Results 121 to 130 of about 1,029 (146)

Adventitious inhibition of yeast alcohol dehydrogenase

Archives of Biochemistry and Biophysics, 1960
Abstract The inhibition of yeast alcohol dehydrogenase by N′ -methylnicotinamide has been shown to be due to contaminating silver ions present in commercial preparations of this reagent. Contamination by metal ions, which was assessed by quantitative analysis, also accounts for the inhibition of yeast alcohol dehydrogenase by semicarbazide ...
F L, HOCH, R G, MARTIN, W E, WACKER, B L, VALLEE   +3 more
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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
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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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Catalysis by Yeast Alcohol Dehydrogenase

1990
Table 7 presents a brief summary of the effects of various mutations on some of the relevant kinetic constants. The results illustrate several important features of the use of site-directed mutagenesis in exploring structure and function of enzymes. Note that most of the mutations affect a given step or kinetic parameter in the mechanism, such as the ...
B V, Plapp, A J, Ganzhorn, R M, Gould, D W, Green, T, Jacobi, E, Warth, D A, Kratzer   +6 more
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Borate inhibition of yeast alcohol dehydrogenase

Biochemistry, 1976
Yeast 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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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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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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Alcohol dehydrogenase activity in the yeast Lipomyces starkeyi

Biochimica et Biophysica Acta (BBA) - Enzymology, 1970
Abstract 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, 1985
Oxidation 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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Induction of isoenzymes of alcohol dehydrogenase in ?flor? yeast

Archiv f�r Mikrobiologie, 1972
Two 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, C, Gómez-Moreno, M, Ruiz-Amil   +2 more
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