Glycerol-3-Phosphate Dehydrogenase 2 (GPD2)

GPD2, is located on the outer surface of the inner mitochondrial membrane and catalyzes the unidirectional conversion of glycerol-3-phosphate to dihydroxyacetone phosphate with concomitant reduction of the enzyme-bound FAD. Together with a cytosolic NAD-linked GPD, GPD2 forms the glycerol phosphate shuttle, which uses the interconversion of G-3-P and DHAP to transfer reducing equivalents into mitochondria, resulting in the reoxidation of NADH formed during glycolysis.The deduced protein contains a leader peptide, followed by a FAD-binding domain, 2 central conserved regions postulated to play a role in glycerol phosphate binding, and 2 C-terminal calcium-binding domains. The calcium-binding region shows greatest homology with the calmodulin and troponin-C subfamilies of the EF-hand family of proteins.