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