Tetrachloroethene reductive dehalogenase

This enzyme belongs to the family of oxidoreductases. The systematic name of this enzyme class is acceptor:trichloroethene oxidoreductase (chlorinating). This enzyme is also called tetrachloroethene reductase. This enzyme participates in tetrachloroethene degradation.

Note that the physiologically relevant reaction actually occurs in the reverse direction from that shown above. In other words, in the bacterial species where this enzyme is found, tetrachloroethene is reductively dechlorinated to trichloroethene and chloride.

This enzyme is one member of a family of enzymes including trichloroethene dehalogenase and vinyl chloride dehalogenase. The other members of this family do not have their own EC numbers at present.

References

Holliger C, Wohlfarth G, Diekert G (1998). "Reductive dechlorination in the energy metabolism of anaerobic bacteria". FEMS Microbiol. Rev. 22 (5): 383–398. doi:10.1111/j.1574-6976.1998.tb00377.x.
Glod G, Angst W, Holliger C, Schwarzenbach RP (1997). "Corrinoid-mediated reduction of tetrachloroethene, trichloroethene, and trichlorofluoroethene in homogeneous aqueous solution: Reaction kinetics and reaction mechanisms". Environ. Sci. Technol. 31 (1): 253–260. doi:10.1021/es9603867.
Neumann A, Wohlfarth G, Diekert G (1996). "Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans". J. Biol. Chem. 271 (28): 16515–9. doi:10.1074/jbc.271.28.16515. PMID 8663199.
Schumacher W, Holliger C, Zehnder AJ, Hagen WR (1997). "Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus". FEBS Lett. 409 (3): 421–5. doi:10.1016/S0014-5793(97)00520-6. PMID 9224702.
Schumacher W, Holliger C (1996). "The proton/electron ration of the menaquinone-dependent electron transport from dihydrogen to tetrachloroethene in "Dehalobacter restrictus"". J. Bacteriol. 178 (8): 2328–33. PMC 177941. PMID 8636034.

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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