Kinetic effects of metal ion chelating reagents and their analogues on bovine lens aldehyde dehydrogenase

Exp Eye Res. 1987 May;44(5):663-75. doi: 10.1016/s0014-4835(87)80137-9.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2,2'-Dipyridyl / pharmacology*
  • Acetaldehyde / metabolism
  • Aldehyde Dehydrogenase / antagonists & inhibitors*
  • Animals
  • Binding, Competitive
  • Cattle
  • Chelating Agents / pharmacology*
  • Kinetics
  • Lens, Crystalline / enzymology*
  • NAD / metabolism
  • Phenanthrolines / pharmacology*
  • Potassium Cyanide / pharmacology
  • Pyridines / pharmacology*

Substances

  • Chelating Agents
  • Phenanthrolines
  • Pyridines
  • NAD
  • 4,7-phenanthroline
  • 1,7-phenanthroline
  • 2,2'-Dipyridyl
  • Aldehyde Dehydrogenase
  • Acetaldehyde
  • Potassium Cyanide
  • 1,10-phenanthroline
  • 4,4'-bipyridyl