira, M.T.; Feijoo, G.; Lema, J.M.
Activation of Kraft lignin by an enzymatic treatment with a versatile peroxidase from Bjerkandera sp. R1
Appl. Biochem. Biotechnol.
169
1262-1278
2013
Bjerkandera sp., Bjerkandera sp. R1
brenda
Santos, A.; Mendes, S.; Brissos, V.; Martins, L.
New dye-decolorizing peroxidases from Bacillus subtilis and Pseudomonas putida MET94: towards biotechnological applications
Appl. Microbiol. Biotechnol.
98
2053-2065
2013
Pseudomonas putida, Pseudomonas putida MET94
brenda
Garcia-Ruiz, E.; Gonzalez-Perez, D.; Ruiz-Duenas, F.J.; Martinez, A.T.; Alcalde, M.
Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase
Biochem. J.
441
487-498
2012
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Sezer, M.; Santos, A.; Kielb, P.; Pinto, T.; Martins, L.O.; Todorovic, S.
Distinct structural and redox properties of the heme active site in bacterial dye decolorizing peroxidase-type peroxidases from two subfamilies: resonance Raman and electrochemical study
Biochemistry
52
3074-3084
2013
Pseudomonas putida, Pseudomonas putida MET94
brenda
Ertan, H.; Siddiqui, K.S.; Muenchhoff, J.; Charlton, T.; Cavicchioli, R.
Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: Insight into manganese peroxidase activation and lignin peroxidase inhibition
Biochimie
94
1221-1231
2012
Bjerkandera adusta
brenda
Bao, X.; Liu, A.; Lu, X.; Li, J.J.
Direct over-expression, characterization and H2O2 stability study of active Pleurotus eryngii versatile peroxidase in Escherichia coli
Biotechnol. Lett.
34
1537-1543
2012
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Contreras, E.; Urra, J.; Vasquez, C.; Palma, C.
Detoxification of azo dyes mediated by cell-free supernatant culture with manganese-dependent peroxidase activity: effect of Mn2+ concentration and H2O2 dose
Biotechnol. Prog.
28
114-120
2012
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Pozdnyakova, N.; Makarov, O.; Chernyshova, M.; Turkovskaya, O.; Jarosz-Wilkolazka, A.
Versatile peroxidase of Bjerkandera fumosa: substrate and inhibitor specificity
Enzyme Microb. Technol.
52
44-53
2013
Bjerkandera fumosa
brenda
Singh, R.; Grigg, J.C.; Armstrong, Z.; Murphy, M.E.; Eltis, L.D.
Distal heme pocket residues of B-type dye-decolorizing peroxidase: arginine but not aspartate is essential for peroxidase activity
J. Biol. Chem.
287
10623-10630
2012
Rhodococcus jostii (Q0SE24)
brenda
Morales, M.; Mate, M.J.; Romero, A.; Martinez, M.J.; Martinez, A.T.; Ruiz-Duenas, F.J.
Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase
J. Biol. Chem.
287
41053-41067
2012
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Praveen, K.; Usha, K.Y.; Viswanath, B.; Reddy, B.R.
Kinetic properties of manganese peroxidase from the mushroom Stereum ostrea and its ability to decolorize dyes
J. Microbiol. Biotechnol.
22
1540-1548
2012
Stereum ostrea
brenda
Salame, T.; Knop, D.; Levinson, D.; Mabjeesh, S.; Yarden, O.; Hadar, Y.
Release of Pleurotus ostreatus versatile-peroxidase from Mn2+ repression enhances anthropogenic and natural substrate degradation
PLoS ONE
7
e52446
2012
Pleurotus ostreatus (Q96V56)
brenda
Taboada-Puig, R.; Lu-Chau, T.; Moreira, M.; Feijoo, G.; Martinez, M.; Lema, J.
A new strain of Bjerkandera sp. production, purification and characterization of versatile peroxidase
World J. Microbiol. Biotechnol.
27
115-122
2011
Bjerkandera sp.
brenda
Gonzalez-Perez, D.; Garcia-Ruiz, E.; Ruiz-Duenas, F.; Martinez, A.; Alcalde, M.
Structural determinants of oxidative stabilization in an evolved versatile peroxidase
ACS Catal.
4
3891-3901
2014
Pleurotus eryngii (O94753)
-
brenda
Mendez-Hernandez, J.E.; Eibes, G.; Arca-Ramos, A.; Lu-Chau, T.A.; Feijoo, G.; Moreira, M.T.; Lema, J.M.
Continuous removal of nonylphenol by versatile peroxidase in a two-stage membrane bioreactor
Appl. Biochem. Biotechnol.
175
3038-3047
2015
Bjerkandera sp., Bjerkandera sp. R1
brenda
Knop, D.; Levinson, D.; Makovitzki, A.; Agami, A.; Lerer, E.; Mimran, A.; Yarden, O.; Hadar, Y.
Limits of versatility of versatile peroxidase
Appl. Environ. Microbiol.
82
4070-4080
2016
Pleurotus ostreatus, Pleurotus ostreatus PC9
brenda
Taboada-Puig, R.; Lu-Chau, T.A.; Eibes, G.; Feijoo, G.; Moreira, M.T.; Lema, J.M.
Continuous removal of endocrine disruptors by versatile peroxidase using a two-stage system
Biotechnol. Prog.
31
908-916
2015
Bjerkandera adusta, Bjerkandera adusta ATCC 90940
brenda
Ravichandran, A.; Sridhar, M.
Insights into the mechanism of lignocellulose degradation by versatile peroxidases
Curr. Sci.
