Results 221 to 230 of about 25,198 (259)
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Borate inhibition of yeast alcohol dehydrogenase
Biochemistry, 1976Yeast alcohol dehydrogenase is inhibited competitively by borate with respect to NAD+. An unusual mechanism of competitive inhibition prevails: the competition for the substrate NAD+ by borate and enzyme. The following evidence supports this conclusion. (1) Much greater inhibition is observed with respect to NAD+ as compared with NADH as substrates. (2)
K W, Smith, S L, Johnson
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Functional Mutants of Yeast Alcohol Dehydrogenase
1982Selection of petite strains of yeast (that is, strains unable to respire aerobically) on media containing allyl alcohol will result in enrichment for mutants at the ADC1 locus. This locus codes for the constitutive alcohol dehydrogenase, ADH-I, which is primarily responsible for the production of ethanol in yeast. The mutant enzymes are functional, and
C, Wills, P, Kratofil, T, Martin
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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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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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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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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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Induction of isoenzymes of alcohol dehydrogenase in ?flor? yeast
Archiv f�r Mikrobiologie, 1972Two isoenzymes of alcohol dehydrogenase (adh I and adh II) from Saccharomyces cheresiensis have been differentiated by thermal treatment of the crude extracts. The effect of pH on the stability and the Km for ethanol are different for the two isoenzymes.
M J, Fernández +2 more
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Nitrogen base inhibition of yeast alcohol dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966Summary The oxidation of ethanol as catalyzed by yeast alcohol dehydrogenase (alcohol: NAD + oxidoreductase, EC 1.1.1.1) is inhibited by a variety of nitrogen bases. Inhibition by 2,9-dimethyl-1,10-phenanthroline, 1,5-phenanthroline, 5,6-benzoquinoline, 7,8-benzoquinoline, quinoline and adenosine was in each case shown to be competitive with respect
B M, Anderson +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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Effect of Rotenone on the Alcohol Dehydrogenase of Yeast Mitochondria
Nature, 1967CHANCE1 applied the crossover theorem to a study of intact yeast cells, and reported an apparent crossover point (or phosphorylation site) between pyridine nucleotide and flavoprotein (site I), between cytochromes b and c (site II) and between eytochrome c and cytochrome oxidase (site III). These observations led to the expectation that intact isolated
W X, Balcavage, J R, Mattoon
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