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Literature summary for 2.2.1.1 extracted from

  • Esakova, O.A.; Meshalkina, L.E.; Kochetov, G.A.
    Effects of transketolase cofactors on its conformation and stability (2005), Life Sci., 78, 8-13.
    View publication on PubMed

General Stability

General Stability Organism
holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart Saccharomyces cerevisiae
Mg2+ holoenzyme reconstituted in the presence of Ca2+ is more stable than its Mg2+ counterpart Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the enzyme is more stable in presence of Ca2+ than Mg2+. Thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate thiamine diphosphate increases the stability of the apoenzyme regardless of wether Mg2+ or Ca2+ is present in the medium Saccharomyces cerevisiae