Mechanisms of Enzyme-catalyzed Oxidation-Reduction Reactions. I. An Investigation of the Yeast Alcohol Dehydrogenase Reaction by Means of the Isotope Rate Effect1,2

1957 ◽  
Vol 79 (5) ◽  
pp. 1159-1166 ◽  
Author(s):  
H. R. Mahler ◽  
Joyce Douglas
Keyword(s):  
Alcohol Dehydrogenase ◽  
Reduction Reactions ◽  
Yeast Alcohol Dehydrogenase ◽  
Oxidation Reduction ◽  
Dehydrogenase Reaction ◽  
Catalyzed Oxidation

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.

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