113
35-42
2017
Bjerkandera adusta, Pleurotus eryngii, Pleurotus ostreatus, Bjerkandera fumosa
-
brenda
Imami, A.; Riemer, S.; Schulze, M.; Amelung, F.; Gorshkov, V.; Ruehl, M.; Ammenn, J.; Zorn, H.
Depolymerization of lignosulfonates by submerged cultures of the basidiomycete Irpex consors and cloning of a putative versatile peroxidase
Enzyme Microb. Technol.
81
8-15
2015
Cerrena consors
brenda
Siddiqui, K.S.; Ertan, H.; Charlton, T.; Poljak, A.; Daud Khaled, A.K.; Yang, X.; Marshall, G.; Cavicchioli, R.
Versatile peroxidase degradation of humic substances use of isothermal titration calorimetry to assess kinetics, and applications to industrial wastes
J. Biotechnol.
178
1-11
2014
Bjerkandera adusta
brenda
Schttmann, I.; Bouws, H.; Szweda, R.; Suckow, M.; Czermak, P.; Zorn, H.
Induction, characterization, and heterologous expression of a carotenoid degrading versatile peroxidase from Pleurotus sapidus
J. Mol. Catal. B
103
79-84
2014
Pleurotus sapidus (Q4QZ27)
-
brenda
Saez-Jimenez, V.; Fernandez-Fueyo, E.; Medrano, F.J.; Romero, A.; Martinez, A.T.; Ruiz-Duenas, F.J.
Improving the pH-stability of versatile peroxidase by comparative structural analysis with a naturally-stable manganese peroxidase
PLoS ONE
10
e0140984
2015
Pleurotus eryngii (O94753), Pleurotus eryngii
brenda
Palma, C.; Lloret, L.; Sepulveda, L.; Contreras, E.
Production of versatile peroxidase from Pleurotus eryngii by solid-state fermentation using agricultural residues and evaluation of its catalytic properties
Prep. Biochem. Biotechnol.
46
200-207
2016
Pleurotus eryngii
brenda
Vignali, E.; Tonin, F.; Pollegioni, L.; Rosini, E.
Characterization and use of a bacterial lignin peroxidase with an improved manganese-oxidative activity
Appl. Microbiol. Biotechnol.
102
10579-10588
2018
Rhodococcus jostii (Q0SE24)
brenda
Gonzalez-Perez, D.; Alcalde, M.
The making of versatile peroxidase by directed evolution
Biocatal. Biotransform.
36
1-11
2018
Pleurotus eryngii (O94753)
-
brenda
Ravichandran, A.; Rao, R.G.; Thammaiah, V.; Gopinath, S.M.; Sridhar, M.
A versatile peroxidase from Lentinus squarrosulus towards enhanced delignification and in vitro digestibility of crop residues
BioResources
14
5132-5149
2019
Lentinus squarrosulus, Lentinus squarrosulus TAMI004
-
brenda
Ravichandran, A.; Rao, R.G.; Gopinath, S.M.; Sridhar, M.
Augmenting versatile peroxidase production from Lentinus squarrosulus and its role in enhancing ruminant feed
BioResources
16
1600-1615
2021
Lentinus squarrosulus, Lentinus squarrosulus 12292 ITS
-
brenda
Mannino, M.H.; Patel, R.S.; Eccardt, A.M.; Perez Magnelli, R.A.; Robinson, C.L.C.; Janowiak, B.E.; Warren, D.E.; Fisher, J.S.
Myoglobin as a versatile peroxidase implications for a more important role for vertebrate striated muscle in antioxidant defense
Comp. Biochem. Physiol. B
234
9-17
2019
Mus musculus (P04247), Equus caballus (P68082), Equus caballus
brenda
Sanchez-Alejandro, F.; Baratto, M.C.; Basosi, R.; Graeve, O.; Vazquez-Duhalt, R.
Addition of new catalytic sites on the surface of versatile peroxidase for enhancement of LRET catalysis
Enzyme Microb. Technol.
131
109429
2019
Bjerkandera adusta (Q3SC77), Bjerkandera adusta
brenda
Durdic, K.I.; Ostafe, R.; Durdevic Delmas, A.; Popovic, N.; Schillberg, S.; Fischer, R.; Prodanovic, R.
Saturation mutagenesis to improve the degradation of azo dyes by versatile peroxidase and application in form of VP-coated yeast cell walls
Enzyme Microb. Technol.
136
109509
2020
Pleurotus eryngii (Q9UVP6), Pleurotus eryngii
brenda
Liu, J.; Zhang, S.; Shi, Q.; Wang, L.; Kong, W.; Yu, H.; Ma, F.
Highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
Int. Biodeter. Biodegrad.
136
41-48
2019
Physisporinus vitreus, Physisporinus vitreus PF18
-
brenda
Zavarzina, A.G.; Lisov, A.V.; Leontievsky, A.A.
The role of ligninolytic enzymes laccase and a versatile peroxidase of the white-rot fungus Lentinus tigrinus in biotransformation of soil humic matter comparative in vivo study
J. Geophys. Res.
123
2727-2742
2018
Lentinus tigrinus, Lentinus tigrinus VKM F-160
-
brenda
Hernandez-Bueno, N.S.; Suarez-Rodrguez, R.; Balcazar-Lopez, E.; Folch-Mallol, J.L.; Ramirez-Trujillo, J.A.; Iturriaga, G.
A versatile peroxidase from the fungus Bjerkandera adusta confers abiotic stress tolerance in transgenic tobacco plants
Plants (Basel)
10
859
2021
Bjerkandera adusta (Q3SC77), Bjerkandera adusta, Bjerkandera adusta UAMH8258 (Q3SC77)
brenda
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