KEGG   ENZYME: 1.97.1.8Help
Entry
EC 1.97.1.8                 Enzyme                                 

Name
tetrachloroethene reductive dehalogenase;
tetrachloroethene reductase
Class
Oxidoreductases;
Other oxidoreductases;
Sole sub-subclass for oxidoreductases that do not belong in the other subclasses
BRITE hierarchy
Sysname
acceptor:trichloroethene oxidoreductase (chlorinating)
Reaction(IUBMB)
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor [RN:R05753]
Reaction(KEGG)
Substrate
trichloroethene [CPD:C06790];
chloride [CPD:C00698];
acceptor [CPD:C00028]
Product
tetrachloroethene [CPD:C06789];
reduced acceptor [CPD:C00030]
Comment
This enzyme allows the common pollutant tetrachloroethene to support bacterial growth and is responsible for disposal of a number of chlorinated hydrocarbons by this organism. The reaction occurs in the reverse direction. The enzyme also reduces trichloroethene to dichloroethene. Although the physiological reductant is unknown, the supply of reductant in some organisms is via reduced menaquinone, itself formed from molecular hydrogen, via EC 1.12.5.1 (hydrogen:quinone oxidoreductase). The enzyme contains a corrinoid and two iron-sulfur clusters. Methyl viologen can act as electron donor.
History
EC 1.97.1.8 created 2001
Pathway
Chloroalkane and chloroalkene degradation
Metabolic pathways
Microbial metabolism in diverse environments
Reference
1
  Authors
Holliger, C, Wohlfarth, G. and Diekert, G.
  Title
Reductive dechlorination in the energy metabolism of anaerobic bacteria.
  Journal
FEMS Microbiol. Rev. 22 (1998) 383-398.
Reference
2
  Authors
Glod, G., Angst, W., Holliger, C. and Schwarzenbach, R.P.
  Title
Corrinoid-mediated reduction of tetrachloroethene, trichloroethene, and trichlorofluoroethene in homogeneous aqueous solution: Reaction kinetics and reaction mechanisms.
  Journal
Environ. Sci. Technol. 31 (1997) 253-260.
Reference
3  [PMID:8663199]
  Authors
Neumann A, Wohlfarth G, Diekert G.
  Title
Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans.
  Journal
J. Biol. Chem. 271 (1996) 16515-9.
Reference
4  [PMID:9224702]
  Authors
Schumacher W, Holliger C, Zehnder AJ, Hagen WR.
  Title
Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus.
  Journal
FEBS. Lett. 409 (1997) 421-5.
Reference
5  [PMID:8636034]
  Authors
Schumacher W, Holliger C.
  Title
The proton/electron ration of the menaquinone-dependent electron transport from dihydrogen to tetrachloroethene in "Dehalobacter restrictus".
  Journal
J. Bacteriol. 178 (1996) 2328-33.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
163913-51-7

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