Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.2.1.1 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

Application Comment Organism
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)

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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