ENZYME entry: EC 3.5.1.114

Accepted Name
N-acyl-aromatic-L-amino acid amidohydrolase.
Alternative Name(s)
Aminoacylase 3.
Aminoacylase III.
Reaction catalysed
  • An N-acyl-aromatic-L-amino acid + H(2)O <=> an aromatic-L-amino acid + a carboxylate
  • An N-acetyl-L-cysteine-S-conjugate + H(2)O <=> an L-cysteine-S-conjugate + acetate
Cofactor(s)
Zn(2+).
Comment(s)
  • This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
  • It preferentially deacetylates N(alpha)-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14.
  • Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114.
  • Cf. EC 3.5.1.14 and EC 3.5.1.15.
Cross-references
BRENDA3.5.1.114
EC2PDB3.5.1.114
ExplorEnz3.5.1.114
PRIAM enzyme-specific profiles3.5.1.114
KEGG Ligand Database for Enzyme Nomenclature3.5.1.114
IUBMB Enzyme Nomenclature3.5.1.114
IntEnz3.5.1.114
MEDLINEFind literature relating to 3.5.1.114
MetaCyc3.5.1.114
UniProtKB/Swiss-Prot
Q6DHI0, ACY3A_DANRE;  Q6DHQ3, ACY3B_DANRE;  Q96HD9, ACY3_HUMAN;  
Q91XE4, ACY3_MOUSE;  Q5M876, ACY3_RAT;  A0JMS7, ACY3_XENLA;  
Q5BJ91, ACY3_XENTR;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.5.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-