scholarly journals Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase.

1982 ◽  
Vol 257 (23) ◽  
pp. 14349-14358 ◽  
Author(s):  
H Eklund ◽  
B V Plapp ◽  
J P Samama ◽  
C I Brändén
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complex ◽  
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.

Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution

1981 ◽  
Vol 146 (4) ◽  
pp. 561-587 ◽  
Author(s):  
Hans Eklund ◽  
Jean-Pierre Samama ◽  
Leif Wallén ◽  
Carl-Ivar Brändén ◽  
Åke Åkeson ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complex ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver

Low-affinity interaction of ethanol with the fluorescent complex between horse liver alcohol dehydrogenase and auramine O

1976 ◽  
Vol 54 (3) ◽  
pp. 287-290
Author(s):  
Patricia M. Bronskill ◽  
J. Tze-Fei Wong
Keyword(s):  
Alcohol Dehydrogenase ◽  
Solvent Effect ◽  
Ternary Complex ◽  
Competitive Displacement ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Kinetic System ◽  
Auramine O ◽  
Affinity Interaction

Quenching of the fluorescence of the complex between horse liver alcohol dehydrogenase (alcohol:NAD+ oxidoreductase (EC 1.1.1.1)) and auramine O complex is inconsistent with a simple competitive displacement of auramine O by ethanol. Instead, the action of ethanol requires an explanation in terms of a solvent effect, or the formation of an enzyme – auramine O – ethanol ternary complex. The latter complex would have to be the low-affinity variety similar to the enzyme–NADH–ethanol ternary complex encountered in the kinetic system.

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