The Enzyme Database

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Accepted name: phenylacetyl-CoA dehydrogenase
Reaction: phenylacetyl-CoA + H2O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol
For diagram of phenylacetyl-CoA metabolism, click here
Other name(s): phenylacetyl-CoA:acceptor oxidoreductase
Systematic name: phenylacetyl-CoA:quinone oxidoreductase
Comments: 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, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 210756-43-7
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 (1999) 507–515. [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 (1998) 509–516. [PMID: 9575237]
[EC created 2004]

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