May 1, 1994

Glyoxylate for affinity labelling of 6-phosphogluconate dehydrogenase

Bollettino della Società italiana di biologia sperimentale
S Hanau, M Berteilli

Abstract

In order to find a new reagent for the affinity labelling, 6-phosphogluconate dehydrogenase was treated with glyoxylate, a versatile metabolite with a carboxyl and a reactive aldehydic group. High concentrations of glyoxylate inhibit the enzyme, while in the presence of the reducing agent cyanoborohydride, the enzyme is irreversibly inactivated by only millimolar glyoxylate. This indicates the formation of a Schiff base between the aldehydic group of glyoxylate and one enzyme lysine residue. The kinetics and substrate competition suggest that inactivation is due to affinity labelling. In the first step the inhibitor carboxylic group binds to the substrate carboxyl binding site, and in the second slower step the aldehydic group binds a nearby lysine. We have also found that other enzymes are inactivated by the combined actions of glyoxylate and cyanoborohydride, with a saturation kinetics. Hence, glyoxylate can be helpful to identify specific lysines at the carboxyl binding sites in proteins.

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Mentioned in this Paper

Enzymes, antithrombotic
Dall Sheep
Lysine
Ligand Binding Domain
Phosphogluconate Dehydrogenase
Glyoxylates
Enzymes for Treatment of Wounds and Ulcers
Binding (Molecular Function)
Urine Lysine Measurement
Glyoxylic acid, sodium salt, 2-(14)C-labeled

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