Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer

Biochemistry ◽  
2020 ◽  
Vol 59 (7) ◽  
pp. 862-879
Author(s):  
Keehyuk Kim ◽  
Bryce V. Plapp
Keyword(s):  
Amino Acid ◽  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Hydrogen Transfer ◽  
Substrate Binding ◽  
Amino Acid Residues ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Substrate Binding Site ◽  
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.

Discrimination of the prochiral hydrogens at the C-2 position of n-alkanes by the methane/ammonia monooxygenase family proteins

2015 ◽  
Vol 13 (30) ◽  
pp. 8261-8270 ◽  
Author(s):  
Akimitsu Miyaji ◽  
Teppei Miyoshi ◽  
Ken Motokura ◽  
Toshihide Baba
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Substrate Binding ◽  
Amino Acid Residues ◽  
Ammonia Monooxygenase ◽  
Substrate Binding Site ◽  
Copper Site ◽  
The Family ◽  
Discriminating Ability

The substrate binding site of AMO/pMMO family proteins can discriminate between the prochiral hydrogens at the C-2 position ofn-alkanes. We predict that at least one of the three amino acid residues at the di-copper site affects the discriminating ability of the family proteins.

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