Any feedback?
Information on EC 1.14.13.50 - pentachlorophenol monooxygenase
for references in articles please use BRENDA:EC1.14.13.50Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.13.50 pentachlorophenol monooxygenaseIUBMB Comments
A flavoprotein (FAD). The enzyme displaces a diverse range of substituents from the 4-position of polyhalogenated phenols but requires that a halogen substituent be present at the 2-position . If C-4 carries a halogen substituent, reaction 1 is catalysed; if C-4 is unsubstituted, reaction 2 is catalysed.
Specify your search results
Word Map
- 1.14.13.50
-
pcp-degrading
- flavobacterium
-
sphingobium
- chlorophenolicum
- tetrachlorohydroquinone
-
bioremediation
- tetrachlorobenzoquinone
-
dehalogenation
- environmental protection
- arthrobacter
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
pcp hydroxylase, pcp-4-monooxygenase, pentachlorophenol-4-monooxygenase, pentachlorophenol 4-monooxygenase, pcp4mo, pentachlorophenol hydroxylase, pcp 4-monooxygenase, phe4mo, pcp-monooxygenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dechlorinase, pentachlorophenol
-
-
-
-
GM610_18120
oxygenase, pentachlorophenol 4-mono-
-
-
-
-
PCP 4-monooxygenase
PCP hydroxylase
PCP-4-monooxygenase
PcpB
pentachlorophenol 4-mono-oxygenase
-
-
-
-
pentachlorophenol 4-monooxygenase
pentachlorophenol dechlorinase
-
-
-
-
pentachlorophenol dehalogenase
-
-
-
-
pentachlorophenol hydroxylase
pentachlorophenol-4-monooxygenase
Phe4MO
PCP hydroxylase
-
-
-
-
pentachlorophenol 4-monooxygenase
-
-
-
-
pentachlorophenol hydroxylase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O
-
-
-
-
pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
mechanism
-
pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
benzene rings of Phe85, Phe87, Tyr397, as well as Tyr216 and the positive charge of Arg235 are important for activity and stabilization of the active site, reaction mechanism
-
pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
direct reduction by NADPH of the flavin at the active site without requirement of intermediate formation
-
pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
tetrachlorobenzoquinone reductase PcpD reaction mechanism
-
pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehalogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating)
A flavoprotein (FAD). The enzyme displaces a diverse range of substituents from the 4-position of polyhalogenated phenols but requires that a halogen substituent be present at the 2-position [2]. If C-4 carries a halogen substituent, reaction 1 is catalysed; if C-4 is unsubstituted, reaction 2 is catalysed.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
124148-88-5
-
136111-57-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
2,3,4,5-tetrachlorophenol + NADPH + O2
2,3,5-trichlorohydroquinone + Cl- + NADP+ + H2O
-
-
-
-
?
2,3,5,6-tetrachlorophenol + 2 NADPH + H+ + O2
2,3,5,6-tetrachloro-p-hydroquinone + 2 NADP+ + chloride + H2O
-
-
-
-
?
2,3,5,6-tetrachlorophenol + NADPH + O2
2,3,5,6-tetrachloro-p-hydroquinone + NADP+
-
-
-
?
2,3,6-trichlorophenol + NADPH + O2
2,3,6-trichloro-p-hydroquinone + NADP+ + H2O
-
-
-
?
2,4,6-tribromophenol + NADPH + O2
2,6-dibromo-p-hydroquinone + Br- + NADP+ + H2O
-
low activity
-
?
2,6-dibromo-4-nitrophenol + NADPH + O2
2,6-dibromo-p-hydroquinone + NO2- + NADP+ + H2O
-
low activity
-
?
2,6-dibromophenol + NADPH + O2
2,6-dibromo-p-hydroquinone + NADP+ + H2O
-
-
-
?
2,6-dichlorophenol + NADPH + H+ + O2
2,6-dichloro-p-hydroquinone + NADP+ + H2O
-
-
-
-
?
2,6-dichlorophenol + NADPH + O2
2,6-dichloro-p-hydroquinone + NADP+ + H2O
-
-
-
?
3,4,5-trichlorophenol + 2 NADPH + H+ + O2
3,5-dichloro-p-hydroquinone + 2 NADP+ + chloride + H2O
-
-
-
-
?
3,5-dibromo-4-hydroxybenzonitrile + 2 NADPH + 2 H+ + O2
2,6-dibromo-p-hydroquinone + CN- + 2 NADP+ + H2O
-
-
-
?
