Kinetic effect of some straight chain aliphatic amines on yeast alcohol dehydrogenase

1975 ◽  
Author(s):  
Michael Dove
Keyword(s):  
Alcohol Dehydrogenase ◽  
Aliphatic Amines ◽  
Kinetic Effect ◽  
Straight Chain ◽  
Yeast Alcohol Dehydrogenase

Kinetic effect of some aliphatic amines on yeast alcohol dehydrogenase

1976 ◽  
Vol 54 (5) ◽  
pp. 432-437
Author(s):  
M. J. Dove ◽  
C. S. Tsai
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ethanol Oxidation ◽  
Initial Rate ◽  
Relative Concentration ◽  
Aliphatic Amines ◽  
Kinetic Effect ◽  
Yeast Alcohol Dehydrogenase ◽  
Protonated Amines ◽  
Ph Range

Initial rate studies of ethanol oxidation catalyzed by yeast alcohol dehydrogenase (EC 1.1.1.1) were carried out in the presence of varying concentrations of aliphatic amines over the pH range from 8.0 to 10.5. Aliphatic amines either activate or inhibit the enzyme depending on whether the pH is greater or less than 9.5 suggesting that the protonated amines activate and the nonprotonated amines inhibit the enzyme. Aliphatic amines activate yeast alcohol dehydrogenase by decreasing Kb while they inhibit the enzyme by increasing both Ka and Kia. When both protonated and nonprotonated amines are present in solution, either overall activation or inhibition will be observed depending on the relative concentration of the two amine species.

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.

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