    2.2.1.1 | hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. In the presence of Ca2+, the active centers of transketolase differ in their affinity for thiamine diphosphate by approximately one order of magnitude. When adding an equimolar amount of thiamine diphosphate to apotransketolase, it becomes completely bound to the 1 active center and is not dissociated from it in the course of subsequent experiments. Hemiholotransketolase 2 is the enzyme in which the only functional active center is the one exhibiting lower affinity for the coenzyme. In order to obtain this species of transketolase, active center 1, the affinity of which for thiamine diphosphate is higher, is to be blocked by an inactive analogue of the coenzyme, hydroxythiamine diphosphate |
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