Electrochemical Studies of the Effect of Temperature on the Adsorption of Yeast Alcohol Dehydrogenase at Pt

Langmuir ◽  
2001 ◽  
Vol 17 (8) ◽  
pp. 2471-2477 ◽  
Author(s):  
Ralph K. R. Phillips ◽  
Sasha Omanovic ◽  
Sharon G. Roscoe
Keyword(s):  
Alcohol Dehydrogenase ◽  
Effect Of Temperature ◽  
Electrochemical Studies ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Subunit conformation of yeast alcohol dehydrogenase.

1978 ◽  
Vol 253 (23) ◽  
pp. 8414-8419
Author(s):  
H. Jörnvall ◽  
H. Eklund ◽  
C.I. Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Yeast Alcohol Dehydrogenase

scholarly journals Isomerization of an enzyme-coenzyme complex in yeast alcohol dehydrogenase-catalysed reactions

2003 ◽  
Vol 68 (2) ◽  
pp. 77-84 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rate Constants ◽  
Equilibrium Constants ◽  
Kinetic Mechanism ◽  
Yeast Alcohol Dehydrogenase ◽  
Catalyzed Reactions ◽  
The Individual ◽  
Individual Rate ◽  
Catalyzed Oxidation

In this work, all the rate constants in the kinetic mechanism of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol by NAD+, at pH 7.0, 25 ?C, have been estimated. The determination of the individual rate constants was achieved by fitting the reaction progress curves to the experimental data, using the procedures of the FITSIM and KINSIM software package of Carl Frieden. This work is the first report in the literature showing the internal equilibrium constants for the isomerization of the enzyme-NAD+ complex in yeast alcohol dehydrogenase-catalyzed reactions.

scholarly journals Binding of coenzymes to yeast alcohol dehydrogenase

2010 ◽  
Vol 75 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin ◽  
Mira Popovic ◽  
Julijan Kandrac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Equilibrium Constants ◽  
Point Mutations ◽  
Free Energies ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Mutant Type ◽  
Yeast Alcohol Dehydrogenase ◽  
Internal Equilibrium ◽  
Individual Reaction

In this work, the binding of coenzymes to yeast alcohol dehydrogenase (EC 1.1.1.1) were investigated. The main criterions were the change in the standard free energies for individual reaction steps, the internal equilibrium constants and the overall changes in the reaction free energies. The calculations were performed for the wild type enzyme at pH 6-9 and for 15 different mutant type enzymes, with single or double point mutations, at pH 7.3. The abundance of theoretical and experimental data enabled the binding of coenzymes to enzyme to be assessed in depth.

scholarly journals Drosophila alcohol dehydrogenase frequencies and temperature

1978 ◽  
Vol 31 (1) ◽  
pp. 97-101 ◽  
Author(s):  
Maria A. Gionfriddo ◽  
Charles L. Vigue
Keyword(s):  
Environmental Factors ◽  
Alcohol Dehydrogenase ◽  
Correlation Coefficients ◽  
Effect Of Temperature ◽  
Early Fall

SUMMARYD. melanogaster imagoes were collected weekly throughout the summer and early fall of 1976. Their Adh genotypes were determined by electrophoresis. The frequency of the Adh4 isoallele fluctuated throughout the period of study. Correlation coefficients assuming no delay, one week delay, two weeks' delay, three weeks' delay, and a four-week delay of the effect of temperature on the frequency of the Adh4 isoallele were insignificant. It was concluded that temperature alone may not be a selective factor but may be selective in combination with other environmental factors.

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