EC Number   |
Cofactor |
Reference |
|---|
    2.2.1.1 | thiamine diphosphate |
not thiamine, thiamine mono-or triphosphate |
485991, 486005, 486006 |
| 2.2.1.1 | thiamine diphosphate |
produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form |
692117 |
| 2.2.1.1 | thiamine diphosphate |
requirement, thiamine diphosphate protein, tightly bound |
486012, 486013 |
| 2.2.1.1 | thiamine diphosphate |
theoretical analysis of interaction between thiamine diphosphate-binding sites of transketolase and determination of equilibrium and kinetic constants of individual stages of the interaction between thiamine diphosphate and the apoenzyme in the presence of Ca2+ |
672288 |
| 2.2.1.1 | thiamine diphosphate |
thiamine B-ring is an essential component of catalysis |
691299 |
| 2.2.1.1 | thiamine diphosphate |
thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium |
675747 |
| 2.2.1.1 | thiamine diphosphate |
two lysine residues and a serine interact with the beta-phosphate of thiamine diphosphate. Residue Gln189 spans over the thiazolium moiety of thiamine diphosphate |
719890 |
| 2.2.1.1 | thiamine diphosphate |
two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme |
691025 |
| 2.2.1.1 | thiamine diphosphate |
with different affinities for the cofactor |
486002 |
