Literature summary for 2.2.1.1 extracted from

Esakova, O.A.; Khanova, E.A.; Meshalkina, L.E.; Golbik, R.; Huebner, G.; Kochetov, G.A.
Effect of transketolase substrates on holoenzyme reconstitution and stability (2005), Biochemistry, 70, 770-776.

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Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
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	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)