Related Experiment Video
Updated: Aug 24, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
Slow-binding inhibition of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase
Rémi Braga1, Laurence Hecquet, Casimir Blonski
1Université Paul Sabatier, LSPCMIB, UMR 5068, Groupe de Chimie Organique Biologique, Bât IIR1, 118 Route de Narbonne, 31062 Toulouse Cedex 4, France.
Abstract:
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase is a key enzyme in the Entner-Doudoroff pathway of bacteria. It catalyzes the reversible production of KDPG from pyruvate and D-glyceraldehyde 3-phosphate through a class I Schiff base mechanism. On the basis of aldolase mechanistic pathway, various pyruvate analogues bearing beta-diketo structures were designed and synthesized as potential inhibitors. Their capacity to inhibit aldolase catalyzed reaction by forming stabilized iminium ion or conjugated enamine were investigated by enzymatic kinetics and UV-vis difference spectroscopy. Depending of the substituent R (methyl or aromatic ring), a competitive or a slow-binding inhibition takes place. These results were examined on the basis of the three-dimensional structure of the enzyme.
Related Concept Videos
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
Glycolysis: Preparatory Phase
Aldol Condensation with β-Diesters: Knoevenagel Condensation
Intramolecular Aldol Reaction
Crossed Aldol Reaction Using Weak Bases
Enzyme Inhibition