3,5-dichlorophenol + NADPH + H+ + O2
3,5-dichloro-p-hydroquinone + NADP+ + H2O
-
-
-
-
?
4-amino-2,6-dichlorophenol + NADPH + O2
2,6-dichloro-p-hydroquinone + NADP+ + NH2OH
-
low activity
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorobenzoquinone + 2 NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + chloride + H2O
-
product is not tetrachlorobenzoquinone as previously thought, ethyl acetate and glutathione can shift the redox-equilibrium in favor of tetrachlorobenzoquinone, room temperature (23-25°C), 50 mM phosphate buffer, pH 7.0, while with NADPH tetrachlorobenzoquinone is reduced to tetrachlorohydroquinone (with 0.5-1 mol NADPH/mol tetrachlorobenzoquinone 50-65% are reduced, with 2.5 mol or more almost complete reduction occurs), deionized distilled water, pH 6.8 (due to interference of phosphate or Tris-HCl buffer with the detection of tetrachlorohydroquinone)
-
?
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NAD+ + chloride + H2O
-
-
-
-
r
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
2,4,6-trichlorophenol + NADPH + O2
2,6-dichloro-p-hydroquinone + Cl- + NADP+ + H2O
-
-
-
-
?
2,4,6-trichlorophenol + NADPH + O2
2,6-dichloro-p-hydroquinone + Cl- + NADP+ + H2O
-
low activity
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
-
-
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
wild-type and transformed E. coli cells
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
-
solitary oxygenolytic pathway for removal of the primary chlorine during PCP degradation, not a hydrolytic one
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
-
wild-type and mutant strains
-
?
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
Bacillus tropicus AOA-CPS1
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
degradation of pentachlorophenol
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
the enzyme is an unusually slow flavin-dependent monooxygenase (kcat = 0.02/s) that converts pentachlorophenol to a highly reactive product, tetrachlorobenzoquinone. By stopped-flow spectroscopy, it is shown that the steps up to and including formation of tetrachlorobenzoquinone are rapid (5-30/s). Before products can be released from the active site, the strongly oxidizing tetrachlorobenzoquinone abstracts an electron from a donor at the active site, possibly a cysteine residue, resulting in an off-pathway diradical state that only slowly reverts to an intermediate capable of completing the catalytic cycle
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
oxygen and NADPH are essential
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
initial enzyme in the PCP catabolic pathway of numerous sphingomonads, PCP-4-monooxygenase (PcpB), catalyzes the parahydroxylation of PCP to tetrachlorohydroquinone, pentachlorophenol degradation pathway, overview
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
initial enzyme in the PCP catabolic pathway of numerous sphingomonads, PCP-4-monooxygenase (PcpB), catalyzes the parahydroxylation of PCP to tetrachlorohydroquinone, pentachlorophenol degradation pathway, overview
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
initial enzyme in the PCP catabolic pathway of numerous sphingomonads, PCP-4-monooxygenase (PcpB), catalyzes the parahydroxylation of PCP to tetrachlorohydroquinone, pentachlorophenol degradation pathway, overview
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
?
pentachlorophenol + NADPH + H+ + O2
tetrachlorobenzoquinone + NADP+ + chloride + H2O
-
-
-
-
ir
pentachlorophenol + NADPH + H+ + O2
tetrachlorobenzoquinone + NADP+ + chloride + H2O
-
first step of pentachlorophenol degradation pathway
-
-
ir
pentachlorophenol + NADPH + H+ + O2
tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
tetrachlorohydroquinone + NADP+ + chloride + H2O
-
pentachlorophenol degradation
-
-
?
pentachlorophenol + NADPH + H+ + O2
tetrachlorohydroquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
tetrachlorohydroquinone + NADP+ + chloride + H2O
-
pentachlorophenol degradation
-
-
?
tetrachlorobenzoquinone + NADPH
tetrachlorohydroquinone + NADP+
-
-
-
-
?
tetrachlorobenzoquinone + NADPH
tetrachlorohydroquinone + NADP+
-
second step in pentachlorophenol degradation, physiological role in association with pentachloro monooxygenase, overview
-
-
?
triiodophenol + NADPH + O2
diiodohydroquinone + iodide + NADP+ + H2O
-
-
-
-
?
triiodophenol + NADPH + O2
diiodohydroquinone + iodide + NADP+ + H2O
-
-
-
?
additional information
?
-
-
no activity with 3,4,5-trichlorophenol, 2,4-dichlorophenol, 3,4-dichlorophenol, 4-chlorophenol
-
-
?
additional information
?
