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1.21.99.5: tetrachloroethene reductive dehalogenase

This is an abbreviated version!
For detailed information about tetrachloroethene reductive dehalogenase, go to the full flat file.

Word Map on EC 1.21.99.5

Reaction

trichloroethene
+
chloride
+
acceptor
=
tetrachloroethene
+
reduced acceptor

Synonyms

1,2,4,5-TeCB reductive dehalogenase, dceA6, dehalogenase, polychloroethene, EC 1.97.1.8, mbrA, PCE dehalogenase, PCE reductase, PCE reductive dehalogenase, PCE-dechlorinating enzyme, PCE-RD, PCE-RDase, PCE-reductive dehalogenase, PCE/PCB RDase, PCE/TCERD, PceA, pceA gene product, PceA1, PceA2, PceATCE, PceC, pceC gene product, PCER, PCERD, perchloroethylene dehalogenase, polychloroethane dehalogenase, RD11, RD8, RDase, RDH, RdhA, RdhA3, reductive dehalogenase, reductive PCE dehalogenase, Ssed_3769, TcbA, TCE dehalogenase, TCE reductase, tetrachlorobenzene dehalogenase, tetrachloroethene (PCE) dehalogenase, tetrachloroethene (PCE) reductive dehalogenase, tetrachloroethene and trichloroethene dehalogenase, tetrachloroethene dehalogenase, tetrachloroethene reductase, tetrachloroethene reductive dehalogenase, tetrachloroethene reductive dehalogenase catalytic subunit PceA, tetrachloroethylene reductase, ThMA, trichloroethene dehalogenase

ECTree

     1 Oxidoreductases
         1.21 Catalysing the reaction X-H + Y-H = X-Y
             1.21.99 With unknown physiological acceptors
                1.21.99.5 tetrachloroethene reductive dehalogenase

Systematic Name

Systematic Name on EC 1.21.99.5 - tetrachloroethene reductive dehalogenase

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SYSTEMATIC NAME
IUBMB Comments
acceptor:trichloroethene oxidoreductase (chlorinating)
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.