KEGG   ENZYME: 1.14.13.50Help
Entry
EC 1.14.13.50               Enzyme                                 

Name
pentachlorophenol monooxygenase;
pcpB (gene name);
pentachlorophenol dechlorinase;
pentachlorophenol dehalogenase;
pentachlorophenol 4-monooxygenase;
PCP hydroxylase;
pentachlorophenol hydroxylase;
PCB 4-monooxygenase;
PCB4MO
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating)
Reaction(IUBMB)
(1) pentachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O [RN:R03982];
(2) 2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O [RN:R07191]
Reaction(KEGG)
R03982 R07191;
(other) R07779
Show
Substrate
pentachlorophenol [CPD:C02575];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007];
2,3,5,6-tetrachlorophenol [CPD:C15505]
Product
2,3,5,6-tetrachloro-1,4-benzoquinone [CPD:C18933];
NADP+ [CPD:C00006];
chloride [CPD:C00698];
H2O [CPD:C00001];
2,3,5,6-tetrachlorohydroquinone [CPD:C03434]
Comment
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.
History
EC 1.14.13.50 created 1992, modified 2005, modified 2017
Pathway
ec00361  Chlorocyclohexane and chlorobenzene degradation
ec00364  Fluorobenzoate degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K03391  pentachlorophenol monooxygenase
Genes
SCH: Sphch_3461
Taxonomy
Reference
1  [PMID:2793827]
  Authors
Schenk T, Muller R, Morsberger F, Otto MK, Lingens F.
  Title
Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790.
  Journal
J Bacteriol 171:5487-91 (1989)
DOI:10.1128/JB.171.10.5487-5491.1989
Reference
2  [PMID:1569020]
  Authors
Xun L, Topp E, Orser CS.
  Title
Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries.
  Journal
J Bacteriol 174:2898-902 (1992)
DOI:10.1128/JB.174.9.2898-2902.1992
Reference
3  [PMID:1512208]
  Authors
Xun L, Topp E, Orser CS.
  Title
Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase.
  Journal
J Bacteriol 174:5745-7 (1992)
DOI:10.1128/JB.174.17.5745-5747.1992
Reference
4  [PMID:8619798]
  Authors
Lange CC, Schneider BJ, Orser CS.
  Title
Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723.
  Journal
Biochem Biophys Res Commun 219:146-9 (1996)
DOI:10.1006/bbrc.1996.0196
Reference
5  [PMID:15262224]
  Authors
Nakamura T, Motoyama T, Hirono S, Yamaguchi I.
  Title
Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase.
  Journal
Biochim Biophys Acta 1700:151-9 (2004)
DOI:10.1016/j.bbapap.2004.04.008
Reference
6  [PMID:19325743]
  Authors
Chen L, Yang J
  Title
Biochemical characterization of the tetrachlorobenzoquinone reductase involved in the biodegradation of pentachlorophenol.
  Journal
Int J Mol Sci 9:198-212 (2008)
Reference
7  [PMID:22482720]
  Authors
Hlouchova K, Rudolph J, Pietari JM, Behlen LS, Copley SD
  Title
Pentachlorophenol hydroxylase, a poorly functioning enzyme required for degradation of pentachlorophenol by Sphingobium chlorophenolicum.
  Journal
Biochemistry 51:3848-60 (2012)
DOI:10.1021/bi300261p
Reference
8  [PMID:25238136]
  Authors
Rudolph J, Erbse AH, Behlen LS, Copley SD
  Title
A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum.
  Journal
Biochemistry 53:6539-49 (2014)
DOI:10.1021/bi5010427
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.50
IUBMB Enzyme Nomenclature: 1.14.13.50
ExPASy - ENZYME nomenclature database: 1.14.13.50
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.50
BRENDA, the Enzyme Database: 1.14.13.50
CAS: 136111-57-4

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