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Literature summary for 2.2.1.1 extracted from

  • Selivanov, V.A.; Kovina, M.V.; Kochevova, N.V.; Meshalkina, L.E.; Kochetov, G.A.
    Studies of thiamin diphosphate binding to the yeast apotransketolase (2003), J. Mol. Catal. B, 26, 33-40.
No PubMed abstract available
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Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+. Influence of Mg2+ is less pronounced than of Ca2+ Saccharomyces cerevisiae
Mg2+ negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+. Influence of Mg2+ is less pronounced than of Ca2+ 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 negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+, caused by increase in the rate of conformational transfer after the thiamine diphosphate binding completion in both active centers, kinetic analysis Saccharomyces cerevisiae
a

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate negative cooperativity between apoenzyme and thiamine diphosphate in presence of Ca2+ or Mg2+ Saccharomyces cerevisiae