Cytosolic transketolase catalyzes the reaction of D-erythrose 4-phosphate and D-xylulose 5-phosphate to form D-glyceraldehyde 3-phosphate and D-fructose 6-phosphate. The active transketolase enzyme is a homodimer with one molecule of thiamine pyrophosphate and magnesium bound to each monomer (Wang et al. 1997).
|Reverse Reaction||D-glyceraldehyde 3-phosphate + D-fructose 6-phosphate <=> xylulose 5-phosphate + D-erythrose 4-phosphate|
|transketolase dimer||transketolase activity (0004802)|
|9357955||Aspartate 155 of human transketolase is essential for thiamine diphosphate-magnesium binding, and cofactor binding is required for dimer formation||Biochim Biophys Acta||1997|