FAD-dependent glycerol-3-phosphate dehydrogenase (GPDH, G3PD, or GlpD)

FAD-dependent glycerol-3-phosphate dehydrogenase is a key mitochondrial enzyme found across prokaryotes and eukaryotes, catalyzing the oxidation of glycerol-3-phosphate to dihydroxyacetone phosphate with concurrent reduction of FAD to FADH2 and transfer of electrons to ubiquinone in the electron transport chain. The enzyme is critical for integrating glycolysis with lipid metabolism and maintaining cellular redox balance. Structurally, it contains FAD-binding and substrate-binding domains, is generally dimeric, and is associated with the outer face of the inner mitochondrial membrane in eukaryotes. It has important roles in energy production, stress adaptation, and intracellular signaling. Because of its essential function in pathogen metabolism and increasingly appreciated role in cancer bioenergetics and human metabolic disorders, it is a diagnostic and therapeutic target in drug development.

Other names

Glycerol-3-phosphate dehydrogenaseGPDHG3PDGlpDFAD-glycerol-3-phosphate dehydrogenaseGlycerol-3-phosphate CoQ reductase

Enzyme inhibition: Small molecule inhibitors bind to the enzyme and block electron transfer, thereby disrupting metabolic pathways critical for parasite survival and/or cell proliferation. Electron transfer blockade may prevent NADH/NAD+ recycling and membrane potential maintenance.