Amidase

Amidase
x-ray structure of native peptide amidase from stenotrophomonas maltophilia at 1.4 a
Identifiers
Symbol	Amidase
Pfam	PF01425
InterPro	IPR000120
PROSITE	PDOC00494
SCOP	1ocm
SUPERFAMILY	1ocm
OPM superfamily	58
OPM protein	1mt5
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide:

Thus, the two substrates of this enzyme are monocarboxylic acid amide and H₂O, whereas its two products are monocarboxylate and NH₃.

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 acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation.