| EC |
3.5.1.14 |
| Accepted name: |
aminoacylase |
| Reaction: |
an N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid |
| Other name(s): |
dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase I; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase |
| Systematic name: |
N-acyl-L-amino-acid amidohydrolase |
| Comments: |
Wide specificity; also hydrolyses dehydropeptides. Used in separating D- and L- amino acids |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, METACYC, PDB, CAS registry number: 9012-37-7 |
| References: |
| 1. |
Birnbaum, S.M., Levintow, L., Kingsley, R.B. and Greenstein, J.P. Specificity of amino acid acylases. J. Biol. Chem. 194 (1952) 455–470. [PMID: 14927637] |
| 2. |
Fones, W.S. and Lee, M. Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase. J. Biol. Chem. 201 (1953) 847–856. [PMID: 13061423] |
| 3. |
Park, R.W. and Fox, S.W. An acylase system related to the utilization of benzoylamino acids by Lactobacillus arabinosus. J. Biol. Chem. 235 (1960) 3193–3197. [PMID: 13732833] |
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| [EC 3.5.1.14 created 1965] |
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