-
-
enzyme CpsB from Bacillus tropicus reacts with PCP to trap 1,4-tetrachlorobenzoquinone (Tet-CBQ) formed as 2,3,5,6-tetrakis[(2-hydroxyethyl)thio]-1,4-hydroquinone (THTH)
-
-
-
additional information
?
-
Bacillus tropicus AOA-CPS1
-
enzyme CpsB from Bacillus tropicus reacts with PCP to trap 1,4-tetrachlorobenzoquinone (Tet-CBQ) formed as 2,3,5,6-tetrakis[(2-hydroxyethyl)thio]-1,4-hydroquinone (THTH)
-
-
-
additional information
?
-
-
broad substrate specificity, hydroxylation in para-position
-
-
?
additional information
?
-
enzyme also removes amino, cyano and nitro groups from the para-position to the hydroxyl group of the phenol
-
-
?
additional information
?
-
-
enzyme also removes amino, cyano and nitro groups from the para-position to the hydroxyl group of the phenol
-
-
?
additional information
?
-
-
overview: enzyme catalyzes a primary attack on a broad range of substituted phenols, hydroxylating the para position and removing halogen, nitro, amino and cyano groups to produce halide, nitrite, hydroxylamine and cyanide respectively
-
-
?
additional information
?
-
-
no activity with 3,4,5-trichlorophenol, 3,5-dichlorophenol
-
-
?
additional information
?
-
-
broad substrate and catalytic reaction range
-
-
?
additional information
?
-
-
biodegradation of the herbicide bromoxynil, i.e. 3,5-dibromo-4-hydroxybenzonitrile
-
-
?
additional information
?
-
-
lateral gene transfer and the origin of the pentachlorophenol pathway, overview
-
-
?
additional information
?
-
-
enzyme expression in response to pentachlorophenol hydroxylase PcpB
-
-
?
additional information
?
-
-
lateral gene transfer and the origin of the pentachlorophenol pathway, overview
-
-
?
additional information
?
-
-
enzyme exhibits substantial uncoupling. The C4a-hydroxyflavin intermediate, instead of hydroxylating the substrate, can decompose to produce H2O2 in a futile cycle that consumes NADPH. The extent of uncoupling varies from 0 to 100% with different substrates. The extent of uncoupling is increased by the presence of bulky substituents at position 3, 4, or 5 and decreased by the presence of a chlorine in the ortho position. The effectiveness of pentachlorophenol hydroxylase is additionally hindered by its promiscuous activity with tetrachlorohydroquinone, a downstream metabolite in the degradation pathway. The conversion of tetrachlorohydroquinone to tetrachlorobenzoquinone reverses flux through the pathway. Substantial uncoupling also occurs during the reaction with tetrachlorohydroquinone
-
-
?
additional information
?
-
broad substrate specificity, hydroxylation in para-position
-
-
?
additional information
?
-
-
lateral gene transfer and the origin of the pentachlorophenol pathway, overview
-
-
?
additional information
?
-
broad substrate specificity, hydroxylation in para-position
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
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
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + chloride + H2O
-
product is not tetrachlorobenzoquinone as previously thought, ethyl acetate and glutathione can shift the redox-equilibrium in favor of tetrachlorobenzoquinone, room temperature (23-25°C), 50 mM phosphate buffer, pH 7.0, while with NADPH tetrachlorobenzoquinone is reduced to tetrachlorohydroquinone (with 0.5-1 mol NADPH/mol tetrachlorobenzoquinone 50-65% are reduced, with 2.5 mol or more almost complete reduction occurs), deionized distilled water, pH 6.8 (due to interference of phosphate or Tris-HCl buffer with the detection of tetrachlorohydroquinone)
-
?
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
degradation of pentachlorophenol
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
tetrachlorobenzoquinone + NADPH
tetrachlorohydroquinone + NADP+
-
second step in pentachlorophenol degradation, physiological role in association with pentachloro monooxygenase, overview
-
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
-
-
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
wild-type and transformed E. coli cells
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
-
solitary oxygenolytic pathway for removal of the primary chlorine during PCP degradation, not a hydrolytic one
-
?
pentachlorophenol + 2 NADPH + H+ + O2
tetrachlorohydroquinone + 2 NADP+ + Cl- + H2O
-
wild-type and mutant strains
-
?
