Abstract 2863 Structural characterization of covalent GAPDH inhibitors

Sugar metabolism is a universally shared metabolic pathway, and all known organisms employ an electron gradient to generate ATP. The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) stands at the intersection of these two pathways, catalyzing an important step in the conversion of glucose to pyruvate and producing the essential electron carrier NADH. In addition to its catalytic role, GAPDH appears to act as a sensor for assessing the status of the cellular oxidative state. A particular active-site cysteine residue is critical to both roles.