Phenylacetyl-CoA hydrolase

Phenylacetyl-CoA hydrolase
Identifiers
EC no.3.1.2.25
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The enzyme phenylacetyl-CoA hydrolase (EC 3.1.2.25) catalyzes the reaction

phenylglyoxylyl-CoA
 
 
H2O
 
Rightward reaction arrow with minor substrate(s) from top left
 
 
 
+
 

The enzyme characterised from the bacterium Thauera aromatica hydrolyses phenylglyoxylyl-CoA to coenzyme A and phenylglyoxylic acid, which form the thioester in the starting material. This is the second step in a pathway for breakdown of phenylacetyl-CoA to phenylglyoxylic acid, after the action of phenylacetyl-CoA dehydrogenase.[1][2] The enzyme has also been found as part of the biosynthesis of β-Lactam antibiotics.[3]

This enzyme is a hydrolase, specifically one acting on thioester bonds. The systematic name of this enzyme class is phenylglyoxylyl-CoA hydrolase.[4]

References

  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 (2): 507–15. doi:10.1046/j.1432-1327.1999.00399.x. PMID 10336636.
  2. ↑ 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 (6): 509–16. Bibcode:1998ArMic.169..509S. doi:10.1007/s002030050604. PMID 9575237.
  3. ↑ Vandamme, E.J. (1977). "Enzymes Involved in β-Lactam Antibiotic Biosynthesis". Advances in Applied Microbiology Volume 21. Vol. 21. pp. 89–123. doi:10.1016/S0065-2164(08)70039-X. ISBN 978-0-12-002621-0. PMID 322456.
  4. ↑ Enzyme 3.1.2.25 at KEGG Pathway Database.