EC - Phenylacetyl-CoA dehydrogenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
phenylacetyl-CoA dehydrogenase
Other name:
phenylacetyl-CoA:acceptor oxidoreductase
Systematic name:
phenylacetyl-CoA:quinone oxidoreductase




The enzyme from Thauera aromatica is a membrane-bound molybdenum—iron—sulfur protein. The enzyme is specific for phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone [1]. A second enzyme, EC, phenylglyoxylyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0033789


  1. Rhee, S.K. and Fuchs, G.
    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 : 507-515 (1999). [PMID: 10336636]
  2. Schneider, S. and Fuchs, G.
    Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica.
    Arch. Microbiol. 169 : 509-516 (1998). [PMID: 9575237]

[EC created 2004]