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Literature summary for 2.2.1.1 extracted from

  • Sevostyanova, I.A.; Yurshev, V.A.; Solovjeva, O.N.; Zabrodskaya, S.V.; Kochetov, G.A.
    Effect of bivalent cations on the interaction of transketolase with its donor substrate (2008), Proteins, 71, 541-545.
    View publication on PubMed
Search for more literature for 2.2.1.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0365
-
 Xylulose 5-phosphate KM for the first active center of transketolase in the presence of Ca2+ Saccharomyces cerevisiae
0.16
-
 Xylulose 5-phosphate KM for the second active center of transketolase in the presence of Ca2+ Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ when Ca2+ is substituted for Mg2+, the two active centers of transketolase are nonequivalent in the ability to bind xylulose 5-phosphate Saccharomyces cerevisiae
Mg2+ in the presence of Mg2+, the two active centers of transketolase are equivalent in the ability to bind xylulose 5-phosphate Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
20
-
-
 Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
4°C, 50% saturated solution of ammonium sulfate, pH 7.6 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-xylulose 5-phosphate + D-ribose 5-phosphate
-
 Saccharomyces cerevisiae sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
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