Phenylacetate—CoA ligase
| phenylacetate-CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.2.1.30 | ||||||||
| CAS number | 57219-71-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a phenylacetate-CoA ligase is an enzyme that catalyzes the chemical reaction
- ATP + phenylacetate + CoA AMP + diphosphate + phenylacetyl-CoA
The 3 substrates of this enzyme are ATP, phenylacetate, and CoA, whereas its 3 products are AMP, diphosphate, and phenylacetyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is phenylacetate:CoA ligase (AMP-forming). Other names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (AMP-forming). This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
References
- 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.
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