EC 3 - Hydrolases
EC 3.5 - Acting on carbon-nitrogen bonds, other than peptide bonds
EC 3.5.1 - In linear amides
EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.5.1.14
Names
Accepted name:
N-acyl-aliphatic-L-amino acid amidohydrolase
Other
names:
α-N-acylaminoacid hydrolase
L-amino-acid acylase
L-aminoacylase
acylase
acylase I
amido acid deacylase
aminoacylase I
benzamidase
dehydropeptidase II
hippurase
hippuricase
histozyme
long acyl amidoacylase
short acyl amidoacylase
aminoacylase 1
ACY1 (gene name)
N-acyl-L-amino-acid amidohydrolase
L-amino-acid acylase
L-aminoacylase
acylase
acylase I
amido acid deacylase
aminoacylase I
benzamidase
dehydropeptidase II
hippurase
hippuricase
histozyme
long acyl amidoacylase
short acyl amidoacylase
aminoacylase 1
ACY1 (gene name)
N-acyl-L-amino-acid amidohydrolase
Systematic name:
N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming)
Reactions
- (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
Cofactor
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
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00613
Gene Ontology:
GO:0004046
CAS Registry Number:
9012-37-7
References
-
Specificity of amino acid acylases.J. Biol. Chem. 194 : 455-470 (1952). [PMID: 14927637]
-
Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase.J. Biol. Chem. 201 : 847-856 (1953). [PMID: 13061423]
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Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters.Biochim. Biophys. Acta 959 : 370-377 (1988). [PMID: 3355856]
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Nuclear magnetic relaxation studies of the role of the metal ion in Mn2(+)-substituted aminoacylase I.Eur. J. Biochem. 188 : 175-180 (1990). [PMID: 2318199]
-
Aminoacylase I from porcine kidney: identification and characterization of two major protein domains.J. Protein Chem. 14 : 233-240 (1995). [PMID: 7662111]
-
Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines.Chem. Res. Toxicol. 11 : 800-809 (1998). [PMID: 9671543]
-
The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney.Biochimie 82 : 129-137 (2000). [PMID: 10727768]
[EC 3.5.1.14 created 1965, modified 2013]