Histidine and aspartate side chains are chiefly used to complex the substrate of this enzyme, while two arginine residues are key to the functioning of its active site.
Overexpression of one isoform of this enzyme plays a role in compensating for the Warburg effect in cancer cells. Histidine and aspartate side chains are chiefly used to complex the substrate of this enzyme, while two arginine residues are key to the functioning of its active site. Activity of this enzyme is reduced, particularly in erythrocytes, in patients with Wernicke's encephalopathy, Korsakoff's syndrome, or beriberi because its cofactor contains thiamine. This enzyme with cofactor TPP catalyzes the formation of glucose-6-P and glyceraldehyde-3-P in a cytosolic pathway that forms NADPH and its namesake five-carbon sugars. For 10 points, name this enzyme that catalyzes the conversion of sedoheptulose-7-P and glyceraldehyde-3-P to D-ribose-5P and D-xylulose-5-P in the Calvin cycle or the reverse reaction in the pentose phosphate pathway.
Overexpression of one isoform of this enzyme plays a role in compensating for the Warburg effect in cancer cells.
{transketolase}