amidase


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am·i·dase

(am'i-dās),
An enzyme that catalyzes the hydrolysis of monocarboxylic amides to free acid plus NH3; ω-amidase acts on amides such as α-ketoglutaramic acid and α-ketosuccinamic acid.

amidase

(am′ĭ-dās″) [ amide + -ase]
An enzyme that catalyzes the hydrolysis of amides; a deamidizing enzyme.
References in periodicals archive ?
(1991) Structure determination by [sup.1]H-NMR spectroscopy of (sulfated) sialylated N-linked carbohydrate chains released from porcine thyroglobulin by peptide-[N.sup.4] -(N-acetyl-O-glucosaminyl)asparagine amidase F.
Tissue protein and enzyme activities of broiler chicks at 21 days of age on different feeding regimes AP SBM-AP CM-AP AP-SBM Pancreatic protein (mg/g) 46.0 32.0 33.0 37.4 Chymotrypsin amidase (1) 3.4 5.8 4.4 4.2 Jejunal protein (mg/g) 30.0 33.0 36.6 35.2 Maltase (pmol/mg) 0.62 0.58 0.48 0.47 Sucrase (pmol/mg) 0.13 0.13 0.14 0.12 Alkaline phosphatase (2) 3.6 3.0 3.0 3.1 Lipase (3) 2.97 2.92 3.84 3.76 AP-CM SEM Pancreatic protein (mg/g) 46.7 2.44 Chymotrypsin amidase (1) 4.0 0.28 Jejunal protein (mg/g) 36.0 1.52 Maltase (pmol/mg) 0.52 0.027 Sucrase (pmol/mg) 0.13 0.006 Alkaline phosphatase (2) 4.3 0.24 Lipase (3) 2.64 0.247 AP, animal protein; SBM, soybean meal; CM, canola meal; SEM, pooled standard error of mean.
A 63.3 kDa N-terminal domain possesses amidase activity while a 53.6 kDa N-terminal domain possesses the glucosaminidase activity [15-18].
Amidase enzyme activity was determined by the method of Erlanger et al.
A fibrinogen-clotting serine proteinase from Cerastes cerastes (horned viper) venom with arginine-esterase and amidase activities.
The soil enzymes that have been used for these studies are dehydrogenase, beta-glucosidase, cellulose, phenol oxidase, urease, amidase, phosphatase and arylsulphatase.
Inhibi- tion of isoniazid - induced hepatotoxicity in rabbits by pretreatment with an amidase inhibitor.
PZA is converted to the active form of pyrazinoic acid (POA) by an amidase enzyme (PncA) also identified by Zhang's group in 1996.
This finding is reminiscent of the observations that the shallot anti-fungal protein ascalin (Wang et al., 2002) and the anti-fungal amidase from Peltophorum pterocarpum (Lam and Ng 2009a) exert an anti-fungal action on only one out of the several fungi examined.
The invention provides ways for inducing and stabilizing nitrile hydratase activity, amidase activity and asparaginase I activity.