Literature summary for 2.2.1.1 extracted from

Esakova, O.A.; Meshalkina, L.E.; Golbik, R.; Hubner, G.; Kochetov, G.A.
Donor substrate regulation of transketolase (2004), Eur. J. Biochem., 271, 4189-4194.

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Inhibitors

Inhibitors	Comment	Organism	Structure
N3'-pyridyl-thiamine	inactive analogue of thiamine diphosphate	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate	donor substrate, but not acceptor substrate, enhances affinity of cofactor to apoenzyme to a different degree for the two active centers, resulting in a negative cooperativity for cofactor binding. Reaction intermediate is a 2-(alpha,beta-dihydroxyethyl)-thiamine diphosphate, which exhibits a higher affinity for the enzyme than thiamine diphosphate	Saccharomyces cerevisiae	a

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)