Evaluating the effects of synthetic POM cycles and NAD+ kinase expression on fatty alcohol production in Saccharomyces cerevisiae. [PDF]
McNeil BA +3 more
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Autotrophic and Mixotrophic Batch Processes with Clostridium autoethanogenum LAbrini in Stirred Tank Bioreactors with Continuous Gassing. [PDF]
Oppelt A +3 more
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Ice-binding protein's dual roles for prolonging the enzymatic activity of alcohol dehydrogenase against freezing. [PDF]
Aguirre D +12 more
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Optimization of Biotechnological Vinegar Production from an Algerian Date Variety Using Indigenous Strains and Response Surface Methodology. [PDF]
Djafri K +6 more
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Yeast alcohol dehydrogenase II
Archives of Biochemistry and Biophysics, 1957Abstract 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 S, GUZMAN BARRON
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Multiple inhibition of yeast alcohol dehydrogenase
Archives of Biochemistry and Biophysics, 1965Abstract 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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Adventitious inhibition of yeast alcohol dehydrogenase
Archives of Biochemistry and Biophysics, 1960Abstract 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 +3 more
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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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Rapid purification of yeast alcohol dehydrogenase
Analytical Biochemistry, 1981Abstract Making use of the unusual stability of yeast alcohol dehydrogenase in the presence of ethanol, a simple, rapid procedure for isolating this enzyme in high yield is presented. Once-crystallized enzyme is obtained within 5 h of commencing the procedure; this is undegraded and substantially free of proteolytic activity.
R K, Scopes +2 more
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Catalysis by Yeast Alcohol Dehydrogenase
1990Table 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 +6 more
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