Literature summary for 2.2.1.1 extracted from

Egan, R.M.; Sable, H.Z.
Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits (1981), J. Biol. Chem., 256, 4877-4883.

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Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	-	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic data concerning the lag phase of transketolase reaction	Saccharomyces cerevisiae

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	can replace Mg2+ to some extent	Saccharomyces cerevisiae
Mg2+	requirement	Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-xylulose 5-phosphate + D-ribose 5-phosphate	Saccharomyces cerevisiae	-	sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	r

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	baker's yeast	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-xylulose 5-phosphate + D-ribose 5-phosphate	-	Saccharomyces cerevisiae	sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	r

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)