Results 181 to 190 of about 832 (217)
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NADPH-dependent glutamate dehydrogenase activity inGibberella zeae
Experimental Mycology, 1985Abstract Glutamate dehydrogenase (GDH)-NADPH (EC 1.4.1.4) activity was examined in mycelial and spore extracts ofGibberella zeae. The specific activity of GDH-NADPH was low in spores. The specific activity of GDH-NADPH in mycelia grown from a spore suspension on a sucrose-salts medium increased greatly with time when ammonia, nitrate, or glutamine ...
Jerome J. Kinzel, John F. Leslie
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Chemistry – An Asian Journal
Abstract Biocatalytic reductions require NAD(P)H generation, which is usually achieved using a glucose / glucose dehydrogenase (GDH) system. However, certain GDHs exhibit cross‐reactivity by reducing various keto or iminium substrates during NADPH regeneration, thereby ...
Jhilik, Mondal +2 more
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Abstract Biocatalytic reductions require NAD(P)H generation, which is usually achieved using a glucose / glucose dehydrogenase (GDH) system. However, certain GDHs exhibit cross‐reactivity by reducing various keto or iminium substrates during NADPH regeneration, thereby ...
Jhilik, Mondal +2 more
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Archives of Biochemistry and Biophysics, 1988
The NADPH dehydrogenase of the cyanobacterium Anabaena variabilis was solubilized, purified, and characterized. Activity staining after nondenaturing polyacrylamide gel electrophoresis, kinetics, and immunological characterization led to the conclusion that only one thylakoid-associated NADPH dehydrogenase exists in Anabaena, identical with ferredoxin ...
S, Scherer +3 more
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The NADPH dehydrogenase of the cyanobacterium Anabaena variabilis was solubilized, purified, and characterized. Activity staining after nondenaturing polyacrylamide gel electrophoresis, kinetics, and immunological characterization led to the conclusion that only one thylakoid-associated NADPH dehydrogenase exists in Anabaena, identical with ferredoxin ...
S, Scherer +3 more
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Activities of NADPH-dependent reductases and sorbitol dehydrogenase in canine and feline lenses
American Journal of Veterinary Research, 2000Abstract Objective—To measure activities of NADPH-dependent reductases and sorbitol dehydrogenase in lenses from healthy dogs and cats. Sample Population—Lenses from 37 dogs and 23 cats. All animals were healthy and had serum glucose concentrations within reference limits.
Salgado D, Forrer RS, Spiess BM
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Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH
Biochimica et Biophysica Acta (BBA) - Enzymology, 1967Abstract 1. 1.|The saturation function of NADP + for glucose-6-phosphate dehydrogenase ( d -glucose 6-phosphate: NADP oxidoreductase, EC 1.1.1.49) from human erythrocytes (electrophoretic type A) is sigmoid-shaped under certain experimental conditions. If the data are plotted in terms of Hill's equation (J. Monod, J.-P. Changeux and F. Jacob ,
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Stereochemistry of NADPH oxidation by dihydropyrimidine dehydrogenase from pig liver
Biochemical and Biophysical Research Communications, 1992Dihydropyrimidine dehydrogenase reduces uracil to 5,6-dihydrouracil in a strictly NADPH-dependent reaction. Either by analysing the 1H-NMR spectra of the NADP+ products formed or by determination of the kinetic isotope effects of stereospecifically deuterated coenzymes dihydropyrimidine dehydrogenase was found to abstract specifically the pro-S ...
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Bioluminescent assay of NADPH-dependent isocitrate dehydrogenase and its substrates and cofactors
Analytical Biochemistry, 1985A bioluminescent assay for NADPH-dependent isocitrate dehydrogenase and for its substrates and cofactors was developed. The method is based on continuous NADPH monitoring in the reaction. The linear range of the assay for the enzyme activity is from 0.05 U/liter to 30 U/liter.
R P, Raunio +2 more
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Characterization of the general anion-binding site in glutamate dehydrogenase-NADPH complex
Biochimica et Biophysica Acta (BBA) - General Subjects, 1991The reductive amination of alpha-ketoglutarate, catalyzed by bovine liver glutamate dehydrogenase, is inhibited by various anions. Formate and acetate ions are competitive with alpha-ketoglutarate. The pH dependence of the pKi profiles for these anions reveals that they bind to the enzyme-NADPH complex only when an enzymatic residue of pK 8.0 +/- 0.1 ...
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On the mechanism of inhibiton of glutamate dehydrogenase by NADH and NADPH
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964K L, YIELDING +2 more
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