IntEnz

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

IntEnz Enzyme Nomenclature
EC 3.5.1.14

Names

Reactions

• 15565 [IUBMB]
  an N-acyl-L-amino acid

  an N-acyl-L-amino acid

  Name origin: UniProt - CHECKED (C)

  CHEBI:59874

  Formula: C3H2NO3R2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  a carboxylate

  a carboxylate

  Name origin: UniProt - CHECKED (C)

  CHEBI:29067

  Formula: CO2R
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  an L-α-amino acid

  an L-alpha-amino acid

  Name origin: UniProt - CHECKED (C)

  CHEBI:59869

  Formula: C2H4NO2R
  Charge: 0

  ChEBI compound status: CHECKED (C)

  
• 36855 [IUBMB]
  an N-acetyl-L-cysteine-S-conjugate

  an N-acetyl-L-cysteine-S-conjugate

  Name origin: UniProt - CHECKED (C)

  CHEBI:58718

  Formula: C5H7NO3SR
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  acetate

  acetate

  Name origin: UniProt - CHECKED (C)

  CHEBI:30089

  Formula: C2H3O2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  an S-substituted L-cysteine

  an S-substituted L-cysteine

  Name origin: UniProt - CHECKED (C)

  CHEBI:58717

  Formula: C3H6NO2SR
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Zn²⁺

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

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]