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
-
-
-
-
?
pentachlorophenol + NADH + H+ + O2
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O
Bacillus tropicus AOA-CPS1
-
-
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
initial enzyme in the PCP catabolic pathway of numerous sphingomonads, PCP-4-monooxygenase (PcpB), catalyzes the parahydroxylation of PCP to tetrachlorohydroquinone, pentachlorophenol degradation pathway, overview
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
initial enzyme in the PCP catabolic pathway of numerous sphingomonads, PCP-4-monooxygenase (PcpB), catalyzes the parahydroxylation of PCP to tetrachlorohydroquinone, pentachlorophenol degradation pathway, overview
-
-
?
pentachlorophenol + NADPH + H+ + O2
2,3,5,6-tetrachlorohydroquinone + NADP+ + chloride + H2O
-
initial enzyme in the PCP catabolic pathway of numerous sphingomonads, PCP-4-monooxygenase (PcpB), catalyzes the parahydroxylation of PCP to tetrachlorohydroquinone, pentachlorophenol degradation pathway, overview
-
-
?
pentachlorophenol + NADPH + H+ + O2
tetrachlorobenzoquinone + NADP+ + chloride + H2O
-
-
-
-
ir
pentachlorophenol + NADPH + H+ + O2
tetrachlorobenzoquinone + NADP+ + chloride + H2O
-
first step of pentachlorophenol degradation pathway
-
-
ir
pentachlorophenol + NADPH + H+ + O2
tetrachlorohydroquinone + NADP+ + chloride + H2O
-
pentachlorophenol degradation
-
-
?
pentachlorophenol + NADPH + H+ + O2
tetrachlorohydroquinone + NADP+ + chloride + H2O
-
pentachlorophenol degradation
-
-
?
additional information
?
-
-
biodegradation of the herbicide bromoxynil, i.e. 3,5-dibromo-4-hydroxybenzonitrile
-
-
?
additional information
?
-
-
lateral gene transfer and the origin of the pentachlorophenol pathway, overview
-
-
?
additional information
?
-
-
enzyme expression in response to pentachlorophenol hydroxylase PcpB
-
-
?
additional information
?
-
-
lateral gene transfer and the origin of the pentachlorophenol pathway, overview
-
-
?
additional information
?
-
-
lateral gene transfer and the origin of the pentachlorophenol pathway, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
dithiothreitol can not be used as electron donor
-
FAD
-
recombinant enzyme has no FAD, activity only in presence of added FAD
NADPH
-
2 mol of NADPH per mol of halogenated substrate, preferred electron donor
NADPH
-
elimination of 1 mol of a halogen, nitro, or cyano group requires 2 mol of NADPH, 1 mol of NADPH is required to remove 1 mol of an amino group or hydrogen
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe3+
-
the catalytic active site of the enzyme has a Fe metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214. Fe3+ does not activate the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tetrachlorobenzoquinone
-
inactivates the enzyme, feedback control
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
pentachlorphenol induces enzyme expression
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
Pentachlorophenol
-
pH 7.0, 25°C, recombinant wild-type enzyme
0.0008
Pentachlorophenol
-
pH 7.0, 25°C, recombinant mutant R235K
0.0029
Pentachlorophenol
-
pH 7.0, 25°C, recombinant mutant Y39F
0.0045
Pentachlorophenol
-
pH 7.0, 25°C, recombinant mutant Y216F
additional information
additional information
-
the enzyme-substrate reaction kinetic studies show the allosteric nature of the enzyme and follow pre-steady state using NADH as a co-substrate. Steady-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9300
Pentachlorophenol
-
pH 7.0, 25°C, recombinant wild-type enzyme
15200
Pentachlorophenol
-
pH 7.0, 25°C, recombinant mutant R235K
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity in crude extracts is undetectable or below the detection limit of 0.1 nU per mg with a chloride sensor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11.5
-
10% of maximal activity at pH 5.0, 25% of maximal activity at pH 6.0, about 10% of maximal activity at pH 11.5, inactive at at pH 12-13
6 - 8.5
-
pH 6.0: about 28% of activity maximum, pH 7.5-8.5: activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 45
-
40°C: activity maximum, 45°C: above 75% of activity maximum, 50°C: inactive
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
identical with Sphingomonas chlorophenolica strain ATCC 39723
-
-
brenda
i.e. Pseudomonas sp. RA2 and Pseudomonas sp. SR3, and Arthrobacter sp. strain ATCC 33790, gene pcpB
-
-
brenda
strain ATCC 39723, formerly Flavobacterium and Sphingomonas, gene pcpB
-
-
brenda
strain RA-2, strain ATCC 39723, gene pcpD immediately downstream of gene pcpB
