Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme with a key role in energy production, catalyzing the conversion of glyceraldehyde-3-phosphate to
1,3-bisphosphoglycerate (10).
furiosus, where GAP oxidation is coupled to the reduction of ferredoxin instead of NAD, resulting in the conservation of energy at the ferredoxin oxidation step via a respiratory membrane-bound hydrogenase [27, 28] rather than by substrate level phosphorylation (SLP) via
1,3-bisphosphoglycerate [3, 5].
In chloroplasts GAPDH catalyzes the reduction of
1,3-bisphosphoglycerate to produce glycerinaldehyd-3-phosphate.
brucei GAPDH, a specific glycolytic enzyme which catalyses the phosphorylation of glyceraldehyde-3-phosphate to
1,3-bisphosphoglycerate with NAD+ and inorganic phosphate, with an IC50 value of 240 [micro]M and to do so as a competitive inhibitor of this enzyme (Nyasse et al.
First the ATP removes one phosphate group from its tail and attaches it to the phosphoglycerate to make
1,3-bisphosphoglycerate. Then NADPH donates its proton and removes the phosphate group from
1,3-bisphosphoglycerate to create glyceraldehyde 3-phosphate (G-3-P or PGAL).