Amidase
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. Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence.