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Literature summary extracted from

  • Sevostyanova, I.A.; Selivanov, V.A.; Yurshev, V.A.; Solovjeva, O.N.; Zabrodskaya, S.V.; Kochetov, G.A.
    Cooperative binding of substrates to transketolase from Saccharomyces cerevisiae (2009), Biochemistry (Moscow), 74, 789-792.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.1 0.014
-
 D-ribose 5-phosphate pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+ Saccharomyces cerevisiae
2.2.1.1 0.021
-
 D-xylulose 5-phosphate pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Ca2+ Saccharomyces cerevisiae
2.2.1.1 0.115
-
 D-xylulose 5-phosphate pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Mg2+ Saccharomyces cerevisiae
2.2.1.1 0.115
-
 D-xylulose 5-phosphate pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Mg2+ Saccharomyces cerevisiae
2.2.1.1 0.4
-
 D-ribose 5-phosphate pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied, presence of Mg2+ Saccharomyces cerevisiae
2.2.1.1 0.4
-
 D-ribose 5-phosphate pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Mg2+ Saccharomyces cerevisiae
2.2.1.1 0.5
-
 D-xylulose 5-phosphate pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+ Saccharomyces cerevisiae
2.2.1.1 0.6
-
 D-ribose 5-phosphate pH 7.6, 25°C, affinity to the second active center when the first center is occupied, presence of Ca2+ Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.1 Ca2+ in the presence of Ca2+, the enzyme exhibits strong negative active site cooperativity in both xylulose 5-phosphate binding and ribose 5-phosphate binding and positive cooperativity in the catalytic activity Saccharomyces cerevisiae
2.2.1.1 Mg2+ nonequivalence of the active sites is not observed in presence of Mg2+ Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Saccharomyces cerevisiae
-
-
-

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 in presence of Ca2+, the active centers of the enzyme are nonequivalent with respect to both ribose 5-phosphate and xylulose 5-phosphate binding Saccharomyces cerevisiae sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
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