Results 211 to 220 of about 104,574 (275)

Yeast alcohol dehydrogenase II.

Archives of Biochemistry and Biophysics, 1957
Abstract Many lines of evidence support the existence of a new alcohol dehydrogenase in yeast. The new enzyme showed a broad spectrum of activity with various alcohols, ethanol having the highest activity. Its properties in many respects appear to be different from the classical alcohol dehydrogenase, and the new enzyme is more able to oxidize the ...
K. Ebisuzaki, E. G. GUZMAN BARRON
semanticscholar   +3 more sources

Inactivation of yeast alcohol dehydrogenase by N-alkylmaleimides.

Archives of Biochemistry and Biophysics, 1968
Abstract 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. Heitz, C. D. Anderson, B. Anderson
semanticscholar   +3 more sources

The zinc content of yeast alcohol dehydrogenase.

Biochemical and Biophysical Research Communications, 1976
Abstract Analyses for zinc in high specific activity preparations of yeast alcohol dehydrogenase (YADH) indicate a metal content of 1.8–1.9 moles of zinc per mole of enzyme subunit. This zinc content is observed for YADH prepared from Bakers yeast by recrystallization from Am2SO4 containing 1 mM EDTA, followed by chromatography on DE-52 and Sephadex ...
J. Klinman, K. Welsh
semanticscholar   +3 more sources

HYDROPHOBIC INTERACTIONS OF INHIBITORS WITH YEAST ALCOHOL DEHYDROGENASE.

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
Summary 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. Anderson, M. L. Reynolds, C. D. Anderson   +2 more
semanticscholar   +3 more sources

Inhibitory effects of the dietary flavonoid quercetin on the enzyme activity of zinc(II)-dependent yeast alcohol dehydrogenase: Spectroscopic and molecular docking studies.

International Journal of Biological Macromolecules, 2017
Sutanwi Bhuiya, Lucy Haque, Ankur Bikash Pradhan, Suman Das   +3 more
semanticscholar   +3 more sources

Mechanism of Action of Yeast Alcohol Dehydrogenase

Nature, 1962
B R, RABIN, E P, WHITEHEAD
openaire   +4 more sources

Transposable elements associated with constitutive expression of yeast alcohol dehydrogenase II.

Cell, 1981
V. Williamson, E. Young, M. Ciriacy
semanticscholar   +3 more sources

Production of methionol from 3-methylthiopropionaldehyde by catalysis of the yeast alcohol dehydrogenase Adh4p.

Journal of Agricultural and Food Chemistry, 2020
Methionol is a sulphur-containing aroma compound that contributes to flavors of fermented foods. In this work, a novel method for methionol production was established using 3-methylthiopropionaldehyde (MMP) and alcohol dehydrogenase (ADH).
Yixin Che, Sheng Yin, Hui Wang, Huaqing Yang, Ru Xu, Qi Wang, Yiping Wu, Julien Boutet, Robert Huet, Chengtao Wang   +9 more
semanticscholar   +1 more source

Substitution of cysteine-153 ligated to the catalytic zinc in yeast alcohol dehydrogenase with aspartic acid and analysis of mechanisms of related medium chain dehydrogenases.

Chemico-Biological Interactions, 2019
The catalytic zincs in complexes of horse liver and yeast alcohol dehydrogenases (ADH) with NAD+ and the substrate analogue, 2,2,2-trifluoroethanol, are ligated to two cysteine residues and one histidine residue from the protein and the oxygen from the ...
Keehyuk Kim, B. Plapp
semanticscholar   +1 more source

Multiple inhibition of yeast alcohol dehydrogenase

Archives of Biochemistry and Biophysics, 1965
Abstract Multiple inhibition of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol was investigated; four different inhibitors were used that were known to function competitively with respect to NAD + in these reactions. The inhibitors, adenosine diphosphate ribose, adenosine diphosphate, N 1 -methylnicotinamide chloride, and 1,10 ...
B M, Anderson, M L, Reynolds
openaire   +2 more sources