Aminoacylase

From Wikipedia, the free encyclopedia

In enzymology, an aminoacylase (EC 3.5.1.14) 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Q7L and 1YSJ.

[edit] References

IUBMB entry for 3.5.1.14
BRENDA references for 3.5.1.14 (Recommended.)
PubMed references for 3.5.1.14
PubMed Central references for 3.5.1.14
Google Scholar references for 3.5.1.14
BIRNBAUM SM, LEVINTOW L, KINGSLEY RB, GREENSTEIN JP (1952). "Specificity of amino acid acylases". J. Biol. Chem. 194: 455–70. PMID 14927637.
FONES WS, LEE M (1953). "Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase". J. Biol. Chem. 201: 847–56. PMID 13061423.
Park RW and Fox, SW (1960). "An acylase system related to the utilization of benzoylamino acids by Lactobacillus arabinosus". J. Biol. Chem. 235: 3193–3197.