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

BRENDA support

Literature summary extracted from

  • Asztalos, P.; Parthier, C.; Golbik, R.; Kleinschmidt, M.; Huebner, G.; Weiss, M.S.; Friedemann, R.; Wille, G.; Tittmann, K.
    Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate (2007), Biochemistry, 46, 12037-12052.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.1 plasmid pGSJ427 carrying the gene for TKA/His6-tag expressed in Escherichia coli strain JM109 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.1 hanging drop vapor diffusion method, transketolase in a covalent complex with donor ketoses D-xylulose 5-phosphate and D-fructose 6-phosphate at 1.47 A and 1.65 A resolution, reveal significant strain in the tetrahedral cofactor-sugar adducts with a 25-30° out-of-plane distortion of the C2-Calpha bond connecting the carbonyl of the substrates with the C2 of the cofactor’s thiazolium part. The noncovalent complex with acceptor aldose ribose 5-phosphate reveals that the sugar is present in multiple forms, in a strained ring-closed beta-D-furanose form in C2-exo conformation as well as in an extended acyclic aldehyde form, with the reactive C1 aldo function held close to Calpha of the presumably planar carbanion/enamine intermediate Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.1 H26A/H261A three hydrogen-bonding interactions between the active site and the 3-hydroxyl and 4-hydroxyl groups of the intermediate cannot be formed when compared to the wild-type Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.1 Ca2+ bound at the subunit interface Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Escherichia coli P27302
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.1 D-fructose 6-phosphate + D-ribose 5-phosphate
-
Escherichia coli D-erythrose 4-phosphate + sedoheptulose 7-phosphate
-
?
2.2.1.1 D-xylulose 5-phosphate + D-ribose 5-phosphate
-
Escherichia coli sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.2.1.1 TKA
-
Escherichia coli
2.2.1.1 transketolase A
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.1 thiamine diphosphate bound at the subunit interface Escherichia coli