Kinetic effects of metal ion chelating reagents and their analogues on bovine lens aldehyde dehydrogenase.
The chelating agents 1,10-phenanthroline and 2,2'-dipyridyl gave partial inhibition of the bovine lens aldehyde dehydrogenase, which was fully reversible and competitive towards acetaldehyde. The non-chelating compounds, 1,7-phenanthroline, 4,7-phenanthroline and 4,4'-dipyridyl gave total competitive inhibition, and significant activation at saturating substrate and coenzyme concentrations, in a manner similar to cyanide. All five isomers prevented the binding of the coenzyme NAD+, the non-chelating phenanthroline compounds being the most effective. An overall mechanism for inhibition by single and bidentate ligands is proposed.
D015082:2,2'-Dipyridyl / Q000494:pharmacology*; D000079:Acetaldehyde / Q000378:metabolism; D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors*; D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002614:Chelating Agents / Q000494:pharmacology*; D007700:Kinetics; D007908:Lens, Crystalline / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D010618:Phenanthrolines / Q000494:pharmacology*; D011190:Potassium Cyanide / Q000494:pharmacology; D011725:Pyridines / Q000494:pharmacology*
D002614:Chelating Agents; D010618:Phenanthrolines; D011725:Pyridines; D009243:NAD; C053487:4,7-phenanthroline; C053486:1,7-phenanthroline; D015082:2,2'-Dipyridyl; D000444:Aldehyde Dehydrogenase; D000079:Acetaldehyde; D011190:Potassium Cyanide; C025205:1,10-phenanthroline; C034306:4,4'-bipyridyl