ExplorEnz: EC 3.5.1.14

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3.5.1.14

Accepted name:

N-acyl-aliphatic-L-amino acid amidohydrolase

Reaction:

(1) an N-acyl-aliphatic-L-amino acid + H₂O = an aliphatic L-amino acid + a carboxylate
(2) an N-acetyl-L-cysteine-S-conjugate + H₂O = an L-cysteine-S-conjugate + acetate

Glossary:

N-acetyl-L-cysteine-S-conjugate = mercapturic acid

Other name(s):

aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase

Systematic name:

N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming)

Comments:

Contains Zn²⁺. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-α-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.

Links to other databases:

BRENDA, EXPASY, Gene, 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.	Henseling, J. and Rohm, K.H. Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters. Biochim. Biophys. Acta 959 (1988) 370–377. [DOI] [PMID: 3355856]
4.	Heese, D., Berger, S. and Rohm, K.H. Nuclear magnetic relaxation studies of the role of the metal ion in Mn²⁺-substituted aminoacylase I. Eur. J. Biochem. 188 (1990) 175–180. [DOI] [PMID: 2318199]
5.	Palm, G.J. and Rohm, K.H. Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. J. Protein Chem. 14 (1995) 233–240. [PMID: 7662111]
6.	Uttamsingh, V., Keller, D.A. and Anders, M.W. Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. Chem. Res. Toxicol. 11 (1998) 800–809. [DOI] [PMID: 9671543]
7.	Lindner, H., Hopfner, S., Tafler-Naumann, M., Miko, M., Konrad, L. and Rohm, K.H. The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney. Biochimie 82 (2000) 129–137. [DOI] [PMID: 10727768]

[EC 3.5.1.14 created 1965, modified 2013]