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme is synthesized in the cytoplasm, then integrated in the inner membranes and finally translocated to the periplasm
brenda
-
enzyme is synthesized in the cytoplasm, then integrated in the inner membranes and finally translocated to the periplasm
brenda
-
enzyme is synthesized in the cytoplasm, then integrated in the inner membranes and finally translocated to the periplasm
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the Bacillus cereus group in the Phe4MO superfamily, sequence comparisons and phylogenetic analysis
evolution
Bacillus tropicus AOA-CPS1
-
the enzyme belongs to the Bacillus cereus group in the Phe4MO superfamily, sequence comparisons and phylogenetic analysis
-
metabolism
hydroxylation of pentachlorophenol in the pentachlorophenol biodegradation pathway
metabolism
-
the first step in the PCP degradation pathway is the rate-limiting step involving the hydroxylation of PCP to 1,4-tetrachlorobenzoquinone (Tet-CBQ). The reaction is catalysed by the enzyme PCP 4-monooxygenase (PcpB) in bacteria and cytochrome p450 monooxygenase in fungus. Phe4MO also plays a critical role in xenobiotic compound degradation and lipid metabolism
metabolism
-
two pathways are proposed for pentachlorophenol (PCP) transformation in BtAOA. In the first pathway, 2,6-bis(1,1-dimethylethyl)phenol, 1-methoxy-5-trimetylsilyoxyhexane, trimethylsilyl 2-butoxyacetate and methyl 2-hydroxyl-3-methylbutanoate fragments are found. The metabolites detected for the proposed second pathway include 1,3-dimethyl-4,6-diisopropylbenzene, 2,4-dimethylbenzenecarboxaldehyde and 2,5-dimethylbenzaldehyde. Both 2,6-di-tert-butylbenzoquinone and 1,3-dimethyl-4,6-diisopropylbenzene cannot be metabolites from the same pathway, it could be that, one of the pathways is initiated by PcpB and the other by cytochrome P450 monooxygenase. Metabolic reconstruction of BtAOA xenobiotics biodegradation pathways, pathway regulation analysis, overview
metabolism
Bacillus tropicus AOA-CPS1
-
the first step in the PCP degradation pathway is the rate-limiting step involving the hydroxylation of PCP to 1,4-tetrachlorobenzoquinone (Tet-CBQ). The reaction is catalysed by the enzyme PCP 4-monooxygenase (PcpB) in bacteria and cytochrome p450 monooxygenase in fungus. Phe4MO also plays a critical role in xenobiotic compound degradation and lipid metabolism
-
metabolism
Bacillus tropicus AOA-CPS1
-
two pathways are proposed for pentachlorophenol (PCP) transformation in BtAOA. In the first pathway, 2,6-bis(1,1-dimethylethyl)phenol, 1-methoxy-5-trimetylsilyoxyhexane, trimethylsilyl 2-butoxyacetate and methyl 2-hydroxyl-3-methylbutanoate fragments are found. The metabolites detected for the proposed second pathway include 1,3-dimethyl-4,6-diisopropylbenzene, 2,4-dimethylbenzenecarboxaldehyde and 2,5-dimethylbenzaldehyde. Both 2,6-di-tert-butylbenzoquinone and 1,3-dimethyl-4,6-diisopropylbenzene cannot be metabolites from the same pathway, it could be that, one of the pathways is initiated by PcpB and the other by cytochrome P450 monooxygenase. Metabolic reconstruction of BtAOA xenobiotics biodegradation pathways, pathway regulation analysis, overview
-
physiological function
-
efficient degradation of pentachlorophenol (PCP) and involvement of different genes and enzymes in the degradation pathway in Bacillus tropicus strain AOA-CPS1
physiological function
Bacillus tropicus AOA-CPS1
-
efficient degradation of pentachlorophenol (PCP) and involvement of different genes and enzymes in the degradation pathway in Bacillus tropicus strain AOA-CPS1
-
additional information
-
enzyme homology structure modeling using PDB IDs 4Q3W and 4JPY individually as templates, overview. The catalytic active site of the enzyme has a Fe3+ metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214
additional information
Bacillus tropicus AOA-CPS1
-
enzyme homology structure modeling using PDB IDs 4Q3W and 4JPY individually as templates, overview. The catalytic active site of the enzyme has a Fe3+ metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214
-
Show AA Sequence and Transmembrane Helices (821 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63000
-
1 * 63000, SDS-PAGE, under certain conditions dimer and multimer conformations are also observed
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 62600-62750, about, native wild-type enzyme, and recombinant wild-type and mutant enzymes, overview
monomer
-
1 * 63000, SDS-PAGE, under certain conditions dimer and multimer conformations are also observed
additional information
-
the predicted enzyme secondary structure comprises 290 residues of betaalphabeta motifs, 2 beta-sheets, 1 beta-hairpins, 6 strands, 15 alpha-helixes, 24 helix-helix interactions and 25 beta-turns
