Phenylacetyl-CoA dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a phenylacetyl-CoA dehydrogenase (EC 1.17.5.1) is an enzyme that catalyzes the chemical reaction
- phenylacetyl-CoA + H2O + 2 quinone
phenylglyoxylyl-CoA + 2 quinol
The 3 substrates of this enzyme are phenylacetyl-CoA, H2O, and quinone, whereas its two products are phenylglyoxylyl-CoA and quinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 group with a quinone or similar compound as acceptor. The systematic name of this enzyme class is phenylacetyl-CoA:quinone oxidoreductase. This enzyme is also called phenylacetyl-CoA:acceptor oxidoreductase.
[edit] References
- IUBMB entry for 1.17.5.1
- BRENDA references for 1.17.5.1 (Recommended.)
- PubMed references for 1.17.5.1
- PubMed Central references for 1.17.5.1
- Google Scholar references for 1.17.5.1
- Rhee SK, Fuchs G (1999). "Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica". Eur. J. Biochem. 262: 507–15. doi:. PMID 10336636.
- Schneider S, Fuchs G (1998). "Phenylacetyl-CoA:acceptor oxidoreductase, a new alpha-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica". Arch. Microbiol. 169: 509–16. doi:. PMID 9575237.

