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Literature summary for 2.2.1.1 extracted from

  • Ospanov, R.V.; Kochetov, G.A.; Kurganov, B.I.
    Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase (2007), Biochemistry (Moscow), 72, 84-92.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ thiamine diphosphate affinity to the enzyme’s active sites is higher in the presence of Ca2+ than in the presence of Mg2+ Saccharomyces cerevisiae
Mg2+ thiamine diphosphate affinity to the enzyme’s active sites is higher in the presence of Ca2+ than in the presence of Mg2+ Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information transketolase reaction is irreversible when hydroxypyruvate is used as a donor substrate Saccharomyces cerevisiae ?
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?

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate two-step mechanism of interaction of thiamine diphosphate with transketolase. Formation of inactive intermediate complex followed by its transformation into catalytically active holoenzyme Saccharomyces cerevisiae