Results 121 to 130 of about 5,660 (180)

Protein carbamylation and proteomics: from artifacts to elucidation of biological functions. [PDF]

Front Anal Sci
You Y, Many G, Nakayasu ES.
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Biodegradation of S-Triazine Herbicides Under Saline Conditions by <i>Paenarthrobacter ureafaciens</i> PC, a New Halotolerant Bacterial Isolate: Insights into Both the Degradative Pathway and Mechanisms of Tolerance to High Salt Concentrations. [PDF]

Microorganisms
Fu C, Jiang Y, Xu B, Fu X, Tan L, Jin M.
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Studies on Bacterial β-Aspartyl amidohydrolases

, 2016
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Studies on Bacterial β-Aspartyl amidohydrolases

Studies on Bacterial β-Aspartyl amidohydrolases
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Dihydropyrimidine amidohydrolase is a zinc metalloenzyme

Biochimica Et Biophysica Acta - Biomembranes, 1979
Bovine liver dihydropyrimidine amidohydrolase (EC 3.5.2.2) has been subjected to atomic absorption analysis. Three different preparations of homogeneous enzyme indicated that the enzyme contains 4.3 +/- 0.3 g atoms of Zn2+ per mol of enzyme or 1.1 g atoms of Zn2+ per subunit. No Co2+, Mn2+, Mg2+ or Cd2+ was detected.
Eugene G Sander, E G Sander
exaly   +3 more sources

Structural Insights into the Substrate Specificity of (S)-Ureidoglycolate Amidohydrolase and Its Comparison with Allantoate Amidohydrolase

Journal of Molecular Biology, 2014
In plants, the ureide pathway is a metabolic route that converts the ring nitrogen atoms of purine into ammonia via sequential enzymatic reactions, playing an important role in nitrogen recovery. In the final step of the pathway, (S)-ureidoglycolate amidohydrolase (UAH) catalyzes the conversion of (S)-ureidoglycolate into glyoxylate and releases two ...
Kitae Han, Sangkee Rhee
exaly   +3 more sources

Allantoate hydrolysis by allantoate amidohydrolase

Archives of Biochemistry and Biophysics, 1970
Abstract The degradation of allantoate by allantoate amidohydrolase from Streptococcus allantoicus resulted in the production of 1 mole of carbon dioxide, 2 moles of NH 3 , and probably 1 mole of (−)-ureidoglycolate per mole of allantoate. Ureidoglycine was an intermediate and presumably also a substrate for allantoate amidohydrolase.
C, van der Drift, F E, de Windt, G D, Vogels   +2 more
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The characterization of amidohydrolases in a freshwater lake sediment

Microbial Ecology, 1989
The properties of three amidohydrolases, i.e., urease (I) EC 3.5.1.5, L-asparaginase (II) EC 3.5.1.1, and L-glutaminase (III) EC 3.5.1.2, were studied in sediment samples taken from a shallow eutrophic freshwater lake.Sediment samples were air dried (ADS) and stored for at least 3 months before being enzymically characterized.
Sallis, P J, Burns, Richard G
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Glutaminase activity of L-asparagine amidohydrolase

Biochemical Pharmacology, 1969
Relatively high concentrations of 6-diazo-5-oxo-norleucine (DON) and azaserine, potent specific inhibitors of many enzymes using glutamine as substrate, do not have an appreciable effect on the activity of Escherechia coliL-asparagine amido-hydrolase (EC 3.5.1.1) when either asparagine or glutamine is used as substrate.
H K, Miller, M E, Balis
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The Purification and Properties of an Amidohydrolase from Soybean

Canadian Journal of Biochemistry, 1974
An amidohydrolase (EC 3.5.1.13) was isolated from the roots of soybean (Glycine max Merril, var. Hawkeye) seedlings and purified 130-fold over the crude extract with 30% recovery. The purification steps entailed ammonium sulfate precipitation, gel filtration, cellulose ion-exchange chromatography, and polyacrylamide gel electrophoresis.
R E, Hoagland, G, Graf
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