In enzymology, an aminoacylase is an enzyme that catalyzes the chemical reaction

an N-acyl-L-amino acid + H2O rightleftharpoons a carboxylate + an L-amino acid

Thus, the two substrates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-L-amino-acid amidohydrolase. Other names in common use include dehydropeptidase II, histozyme, hippuricase, benzamidase, acylase I, hippurase, amido acid deacylase, L-aminoacylase, acylase, aminoacylase I, L-amino-acid acylase, alpha-N-acylaminoacid hydrolase, long acyl amidoacylase, and short acyl amidoacylase. This enzyme participates in urea cycle and metabolism of amino groups.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .


  • BIRNBAUM SM, LEVINTOW L, KINGSLEY RB, GREENSTEIN JP "Specificity of amino acid acylases". J. Biol. Chem. 194 455–70.
  • FONES WS, LEE M "Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase". J. Biol. Chem. 201 847–56.
  • Park RW and Fox, SW "An acylase system related to the utilization of benzoylamino acids by Lactobacillus arabinosus". J. Biol. Chem. 235 3193–3197.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes

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