Results 161 to 170 of about 23,804 (206)

Inhibition of yeast alcohol dehydrogenase by dehydroretronecine

Food and Cosmetics Toxicology, 1977
Abstract The interaction of dehydroretronecine, a hepatocarcinogenic metabolite of the pyrrolizidine alkaloid monocrotaline, with yeast alcohol dehydrogenase (ADH), cysteine and bovine serum albumin (BSA) was studied. Dehydroretronecine inhibited ADH with an inhibition constant (Ki) of 3.38 × 10−2 m at pH 7.5 and 25 °C.
P S, Sun, M T, Hsia, F S, Chu, J R, Allen   +3 more
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Zinc Release from Irradiated Yeast Alcohol Dehydrogenase

International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1987
The release of Zn2+ from gamma-irradiated yeast alcohol dehydrogenase has been measured using atomic absorption spectrometry. Radiolysis is accompanied by release of Zn2+ at a rate which is dependent on the nature of the free radicals available for reaction. Hydroxyl radicals and hydrogen atoms readily cause zinc release with G values of 0.13 and 0.11 (
S, Abelidis, J S, Moore, A, Chakravarty
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Functional Mutants of Yeast Alcohol Dehydrogenase

1982
Selection 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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Interaction of Eu3+ with Yeast Alcohol Dehydrogenase

Journal of Protein Chemistry, 1999
The activity of yeast alcohol dehydrogenase is markedly enhanced by Eu3+ ions. At pH 7.0 two binding constants for Eu3+, 1.0x10(-2) and 2.0x10(-3) microM, were obtained using a Scatchard plot. The presence of Zn2+ ions restricts the Eu3+ -induced increase in the activity of yeast alcohol dehydrogenase.
Y X, Zhang, C L, Duan, H M, Zhou
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Nitrogen base inhibition of yeast alcohol dehydrogenase

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
Summary 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, M L, Reynolds, C D, Anderson   +2 more
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Coenzyme binding capacity of yeast alcohol dehydrogenase

Biochemical and Biophysical Research Communications, 1978
Abstract Commercial lyophilized preparations of yeast alcohol dehydrogenase from Boehringer G.m.b.H. (Mannheim, Germany) bind 2 mols of reduced coenzyme/144000 g of enzyme (1). After the purification by a DEAE-Sephadex column chromatography, the coenzyme binding capacity is raised to 4 mols of NADH/mol of enzyme.
V, Leskovac, D, Pericin
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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 P, Klinman, K, Welsh
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Cryo-Electron Microscopy Structures of Yeast Alcohol Dehydrogenase

Biochemistry, 2021
Structures of yeast alcohol dehydrogenase determined by X-ray crystallography show that the subunits have two different conformational states in each of the two dimers that form the tetramer. Apoenzyme and holoenzyme complexes relevant to the catalytic mechanism were described, but the asymmetry led to questions about the cooperativity of the subunits ...
Sai Rohit Guntupalli, Zhuang Li, Leifu Chang, Bryce V. Plapp, Ramaswamy Subramanian   +4 more
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Inactivation of Yeast Alcohol Dehydrogenase by Nitrilopropionamides

Journal of Enzyme Inhibition, 1994
A 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, 1981
AbstractThe 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, Yumiko Genko, Yoshio Harano   +2 more
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