Literature summary for 2.2.1.1 extracted from

Selivanov, V.A.; Kovina, M.V.; Kochevova, N.V.; Meshalkina, L.E.; Kochetov, G.A.
Kinetic study of the H103A mutant yeast transketolase (2004), FEBS Lett., 567, 270-274.

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Protein Variants

Protein Variants	Comment	Organism
H103A	mutantion does not affect affinity of the coenzyme to apoenzyme in presence of Ca2+, but affects all the kinetic parameters for coenzyme-apoenzyme interaction in presence of Mg2+. Acceleration of one-substrate reaction with slow-down of two-substrate reaction, kinetics	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	kinetics in presence of Ca2+	Saccharomyces cerevisiae
Mg2+	kinetics in presence of Mg2+	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	H103 stabilizes reaction intermediate, kinetics	Saccharomyces cerevisiae	a

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Release 2023.1 (January 2023)