KEGG   ENZYME: 1.21.99.5
Entry
EC 1.21.99.5                Enzyme                                 
Name
tetrachloroethene reductive dehalogenase;
tetrachloroethene reductase
Class
Oxidoreductases;
Catalysing the reaction X-H + Y-H = X-Y;
With unknown physiological acceptors
Sysname
acceptor:trichloroethene oxidoreductase (chlorinating)
Reaction(IUBMB)
trichloroethene + chloride + acceptor = tetrachloroethene + reduced acceptor [RN:R05753]
Reaction(KEGG)
R05753;
(other) R05499 R05500 R05501
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. 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 involves menaquinol, which is reduced by molecular hydrogen via the action of 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 in vitro.
History
EC 1.21.99.5 created 2001 as EC 1.97.1.8, transferred 2017 to EC 1.21.99.5
Pathway
ec00625  Chloroalkane and chloroalkene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K21647  tetrachloroethene reductive dehalogenase
Genes
SMULSMUL_1531(pceA)
SHALSHALO_1495
SULSSdiek1_1587
SULJSJPD1_1504
SULTFA592_00015 FA592_00070 FA592_13750
PBIZLWC08_09670
CALKHUE98_04865
DETHHX448_00270 HX448_00330 HX448_01225 HX448_02085 HX448_02090 HX448_02095 HX448_03030 HX448_03180 HX448_03295 HX448_03300 HX448_03310 HX448_03315 HX448_03350 HX448_03355 HX448_05565 HX448_07555 HX448_07630 HX448_07635 HX448_08110 HX448_08115 HX448_08120 HX448_08405 HX448_08815 HX448_08840 HX448_08850 HX448_09535 HX448_09555
Reference
1
  Authors
Holliger, C, Wohlfarth, G. and Diekert, G.
  Title
Reductive dechlorination in the energy metabolism of anaerobic bacteria.
  Journal
FEMS Microbiol Rev 22:383-398 (1998)
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 31:253-260 (1997)
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 271:16515-9 (1996)
DOI:10.1074/jbc.271.28.16515
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 409:421-5 (1997)
DOI:10.1016/S0014-5793(97)00520-6
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 178:2328-33 (1996)
DOI:10.1128/JB.178.8.2328-2333.1996
Other DBs
ExplorEnz - The Enzyme Database: 1.21.99.5
IUBMB Enzyme Nomenclature: 1.21.99.5
ExPASy - ENZYME nomenclature database: 1.21.99.5
BRENDA, the Enzyme Database: 1.21.99.5
CAS: 163913-51-7

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