| Description | This entry represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolase ( ) is a homodimeric zinc-binding mammalian enzyme that catalyzes the hydrolysis of N-alpha-acylated amino acids except L-aspartic acid [ , ]. These enzymes are listed as non-peptidase homologues in MEROPS peptidase family M20A (clan MH). Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase [, ]. | Name | N-acyl-L-amino-acid amidohydrolase |
| Short Name | N-acyl_aa_amidohydrolase | Type | Family |
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