Cytosolic glyceraldehyde 3-phosphate dehydrogenase catalyzes the reversible reaction of glyceraldehyde 3-phosphate, orthophosphate, and NAD+ to form NADH + H+ and 1,3-bisphosphoglycerate, the first energy rich intermediate of glycolysis. The biochemical details of this reaction were worked out by C and G Cori and their colleagues (Taylor et al. 1948; Cori et al. 1948).
While there are multiple human glyceraldehyde 3-phosphate dehydrogenase-like pseudogenes, there is only one glyceraldehyde 3-phosphate dehydrogenase gene expressed in somatic tissue (Benham and Povey 1989; Heinz and Freimuller 1982; Ercolani et al. 1988), and studies of aged human erythrocytes suggest that variant forms of the enzyme arise as a result of post-translational modifications (Edwards et al. 1976). There is, however, an authentic second isoform of glyceraldehyde 3-phosphate dehydrogenase whose expression is confined to spermatogenic cells of the testis (Welch et al. 2000).
|Reverse Reaction||1,3-bisphospho-D-glycerate + NADH + H+ <=> D-glyceraldehyde 3-phosphate + Orthophosphate + NAD+|
|glyceraldehyde-3-phosphate dehydrogenase tetramer||glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity (0004365)|
|2793178||Members of the human glyceraldehyde-3-phosphate dehydrogenase-related gene family map to dispersed chromosomal locations.||Genomics||1989|
|Crystalline D-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle||J Biol Chem||1948|
|183598||Isozymes of glyceraldehyde-3-phosphate dehydrogenase in man and other mammals.||Ann Hum Genet||1976|
|3170585||Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene||J Biol Chem||1988|
|7144574||Glyceraldehyde-3-phosphate dehydrogenase from human tissues.||Methods Enzymol||1983|
|10714828||Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells.||J Androl||2000|
|18910717||The prosthetic group of crystalline d-glyceraldehyde-3-phosphate dehydrogenase||J. Biol. Chem.||1948|