Phenylacetyl-CoA dehydrogenase

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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.

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&ndash, 15. 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&ndash, 16. PMID 9575237.

External links

Template:1.17-enzyme-stub


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