| EC |
2.3.1.192 |
| Accepted name: |
glycine N-phenylacetyltransferase |
| Reaction: |
phenylacetyl-CoA + glycine = CoA + phenylacetylglycine |
| Other name(s): |
arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name) |
| Systematic name: |
phenylacetyl-CoA:glycine N-phenylacetyltransferase |
| Comments: |
Not identical with EC 2.3.1.13 (glycine N-acyltransferase).
This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Nandi, D.L., Lucas, S.V. and Webster, L.T. Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization. J. Biol. Chem. 254 (1979) 7230–7237. [PMID: 457678] |
| 2. |
Kelley, M. and Vessey, D.A. The effects of ions on the conjugation of xenobiotics by the aralkyl-CoA and arylacetyl-CoA N-acyltransferases from bovine liver mitochondria. J. Biochem. Toxicol. 5 (1990) 125–135. [DOI] [PMID: 2283662] |
| 3. |
Vessey, D.A. and Lau, E. Determination of the sequence of the arylacetyl acyl-CoA:amino acid N-acyltransferase from bovine liver mitochondria and its homology to the aralkyl acyl-CoA:amino acid N-acyltransferase. J. Biochem. Mol. Toxicol. 12 (1998) 275–279. [DOI] [PMID: 9664233] |
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| [EC 2.3.1.192 created 2010] |
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