| EC |
1.14.14.173 |
| Accepted name: |
2,4,6-trichlorophenol monooxygenase |
| Reaction: |
(1) 2,4,6-trichlorophenol + FADH2 + O2 = 2,6-dichloro-1,4-benzoquinone + Cl- + FAD + H2O
(2) 2,6-dichlorohydroquinone + FADH2 + O2 = 2-chloro-6-hydroxy-1,4-benzoquinone + Cl- + FAD + H2O |
| Other name(s): |
tcpA (gene name) |
| Systematic name: |
2,4,6-trichlorophenol,FADH2:oxygen oxidoreductase (dechlorinating) |
| Comments: |
The enzyme, characterized from a number of bacterial species, 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 displaces two chlorine atoms by attacking two different positions in the substrate. Each reaction catalysed by the enzyme displaces a single chlorine and results in formation of a dione, which must be reduced by FADH2 before the monooxygenase could catalyse the second reaction. 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. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Louie, T.M., Webster, C.M. and Xun, L. Genetic and biochemical characterization of a 2,4,6-trichlorophenol degradation pathway in Ralstonia eutropha JMP134. J. Bacteriol. 184 (2002) 3492–3500. [PMID: 12057943] |
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| [EC 1.14.14.173 created 2020] |
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