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Benzoyl-CoA reductase

From Wikipedia, the free encyclopedia

In enzymology, a benzoyl-CoA reductase (EC 1.3.7.8) is an enzyme that catalyzes the chemical reaction

benzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate

The 4 substrates of this enzyme are benzoyl-CoA, reduced acceptor, ATP, and H2O, whereas its 4 products are cyclohexa-1,5-diene-1-carbonyl-CoA, acceptor, ADP, and phosphate.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is cyclohexa-1,5-diene-1-carbonyl-CoA:acceptor oxidoreductase (aromatizing, ATP-forming). This enzyme is also called benzoyl-CoA reductase (dearomatizing). This enzyme participates in benzoate degradation via CoA ligation. It has two cofactors: manganese, and magnesium.

References

  • Boll M, Fuchs G (1995). "Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K172". Eur. J. Biochem. 234 (3): 921–33. doi:10.1111/j.1432-1033.1995.921_a.x. PMID 8575453.


This page was last edited on 26 August 2023, at 13:18
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