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Literature summary for 2.2.1.1 extracted from

  • Martinez-Torres, R.J.; Aucamp, J.P.; George, R.; Dalby, P.A.
    Structural stability of E. coli transketolase to urea denaturation (2007), Enzyme Microb. Technol., 41, 653-662.
No PubMed abstract available
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Application

Application Comment Organism
biotechnology improvement of biocatalytic processes using transketolase over prolonged reaction times will need to address the formation of cofactor-associated intermediate state Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged wild-type transketolase overexpressed from Escherichia coli XL10-Gold, containing plasmid pQR791 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Urea denaturation of holo-transketolase by urea displays at least three transitions, where only the final equilibrium denaturation transition is the same for both apo-transketolase and holo-transketolase. Enzyme is deactivated initially by changes in structure associated with the cofactors, but this event does not release the cofactor from the enzyme. Holo-transketolase does not denature to apo-transketolase at 2 M urea. Complete dissociation of cofactors from holo-transketolase at 3.8 M urea without formation of the compact form of apo-transketolase (intermediate form). Holo-transketolase and apo-transketolase at 7.2 M urea both show a common denatured form Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ is necessary for the catalytic activation of thiamine diphosphate-associated apo-transketolase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P27302
-
-

Purification (Commentary)

Purification (Comment) Organism
His-tagged wild-type transketolase purified on Ni-NTA resin Escherichia coli

Storage Stability

Storage Stability Organism
4°C, 250 mM Tris-HCl buffer, pH 7.5, 2 weeks Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-hydroxypyruvate + glycolaldehyde
-
 Escherichia coli L-erythrulose + CO2
-
 ?

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate produces a degree of structure similar to that of the fully reconstituted holo-transketolase dimer without urea. Thiamine diphosphate binds to apo-transketolase in the absence of the metal ion, though in a catalytically inactive form Escherichia coli