EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase

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

Reactions

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
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004046
CAS Registry Number: 9012-37-7
UniProtKB/Swiss-Prot: (21) [show] [UniProt]

References

  1. Birnbaum, S.M., Levintow, L., Kingsley, R.B. and Greenstein, J.P.
    Specificity of amino acid acylases.
    J. Biol. Chem. 194 : 455-470 (1952). [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 : 847-856 (1953). [PMID: 13061423]
  3. Henseling, J., Rohm, K. H.
    Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters.
    Biochim. Biophys. Acta 959 : 370-377 (1988). [PMID: 3355856]
  4. Heese, D., Berger, S., Rohm, K. H.
    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]
  5. Palm, G. J., Rohm, K. H.
    Aminoacylase I from porcine kidney: identification and characterization of two major protein domains.
    J. Protein Chem. 14 : 233-240 (1995). [PMID: 7662111]
  6. Uttamsingh, V., Keller, D. A., Anders, M. W.
    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]
  7. Lindner, H., Hopfner, S., Tafler-Naumann, M., Miko, M., Konrad, L., Rohm, K. H.
    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]