Aminoacylase

In enzymology, an aminoacylase (EC 3.5.1.14) 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.

Enzyme structure

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Q7L and 1YSJ. These structures also correspond to two known primary amino acid sequences for aminoacylases. The associated papers identify two types of domains comprising aminoacylases: Zinc binding domains - which bind Zn²⁺ ions - and domains that facilitate dimerization of Zinc binding domains. It is this dimerization that allows catalysis to occur, since aminoacylase's active site lies between its two Zinc binding domains.