additional information
Bacillus tropicus AOA-CPS1
-
the predicted enzyme secondary structure comprises 290 residues of betaalphabeta motifs, 2 beta-sheets, 1 beta-hairpins, 6 strands, 15 alpha-helixes, 24 helix-helix interactions and 25 beta-turns
-
additional information
-
homology modeling and model building of three-dimensional structure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F223A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
F225A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
F85A
F87A
-
site-directed mutagenesis, mutant enzyme is nearly not soluble in contrast to the wild-type, highly reduced activity compared to the wild-type enzyme
moe
-
construction of an allelic exchange mutant and a pcpD knockout mutant strains, the latter show reduced activity at high pentachlorophenol concentrations, not at low concentrations
R235A
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
R235E
R235K
Y216A
Y216F
-
site-directed mutagenesis, 60% decreased activity compared to the wild-type enzyme
Y397A
Y397F
additional information
F85A
-
site-directed mutagenesis, 60% decreased activity compared to the wild-type enzyme
F85A
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
R235E
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R235E
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
R235K
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
R235K
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
R235K
-
site-directed mutagenesis, mutant enzyme is nearly not soluble in contrast to the wild-type, reduced activity compared to the wild-type enzyme
Y216A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Y216A
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
Y397A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Y397A
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
Y397F
-
site-directed mutagenesis, 60% increased activity compared to the wild-type enzyme
Y397F
-
site-directed mutagenesis, determination of molecular weight and comparison to wild-type enzyme
additional information
-
introduction of tobacco etch virus protease cleavage site into the enzyme as a glutathione-S-transferase fusion protein
additional information
-
targeted mutagenesis via allelic exchange, construction of isogenic mutant without PCP 4-monooxygenase activity and 2 cointegration mutants with slow activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, as ammonium sulfate precipitate or in solution at concentration greater than 1 mg/ml, 2 months
-
4°C, in cell extract or as 40-60% fraction of ammonium sulfate precipitation, total loss of activity after 3 days
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
frozen pellet of cell culture is suspended in lysis buffer (50 mM Tris-HCl, pH 7.7, 025 mM phenylmethanesulfonyl fluoride, 1 microM pepstatin A, lysozyme), cells disrupted by sonication, centrifuged, supernatant purified by affinity chromatography, mixed with Ni-NTA agarose medium, washed, packed into a column, eluted, active fractions combined and stored in buffer (20 mM phosphate buffer, pH 7.0, 0.25 mM phenylmethanesulfonyl fluoride, 5% glycerol)
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant enzyme from Pseudomonas aeruginosa to over 95% homogeneity by nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
recombinant wild-type and mutant from Escherichia coli as glutathione-S-transferase fusion proteins
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
analogues of PCP catabolic genes (cpsABCDE, and p450) are successfully amplified from the whole genome of BtAOA using the primers designed based on the gene sequences retrieved from the whole genome annotation data submitted at NCBI
-
DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
Escherichia coli M15 overexpressing recombinant hexahistidine-tagged pentachlorophenol 4-monooxygenase
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene isolated from Pseudomonas sp. plasmid, recombinant expression in Escherichia coli XLBlue1alpha, DNA sequence analysis of the recombinant clones, comparison with other sequences
-
gene pcpB, DNA and amino acid sequence analysis, phylogenetic analysis
gene pcpD, expression as C-terminally His12-tagged protein in Pseudomonas aeruginosa strain PAO1-Lac
-
pcpB gene, constitutive overexpression in Escherichia coli, DNA sequence determination and analysis
pcpB gene, expression in Escherichia coli and Flavobacterium sp. ATCC 39723 of wild-type and isogenic mutant, DNA sequence analysis
-
pcpB gene, expression in Escherichia coli BL21, DNA sequence analysis
