|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
In Pathway: phenylacetate degradation I (aerobic)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: phenylacetate—CoA ligase
Enzyme Commission Synonyms: phenacyl coenzyme A synθse, phenylacetyl-CoA ligase, PA-CoA ligase, phenylacetyl-CoA ligase (AMP-forming)
Enzyme Commission Summary:
Also acts, more slowly, on acetate, propanoate and butanoate, but not on hydroxy derivatives of phenylacetate and related compounds.
Ferrandez98: Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E (1998). "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." J Biol Chem 1998;273(40);25974-86. PMID: 9748275
MartinezBlanco90: Martinez-Blanco H, Reglero A, Rodriguez-Aparicio LB, Luengo JM (1990). "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the catabolism of phenylacetic acid." J Biol Chem 265(12);7084-90. PMID: 2324116
Vessey03: Vessey DA, Lau E, Kelley M, Warren RS (2003). "Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria." J Biochem Mol Toxicol 17(1);1-6. PMID: 12616642
Vessey99: Vessey DA, Kelley M, Warren RS (1999). "Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids." Biochim Biophys Acta 1428(2-3);455-62. PMID: 10434065
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