Results 211 to 220 of about 10,587 (231)
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Response of amidohydrolases in soils to chloroform fumigation

Journal of Plant Nutrition and Soil Science, 2002
An ongoing challenge in enzymology is the differentiation between the various pools of enzymes in soils, i.e. between accumulated (extracellular) enzymes and enzymes associated with the microbial biomass (intracellular enzymes). In order to solve this problem, 10 surface soils representing a wide range of physico-chemical properties and purified ...
Susanne Klose, M. Ali Tabatabai
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Amidohydrolases in soils as affected by cropping systems

Applied Soil Ecology, 2003
Cropping systems influence the ecology of agricultural soils. The effects of crop rotation and N fertilization on the activities of four amidohydrolases (amidase, l-asparaginase, l-aspartase, and l-glutaminase) were studied in soils of two long-term cropping systems in Iowa: the Northeast Research Center (NERC) and the Clarion–Webster Research Center ...
Daniel E. Dodor, M. A. Tabatabai
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Enzymological and Molecular Biological Studies on Anandamide Amidohydrolase

1999
Previously 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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Anandamide amidohydrolase (fatty acid amide hydrolase)

Prostaglandins & Other Lipid Mediators, 2000
Anandamide (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 ...
Shozo Yamamoto, Natsuo Ueda
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Structural and Catalytic Diversity within the Amidohydrolase Superfamily

Biochemistry, 2005
The 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, 1995
Allantoate 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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Novel Inhibitors of Brain, Neuronal, and Basophilic Anandamide Amidohydrolase

Biochemical and Biophysical Research Communications, 1997
Mammalian brain as well as mouse neuroblastoma (N18TG2) and rat basophilic leukaemia (RBL) cells were previously shown to contain "anandamide amidohydrolase', a membrane-bound enzyme sensitive to serine and cysteine protease inhibitors and catalyzing the hydrolysis of the endogenous cannabimimetic metabolite, anandamide (arachidonoyl-ethanolamide ...
De Petrocellis L   +7 more
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Resolution of S-benzyl-DL-penicillamine with penicillin amidohydrolase [PDF]

open access: possibleCollection of Czechoslovak Chemical Communications, 1981
Racemic m-phenylacetyl-S-benzylpenicillamine was resolved into otical isomers by action of penicillin amidohydrolase (E.C.3.5.1.11) in high yield and optical purity.
Petr Šimek   +4 more
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Purification of Penicillin Amidohydrolase, an Enzyme for Semisynthetic Procedures

Collection of Czechoslovak Chemical Communications, 1992
Penicillin amidohydrolase (EC 3.5.1.11.) is one of the few enzymes used successfully for deprotection of primary amino groups of semisynthetic peptides. The available material is usually contamined by endo- and exopeptidases. We managed to prepare the enzyme devoid of trypsin- and chymotrypsin-like activities using affinity chromatography with specific
Ivo Bláha   +5 more
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Anandamide Amidohydrolase from Porcine Brain

1997
Ethanolamide of arachidonic acid was isolated from porcine brain as an endogenous ligand for cannabinoid receptors, and referred to as anandamide.1 In consideration of various biological activities of anandamide,2 it is very important to elucidate how the production and degradation of this new compound are regulated by enzymes within the cells.
Shozo Yamamoto   +3 more
openaire   +2 more sources

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