Results 171 to 180 of about 23,804 (206)
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Inactivation of yeast alcohol dehydrogenase by N-alkylmaleimides
Archives of Biochemistry and Biophysics, 1968Abstract Seven N-alkylmaleamic acids were synthesized and converted through heating to the corresponding N-alkylmaleimides. Alkylmaleimides of varying chainlength were shown to effectively inactivate yeast alcohol dehydrogenase at pH 7.0. The effect of pH on the rate of hydrolysis of N-ethylmaleimide was studied in the pH range from 8.6 to 9.4 where ...
J R, Heitz, C D, Anderson, B M, Anderson
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Hydrophobic interactions of inhibitors with yeast alcohol dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965Summary Eleven N1-alkylnicotinamide chlorides have been prepared and studied as inhibitors in the yeast alcohol dehydrogenase (alcohol :NAD+ oxidoreductase, EC 1.1.1.1) catalyzed oxidation of ethanol. The effectiveness of these inhibitors increased with increasing chain length of the alkyl substituent.
B M, ANDERSON +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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Production of yeast alcohol dehydrogenase isoenzymes by selection
Nature, 1976Mutants of yeast alcohol dehydrogenase have been produced that protect the cell against the poisonous aldehyde acrolein by increasing the NADH-NAD ratio. The altered properties include changes both in binding constants and in cooperativity. Such mutants may be useful in exploring the nature of adaptation at the molecular level.
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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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American Cancer Society nutrition and physical activity guideline for cancer survivors
Ca-A Cancer Journal for Clinicians, 2022Cheryl L Rock +2 more
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