Kinetic mechanism of horse liver alcohol dehydrogenase SS

Biochemistry ◽  
1980 ◽  
Vol 19 (21) ◽  
pp. 4843-4848 ◽  
Author(s):  
Casimir N. Ryzewski ◽  
Regina Pietruszko
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kinetic Mechanism ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

Parallelism between ethanol and imidazole interactions with horse liver alcohol dehydrogenase

1978 ◽  
Vol 56 (11) ◽  
pp. 1016-1020 ◽  
Author(s):  
Patricia A. Collins ◽  
Charles S. Hanes ◽  
J. Tze-Fei Wong
Keyword(s):  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Kinetic Mechanism ◽  
Free Enzyme ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Rate Effects ◽  
Horse Liver ◽  
Substrate Concentrations ◽  
Enzyme Species

The rate effects of imidazole on the EE isoenzyme of horse liver alcohol dehydrogenase have been analysed in terms of the elucidated kinetic mechanism of the enzyme. These imidazole effects on both directions of the reaction within nonexcess as well as excess ranges of substrate concentrations pointed to the competition between imidazole and ethanol for binding to the same three enzyme species in the kinetic mechanism, namely the free enzyme, the enzyme–NAD+ complex, and the enzyme–NADH complex. Moreover, both imidazole and ethanol brought about an enhancement in the rate of dissociation of NAD+ from its binding site on the enzyme.

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