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ENZYME

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-alpha-amino acid + H2O <=> a carboxylate + an aromatic L-alpha-amino acid
  • an N-acetyl-L-cysteine-S-conjugate + H2O <=> acetate + an S-substituted L-cysteine
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
Rhea expert-curated reactions3.5.1.114
UniProtKB/Swiss-Prot
Q6DHI0, ACY3A_DANREQ6DHQ3, ACY3B_DANREQ96HD9, ACY3_HUMAN
Q91XE4, ACY3_MOUSEQ5M876, ACY3_RATA0JMS7, ACY3_XENLA
Q5BJ91, ACY3_XENTRQ32LT9, P2011_DANREQ08BB2, P2012_DANRE
Q2T9M7, P20D1_BOVINQ5ZL18, P20D1_CHICKQ6GTS8, P20D1_HUMAN
Q8C165, P20D1_MOUSEQ08BT9, P20D1_XENTR

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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.-.-.-