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Literature summary 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.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.1 EDTA
-
 Saccharomyces cerevisiae

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Saccharomyces cerevisiae
-
 baker's yeast
-

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.2.1.1 25
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.1 thiamine diphosphate
-
 Saccharomyces cerevisiae