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Inactivation of Yeast Alcohol Dehydrogenase by Nitrilopropionamides
Journal of Enzyme Inhibition, 1994A series of halonitrilopropionamides have been examined as potential inhibitors of yeast alcohol dehydrogenase. Analogues with a good leaving group on the alpha-carbon, and a geminal electronegative atom, were found to be initial competitive inhibitors against NAD with inhibition constants as low as 0.6 microM.
G C, Shiao, V, Kathardekar, R E, Viola
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Stability of immobilized yeast alcohol dehydrogenase
Biotechnology and Bioengineering, 1981AbstractThe effects of substrate on stabilities of native (NA) and three kinds of immobilized yeast alcohol dehydrogenase (IMA), namely PGA (the carrier; porous glass), SEA (agarose gel) prepared covalently, and AMA (anion‐exchange resin) prepared ionically, were studied. The following results were obtained.
Hiroshi Ooshima +2 more
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Interaction of Yeast Alcohol Dehydrogenase with Protoberberine Alkaloids
Journal of Enzyme Inhibition, 1985Oxidation of ethanol and reduction of aldehyde catalysed by yeast alcohol dehydrogenase is inhibited by several naturally occurring as well as semi-synthetic protoberberine alkaloids. The affinity of these compounds for the enzyme depends essentially on their hydrophobicity.
J, Kovár, J, Stejskal, L, Matyska
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Regulation of Yeast Alcohol Dehydrogenase Isozymes
1981The two major alcohol dehydrogenases of yeast are coded by separate nuclear genes, and show 95% amino acid homology. Nonetheless, the “constitutive” ADH, ADH-I, preferentially catalyzes the reaction acetaldehyde → ethanol, and the inducible ADH, ADH-II, preferentially catalyzes the reverse reaction.
Christopher Wills +2 more
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The intrinsic zinc atoms of yeast alcohol dehydrogenase
Biochemical and Biophysical Research Communications, 1975The intrinsic Zn content of yeast alcohol dehydrogenase (YADH) has been determined by three highly sensitive analytical techniques. The enzyme prepared from baker's yeast has a specific activity of 430–460 U/mg and contains 4 intrinsically bound Zn atoms per tetrameric enzyme of molecular weight 150,000.
C, Veillon, A J, Sytkowski
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Studies on methylated yeast alcohol dehydrogenase
Bioorganic Chemistry, 1980Abstract The incubation of yeast alcohol dehydrogenase with formaldehyde in the presence of NaBH 4 methylates lysine residues to form ϵ N ,ϵ N -dimethyl lysine with a concurrent decrease in enzymic activity which is not alleviated by the presence of coenzymes.
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Alcohol dehydrogenase activity in the yeast Lipomyces starkeyi
Biochimica et Biophysica Acta (BBA) - Enzymology, 1970Abstract The oxidation of ethanol and the NAD-dependent alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) activity were studied in the aerobic yeast Lipomyces starkeyi. Cells grown on glucose as a carbon source contain little ethanol dehydrogenase activity, but do contain an enzyme which oxidizes cinnamyl alcohol.
H M, Heick, M, Barrette
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International Journal of Biological Macromolecules, 2015
M. Shakir +6 more
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M. Shakir +6 more
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Redox-elimination reaction catalyzed by yeast alcohol dehydrogenase.
Biochemistry international, 1991Yeast alcohol dehydrogenase (EC 1.1.1.1) catalyzed reduction of N,N-dimethyl-4-nitrosoaniline by NADH. The stoichiometry of reaction, steady-state kinetic parameters, and the pH-profile for this reaction were estimated. On that basis, the minimal mechanism of the above reaction was postulated.
Trivić, Svetlana, Leskovac, Vladimir
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