pcpB gene, expression of wild-type and mutant in Escherichia coli as glutathione-S-transferase fusion protein
-
sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene pcpB, DNA and amino acid sequence analysis, phylogenetic analysis
-
gene pcpB, DNA and amino acid sequence analysis, phylogenetic analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
pentachlorophenol is a chloroaromatic pesticide used to protect lumber, and an environmental pollutant, Sphingobium chlorophenolicum is a microorganism that can degrade the agent to 3-oxoadipate using 5 catalytic enzymes, pentachlorophenol 4-monooxygenase catalyzes the first and rate-limiting step
environmental protection
additional information
environmental protection
-
PCP-decontamination of soil and water, degradation of 3,5-dibromophenol derived in soil from the herbicide bromoxynil, i.e. 3,5-dibromo-4-hydroxybenzonitrile
environmental protection
-
development of biological methods for the decontamination of halophenol-polluted sites
environmental protection
bioaugmentation of groundwater with known Sphingobium chlorophenolicum L-1, amendment of nutrients, and air sparging result in an enhanced degradation of pentachlorophenol and hence bioremediation of PCP-contaminated groundwater. The amendments to the site undergoing air sparging may result in more effective and less time-consuming bioremediation of pentachlorophenol-contaminated groundwater without adding significantly high cost and labor
environmental protection
-
bioaugmentation of groundwater with known Sphingobium chlorophenolicum L-1, amendment of nutrients, and air sparging result in an enhanced degradation of pentachlorophenol and hence bioremediation of PCP-contaminated groundwater. The amendments to the site undergoing air sparging may result in more effective and less time-consuming bioremediation of pentachlorophenol-contaminated groundwater without adding significantly high cost and labor
-
additional information
-
the enzyme can be used for development of a model system for the study of recent evolution of catabolic pathways among bacteria that degrade xenobiotic molecules introduced into the environment during the recent past
additional information
-
the enzyme can be used for development of a model system for the study of recent evolution of catabolic pathways among bacteria that degrade xenobiotic molecules introduced into the environment during the recent past
additional information
-
the enzyme can be used for development of a model system for the study of recent evolution of catabolic pathways among bacteria that degrade xenobiotic molecules introduced into the environment during the recent past
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schenk, T.; Muller, R.; Mrsberger, F.; Otto, M.K.; Lingens, F.
Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790
J. Bacteriol.
171
5487-5491
1989
Arthrobacter sp.
brenda
Schenk, T.; Muller, R.; Lingens, F.
Mechanism of enzymatic dehalogenation of pentachlorophenol by Arthrobacter sp. strain ATCC 33790
J. Bacteriol.
172
7272-7274
1990
Arthrobacter sp.
brenda
Xun, L.; Orser, C.S.
Purification and properties of pentachlorophenol hydroxylase, a flavoprotein from Flavobacterium sp. strain ATCC 39723 [published erratum appears in J Bacteriol 1992 Aug;174(15):5176]
J. Bacteriol.
173
4447-4453
1991
Flavobacterium sp.
brenda
Xun, L.; Topp, E.; Orser, C.S.
Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries
J. Bacteriol.
174
2898-2902
1992
Flavobacterium sp.
brenda
Topp, E.; Xun, L.; Orser, C.S.
Biodegradation of the herbicide bromoxynil (3,5-dibromo-4-hydroxybenzonitrile) by purified pentachlorophenol hydroxylase and whole cells of Flavobacterium sp. strain ATCC 39723 is accompanied by cyanogenesis
Appl. Environ. Microbiol.
58
502-506
1992
Flavobacterium sp.
brenda
Leung, K.T.; Campbell, S.; Gan, Y.; White, D.C.; Lee, H.; Trevors, J.T.
The role of the Sphingomonas species UG30 pentachlorophenol-4-monooxygenase in p-nitrophenol degradation
FEMS Microbiol. Lett.
173
247-253
1999
Flavobacterium sp., Sphingomonas sp. (O68977), Sphingomonas sp. UG30 (O68977)
brenda
Orser, C.S.; Lange, C.C.; Xun, L.; Zahrt, T.C.; Schneider, B.J.
Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli
J. Bacteriol.
175
411-416
1993
Flavobacterium sp. (P42535), Flavobacterium sp.
brenda
Lange, C.C.; Schneider, B.J.; Orser, C.S.
Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723
Biochem. Biophys. Res. Commun.
219
146-149
1996
Flavobacterium sp.
brenda
Wang, H.; Tiirola, M.A.; Puhakka, J.A.; Kulomaa, M.S.
Production and characterization of the recombinant Sphingomonas chlorophenolica pentachlorophenol 4-monooxygenase
Biochem. Biophys. Res. Commun.
