EC Number   |
Cofactor |
Reference |
|---|
    2.2.1.1 | thiamine diphosphate |
bound at the subunit interface |
690883 |
| 2.2.1.1 | thiamine diphosphate |
dependent on |
756083, 756453, 756467 |
| 2.2.1.1 | thiamine diphosphate |
donor substrates (e.g. hydroxypyruvate or dihydroxyacetone) increase the affiniffty of the coenzyme for transketolase, whereas acceptor substrates do not. The effect of the substrate on the interaction of the coenzyme with apotransketolase and on stability of the reconstituted holoenzyme is caused by generation of 2-(alpha,beta-dihydroxyethyl)thiamine diphosphate (an intermediate product of the transketolase reaction), which has higher affinity for apotransketolase than thiamine diphosphate |
672281 |
| 2.2.1.1 | thiamine diphosphate |
homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel |
699615 |
| 2.2.1.1 | thiamine diphosphate |
i.e. functional form of vitamin B1 |
486000 |
| 2.2.1.1 | 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. Hemiholotransketolase 1 is the enzyme in which the only functional active center is the one exhibiting higher affinity for thiamine diphosphate. 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 |
690697 |
| 2.2.1.1 | thiamine diphosphate |
interaction with the coenzyme binding site of the enzyme is described |
674081 |
| 2.2.1.1 | thiamine diphosphate |
Km value is 0.074 mM |
718950 |
| 2.2.1.1 | thiamine diphosphate |
Km-value 0.0018 mM |
657667 |
| 2.2.1.1 | thiamine diphosphate |
negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+ |
659740 |
