Results 151 to 160 of about 23,804 (206)

Ice-binding protein's dual roles for prolonging the enzymatic activity of alcohol dehydrogenase against freezing. [PDF]

open access: yesInt J Biol Macromol
Aguirre D   +12 more
europepmc   +1 more source

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 S, GUZMAN BARRON
openaire   +2 more sources

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

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   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

Rapid purification of yeast alcohol dehydrogenase

Analytical Biochemistry, 1981
Abstract 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
openaire   +2 more sources

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   +6 more
openaire   +2 more sources

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