289
161-166
2001
Flavobacterium sp.
brenda
Wang, H.; Marjomaki, V.; Ovod, V.; Kulomaa, M.S.
Subcellular localization of pentachlorophenol 4-monooxygenase in Sphingobium chlorophenolicum ATCC 39723
Biochem. Biophys. Res. Commun.
299
703-709
2002
Flavobacterium sp.
brenda
Thakur, I.S.; Verma, P.; Upadhayaya, K.
Molecular cloning and characterization of pentachlorophenol-degrading monooxygenase genes of Pseudomonas sp. from the chemostat
Biochem. Biophys. Res. Commun.
290
770-774
2002
Pseudomonas sp., Pseudomonas sp. IST 103
brenda
Nakamura, T.; Motoyama, T.; Hirono, S.; Yamaguchi, I.
Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase
Biochim. Biophys. Acta
1700
151-159
2004
Sphingobium chlorophenolicum
brenda
Nakamura, T.; Motoyama, T.; Hirokawa, T.; Hirono, S.; Yamaguchi, I.
Computer-aided modeling of pentachlorophenol 4-monooxygenase and site-directed mutagenesis of its active site
Chem. Pharm. Bull.
51
1293-1298
2003
Sphingobium chlorophenolicum
brenda
Shah, S.; Thakur, I.S.
Enzymatic dehalogenation of pentachlorophenol by Pseudomonas fluorescens of the microbial community from tannery effluent
Curr. Microbiol.
47
65-70
2003
Pseudomonas fluorescens
brenda
Dai, M.; Rogers, J.B.; Warner, J.R.; Copley, S.D.
A previously unrecognized step in pentachlorophenol degradation in Sphingobium chlorophenolicum is catalyzed by tetrachlorobenzoquinone reductase (PcpD)
J. Bacteriol.
185
302-310
2003
Sphingobium chlorophenolicum
brenda
Crawford, R.L.; Jung, C.M.; Strap, J.L.
The recent evolution of pentachlorophenol (PCP)-4-monooxygenase (PcpB) and associated pathways for bacterial degradation of PCP
Biodegradation
18
525-539
2006
Sphingomonas sp., Sphingobium chlorophenolicum, Mycolicibacterium chlorophenolicum
brenda
Su, Y.; Chen, L.; Bandy, B.; Yang, J.
The Catalytic Product of Pentachlorophenol 4-Monooxygenase is Tetra-chlorohydroquinone rather than Tetrachlorobenzoquinone
Open Microbiol. J.
2
100-106
2008
Sphingobium chlorophenolicum (P42535), Sphingobium chlorophenolicum
brenda
Hlouchova, K.; Rudolph, J.; Pietari, J.M.; Behlen, L.S.; Copley, S.D.
Pentachlorophenol hydroxylase, a poorly functioning enzyme required for degradation of pentachlorophenol by Sphingobium chlorophenolicum
Biochemistry
51
3848-3860
2012
Sphingobium chlorophenolicum
brenda
Rudolph, J.; Erbse, A.H.; Behlen, L.S.; Copley, S.D.
A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum
Biochemistry
53
6539-6549
2014
Sphingobium chlorophenolicum (P42535)
brenda
Joshi, V.; Prewitt, M.; Ma, D.; Borazjani, H.
Enhanced remediation of pentachlorophenol (PCP)-contaminated groundwater by bioaugmentation with known PCP-degrading bacteria
Bioremediat. J.
19
160-170
2015
Sphingobium chlorophenolicum (P42535), Sphingobium chlorophenolicum L-1 (P42535)
-
brenda
Aregbesola, O.A.; Kumar, A.; Mokoena, M.P.; Olaniran, A.O.
Classic pentachlorophenol hydroxylating phenylalanine 4-monooxygenase from indigenous Bacillus tropicus strain AOA-CPS1 cloning, overexpression, purification, characterization and structural homology modelling
Appl. Biochem. Biotechnol.
194
635-658
2022
Bacillus tropicus, Bacillus tropicus AOA-CPS1
brenda
Aregbesola, O.A.; Kumar, A.; Mokoena, M.P.; Olaniran, A.O.
Whole-genome sequencing, genome mining, metabolic reconstruction and evolution of pentachlorophenol and other xenobiotic degradation pathways in Bacillus tropicus strain AOA-CPS1
Funct. Integr. Genomics
21
171-193
2021
Bacillus tropicus, Bacillus tropicus AOA-CPS1
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.13.50)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
