Results 151 to 160 of about 3,806 (190)
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Glutaminase activity of L-asparagine amidohydrolase
Biochemical Pharmacology, 1969Relatively 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, 1974An 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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Catalytic Properties of Purified Recombinant Anandamide Amidohydrolase
Prostaglandins & Other Lipid Mediators, 1999The major degradative pathway of anandamide, an endogenous ligand for cannabinoid receptors, is its enzymatic hydrolysis to arachidonic acid and ethanolamine.1The enzyme responsible for this reaction has been referred to as anandamide amidohydrolase23or fatty acid amide hydrolase.4‘N-Acylethanolamine amidohydrolase’ reported much earlier by Schmid and ...
Natsuo, Ueda +6 more
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Glycosylasparaginase Precursor and other Self-Processing N-terminal Nucleophile Amidohydrolases [PDF]
, 2013 Nathan N Aronson
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Mechanism and thermodynamics of ligand binding to auxin amidohydrolase
Journal of Molecular Recognition, 2011AbstractBrILL2 is catalytically the most efficient auxin amidohydrolase from Brassica rapa, playing a key role in auxin metabolism by catalyzing its release from amino acid conjugates. Auxins, with the most abundant representative indole‐acetic acid ([1H‐indol‐3‐yl]‐acetic acid, IAA), are a group of plant hormones that in very small concentrations ...
Simunovic, Mijo +2 more
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Enzymological and Molecular Biological Studies on Anandamide Amidohydrolase
1999Previously we suggested that anandamide amidohydrolase partially purified from porcine brain catalyzed the anandamide synthesis. The reversibility of the anandamide hydrolytic reaction was confirmed with a recombinant enzyme of rat liver. We also showed that the recombinant enzyme had a wide substrate specificity hydrolyzing primary amides and esters ...
Ueda N +8 more
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Characterization of unexplored amidohydrolase enzyme—pterin deaminase
Applied Microbiology and Biotechnology, 2016Pterin deaminase is an amidohydrolase enzyme hydrolyzing pteridines to form lumazine derivatives and ammonia. The enzyme captured the attention of scientists as early as 1959 and had been patented for its application as an anticancer agent. It is ubiquitously present in prokaryotes and has been reported in some eukaryotes such as honey bee, silkworm ...
Angayarkanni, Jayaraman +5 more
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Anandamide amidohydrolase (fatty acid amide hydrolase)
Prostaglandins & Other Lipid Mediators, 2000Anandamide (N-arachidonoylethanolamine) loses its cannabimimetic activity when it is hydrolyzed to arachidonic acid and ethanolamine by the catalysis of an enzyme referred to as anandamide amidohydrolase or fatty acid amide hydrolase. Cravatt's group and our group cloned cDNA of the enzyme from rat, human, mouse and pig, and the primary structures ...
N, Ueda, S, Yamamoto
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Structural and Catalytic Diversity within the Amidohydrolase Superfamily
Biochemistry, 2005The amidohydrolase superfamily comprises a remarkable set of enzymes that catalyze the hydrolysis of a wide range of substrates bearing amide or ester functional groups at carbon and phosphorus centers. The most salient structural landmark for this family of hydrolytic enzymes is a mononuclear or binuclear metal center embedded within the confines of a
Clara M, Seibert, Frank M, Raushel
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Purification and Characterization of Allantoate Amidohydrolase fromBacillus fastidiosus
Archives of Biochemistry and Biophysics, 1995Allantoate amidohydrolase from Bacillus fastidiosus was purified 170-fold to homogeneity as judged by isoelectric focusing and nondenaturing and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass was estimated to be 128 kDa. The enzyme appeared to be a homodimer with a subunit molecular mass of 66 kDa.
Xu, Z.W. +2 more
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