Aminoacylase

In enzymology, an aminoacylase (EC3.5.1.14) is an enzyme that catalyzes the chemical reaction

N-acyl-L-amino acid+ H₂O ⇌ carboxylate + 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.