Amino Acid Residues in the Nicotinamide Binding Site Contribute to Catalysis by Horse Liver Alcohol Dehydrogenase†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2907-2915 ◽  
Author(s):  
Jon K. Rubach ◽  
Bryce V. Plapp
Keyword(s):  
Amino Acid ◽  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Amino Acid Residues ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

scholarly journals Contribution of buried distal amino acid residues in horse liver alcohol dehydrogenase to structure and catalysis

2018 ◽  
Vol 27 (3) ◽  
pp. 750-768 ◽  
Author(s):  
Karthik K. Shanmuganatham ◽  
Rachel S. Wallace ◽  
Ann Ting-I Lee ◽  
Bryce V. Plapp
Keyword(s):  
Amino Acid ◽  
Alcohol Dehydrogenase ◽  
Amino Acid Residues ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

Interaction of horse liver alcohol dehydrogenase with acridine orange

1981 ◽  
Vol 46 (9) ◽  
pp. 2268-2277 ◽  
Author(s):  
Jan Kovář ◽  
Eva Dürrová
Keyword(s):  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Acridine Orange ◽  
Binding Sites ◽  
Ternary Complex ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

The inhibition of horse liver alcohol dehydrogenase by acridine orange was studied as a function of the concentration of the two coenzyme and substrate forms, the inhibitor concentration, pH, and in the presence of other inhibitors of the enzyme. The changes in optical properties, of the dye occurring during its binding to the enzyme (especially the absorption spectra and the fluorescence polarization) were also studied. The existence of an efficient resonance energy transfer from the excited NADH molecule to the acridine orange molecule in the corresponding ternary complex with the enzyme has also been demonstrated. The results obtained provide evidence showing that the binding site of alcohol dehydrogenase for acridine orange differs from the binding sites of this enzyme for both the coenzyme and the substrate. This binding site most likely is localized in a large substrate pocket of the enzyme near to the binding sites for o-phenanthroline and berberine and very close to the binding site for tricyclic psychochemicals.

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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