Canadian Medical Guide > Chemicals and Drugs > Enzymes and Coenzymes > Enzymes > Hydrolases > Amidohydrolases Terms and Definitions

Amidohydrolases

Medical Definition:
CAS Number:	EC 3.5.

Amidohydrolases Categories.

	Allophanate Hydrolase - An enzyme that catalyzes the hydrolysis of allophanic acid to two molecules of ammonia plus two molecules of "active carbon dioxide". EC 3.5.1.54.
	Arylformamidase - An enzyme that catalyzes the conversion of N-formyl-L-kynurenine and water to formate and L-kynurenine. It also acts on other aromatic formylamines. (Enzyme Nomenclature, 1992) EC 3.5.1.9.
	Asparaginase - A hydrolase enzyme that converts L-asparagine and water to L-aspartate and NH3. EC 3.5.1.1.
	Aspartylglucosylaminase - An enzyme that catalyzes the conversion of N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine and water to N-acetyl-beta-D-glucosaminylamine and L-aspartate. It acts only on asparagine oligosaccharides containing one amino acid, i.e. the asparagine has free alpha-amino and alpha-carboxyl groups. (From Enzyme Nomenclature, 1992) EC 3.5.1.26.
	beta-Lactamases - Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these enzymes are penicillins and cephalosporins. EC 3.5.2.6.
	Biotinidase - An enzyme which catalyzes the release of BIOTIN from biocytin. In human, defects in the enzyme are the cause of the organic acidemia MULTIPLE CARBOXYLASE DEFICIENCY or BIOTINIDASE DEFICIENCY.
	Dihydroorotase - An enzyme that, in the course of pyrimidine biosynthesis, catalyzes ring closure by removal of water from N-carbamoylaspartate to yield dihydro-orotic acid. EC 3.5.2.3.
	Glutaminase
	Histone Deacetylases - Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. Some of these belong to the SIRTUINS protein family.
	N-Acetylmuramoyl-L-alanine Amidase - An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.
	Nicotinamidase - An enzyme that catalyzes the hydrolysis of nicotinamide to nicotinate and ammonia. EC 3.5.1.19.
	Penicillin Amidase - An enzyme catalyzing the hydrolysis of penicillin to penicin and a carboxylic acid anion. EC 3.5.1.11.
	Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - An amidohydrolase that removes intact asparagine-linked oligosaccharide chains from glycoproteins. It requires the presence of more than two amino-acid residues in the substrate for activity. This enzyme was previously listed as EC 3.2.2.18.
	Pyroglutamate Hydrolase - Hydrolyzes pyroglutamic acid in the presence of ATP to glutamate plus ADP and inorganic phosphate. Deficiency leads to pyroglutamic acidurea.
	Sirtuins - A homologous family of proteins that includes the NAD-dependent protein deacetylases which deacetylate proteins by catalyzing the formation of O-acetyl-ADP-ribose from the ADP-RIBOSE moiety (of NAD) and the acetyl group that is being removed from the protein. Sir2p, from Saccharomyces cerevisiae, is the founding member and the family includes other homologs (HSTs - homologs of Sir Two). Some HISTONE DEACETYLASES (the Sir2-like HDACs) belong to this family of proteins.
	Urease - An enzyme that catalyzes the conversion of urea and water to carbon dioxide and ammonia. EC 3.5.1.5.

Amidohydrolases Medical Definitions and Terms

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