| EC |
1.17.5.1 |
| Accepted name: |
phenylacetyl-CoA dehydrogenase |
| Reaction: |
phenylacetyl-CoA + H2O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol |
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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 3.1.2.25, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 210756-43-7 |
| References: |
| 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. [DOI] [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] |
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| [EC 1.17.5.1 created 2004] |
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