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Literature summary extracted from

  • Matosevic, S.; Lye, G.J.; Baganz, F.
    Design and characterization of a prototype enzyme microreactor: Quantification of immobilized transketolase kinetics (2009), Biotechnol. Prog., 26, 118-126.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.2.1.1 synthesis desing of an enzyme microreaktor by reversible immobilization of His6-tagged enzyme a 200-microm ID fused silica capillary for quantitative kinetic analysis. Transketolase kinetic parameters in the mircoreactor are comparable with those measured in free solution. Quantitative elution of the immobilized transketolase and the regeneration and reuse of the derivatized capillary over five cycles are possible Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.1 expression in Escherichia coli, His-taggged protein Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.1 26
-
lithium beta-hydroxypyruvate pH 7.0, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.1 lithium beta-hydroxypyruvate + glycolaldehyde
-
Escherichia coli L-erythrulose + ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2.1.1 410000
-
lithium beta-hydroxypyruvate pH 7.0, 25°C Escherichia coli