KEGG   ENZYME: 1.14.14.173
Entry
EC 1.14.14.173              Enzyme                                 
Name
2,4,6-trichlorophenol monooxygenase;
tcpA (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
2,4,6-trichlorophenol,FADH2:oxygen oxidoreductase (dechlorinating)
Reaction(IUBMB)
2,4,6-trichlorophenol + FADH2 + O2 = 6-chloro-2-hydroxy-1,4-benzoquinone + 2 Cl- + FAD (overall reaction) [RN:R13143];
(1a) 2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichloro-1,4-benzoquinone + Cl- + FAD + H2O [RN:R05449];
(1b) 2,6-dichloro-1,4-benzoquinone + H2O = 6-chloro-2-hydroxy-1,4-benzoquinone + Cl- [RN:R13142]
Reaction(KEGG)
Substrate
2,4,6-trichlorophenol [CPD:C07098];
FADH2 [CPD:C01352];
O2 [CPD:C00007];
2,6-dichloro-1,4-benzoquinone [CPD:C21103];
H2O [CPD:C00001]
Product
6-chloro-2-hydroxy-1,4-benzoquinone [CPD:C22290];
Cl- [CPD:C00698];
FAD [CPD:C00016];
2,6-dichloro-1,4-benzoquinone [CPD:C21103];
H2O [CPD:C00001]
Comment
The enzyme, characterized from Cupriavidus pinatubonensis, participates in the degradation of 2,4,6-trichlorophenol, a compound that has been used for decades as a wood preservative. The enzyme is a multifunctional flavin-dependent monooxygenase that catalyses two different reactions to displace two chlorine atoms, a monooxygenase reaction followed by a hydrolysis reaction that takes advantage of the reactivity of the product of the first reaction, 2,6-dichloro-1,4-benzoquinone [2]. The large amount of FADH2 that is required is generated by a dedicated flavin reductase (TcpB). cf. EC 1.14.14.172, 3,5,6-trichloropyridin-2-ol monooxygenase.
History
EC 1.14.14.173 created 2020, modified 2022
Pathway
ec00361  Chlorocyclohexane and chlorobenzene degradation
ec01120  Microbial metabolism in diverse environments
Orthology
K15246  chlorophenol-4-monooxygenase
K24293  3,5,6-trichloropyridin-2-ol/2,4,6-trichlorophenol monooxygenase
Genes
RPJN234_22415
CNCCNE_BB1p03440(tcpA)
REUReut_A1585
COXE0W60_29395(tcpA)
PHSC2L64_40520
PTERC2L65_19195
SRCM271_03085
SCADDN051_03580
SDXC4B68_04165
SFYGFH48_02550
SCHFIPT68_01680
SSPNLXH13_00190
SCYNN8I84_40615
AGLAOIE69_10100 OIE69_40295
PDXPsed_2279
 » show all
Reference
1  [PMID:12057943]
  Authors
Louie TM, Webster CM, Xun L
  Title
Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134.
  Journal
J Bacteriol 184:3492-500 (2002)
DOI:10.1128/jb.184.13.3492-3500.2002
  Sequence
Reference
2  [PMID:14662756]
  Authors
Xun L, Webster CM.
  Title
A monooxygenase catalyzes sequential dechlorinations of 2,4,6-trichlorophenol by oxidative and hydrolytic reactions.
  Journal
J Biol Chem 279:6696-700 (2004)
DOI:10.1074/jbc.M312072200
Reference
3  [PMID:22949829]
  Authors
Hayes RP, Webb BN, Subramanian AK, Nissen M, Popchock A, Xun L, Kang C.
  Title
Structural and catalytic differences between two FADH(2)-dependent monooxygenases: 2,4,5-TCP 4-monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-monooxygenase (TcpA) from Cupriavidus necator JMP134.
  Journal
Int J Mol Sci 13:9769-9784 (2012)
DOI:10.3390/ijms13089769
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.173
IUBMB Enzyme Nomenclature: 1.14.14.173
ExPASy - ENZYME nomenclature database: 1.14.14.173
BRENDA, the Enzyme Database: 1.14.14.173

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