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ENZYME

ENZYME entry: EC 3.5.1.14

Accepted Name
N-acyl-aliphatic-L-amino acid amidohydrolase
Alternative Name(s)
acylase I
aminoacylase 1
aminoacylase I
benzamidase
dehydropeptidase II
hippuricase
histozyme
N-acyl-L-amino-acid amidohydrolase
Reaction catalysed
  • an N-acyl-L-amino acid + H2O <=> a carboxylate + an L-alpha-amino acid
  • an N-acetyl-L-cysteine-S-conjugate + H2O <=> acetate + an S-substituted L-cysteine
Comment(s)
  • 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-alpha-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 and EC 3.5.1.114.
Cross-references
BRENDA3.5.1.14
EC2PDB3.5.1.14
ExplorEnz3.5.1.14
PRIAM enzyme-specific profiles3.5.1.14
KEGG Ligand Database for Enzyme Nomenclature3.5.1.14
IUBMB Enzyme Nomenclature3.5.1.14
IntEnz3.5.1.14
MEDLINEFind literature relating to 3.5.1.14
MetaCyc3.5.1.14
Rhea expert-curated reactions3.5.1.14
UniProtKB/Swiss-Prot
K9NBS6, AAM_RHOERQ6AYS7, ACY1A_RATQ6PTT0, ACY1B_RAT
Q55DP8, ACY1_DICDIQ03154, ACY1_HUMANQ99JW2, ACY1_MOUSE
P37111, ACY1_PIGQ5RFB0, ACY1_PONABP37112, AMAA_GEOSE
P37356, AMAA_PARTMQ32LT9, 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.-.-
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