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  • Title: Slow-binding inhibition of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase.
    Author: Braga R, Hecquet L, Blonski C.
    Journal: Bioorg Med Chem; 2004 Jun 01; 12(11):2965-72. PubMed ID: 15142555.
    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.
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