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Literature summary extracted from

  • Fullam, E.; Pojer, F.; Bergfors, T.; Jones, T.; Cole, S.
    Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme (2012), Open Biology, 2, 110026.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.2.1.1 oxythiamine inhibitor of human enzyme, is not inhibitory up to 0.03 mM. Instead, oxythiamine, at this concentration, increases the rate of the reaction by 30% under the assay conditions tested Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.1 expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.1 to 2.5 A resolution. Final model includes 410 water molecules, four thiamine diphosphate molecules, 4 Mg2+ ions and eight glycerol molecules. The enzyme forms a homodimer, where the two monomeric units are related by a non-crystallographic twofold axis. There are two dimers per asymmetric unit that are related to each other by a twofold axis to create a noncrystallographic screw axis parallel to the crystallographic Z-axis Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.1 additional information oxythiamine, inhibitor of human enzyme, is not inhibitory up to 0.03 mM. Instead, oxythiamine, at this concentration, increases the rate of the reaction by 30% under the assay conditions tested. 5-benzyl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one also has no inhibitory effect Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.1 0.4
-
 D-xylulose 5-phosphate pH 7.6, 37°C Mycobacterium tuberculosis
2.2.1.1 0.6
-
 D-fructose 6-phosphate pH 7.6, 37°C Mycobacterium tuberculosis
2.2.1.1 0.8
-
 D-ribose 5-phosphate pH 7.6, 37°C Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.1 Mg2+ The Mg2+ ion is octahedrally coordinated to residues Asp177, Asn207 and Ile209, along with two oxygen atoms of the diphosphate moiety of the cofactor thiamine diphosphate and a water molecule Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.1 Mycobacterium tuberculosis P9WG25
-
-
2.2.1.1 Mycobacterium tuberculosis H37Rv P9WG25
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.1 D-fructose 6-phosphate + Fe(CN)3-
-
 Mycobacterium tuberculosis glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
 ?
2.2.1.1 D-fructose 6-phosphate + Fe(CN)3-
-
 Mycobacterium tuberculosis H37Rv glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+
-
 ?
2.2.1.1 D-xylulose 5-phosphate + D-ribose 5-phosphate
-
 Mycobacterium tuberculosis sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 ?
2.2.1.1 D-xylulose 5-phosphate + D-ribose 5-phosphate
-
 Mycobacterium tuberculosis H37Rv sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.2.1.1 dimer crystallization data Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.1 thiamine diphosphate an active site cleft is formed between the two monomeric units allowing the cofactors thiamine diphosphate and Mg2+ to bind, such that the N-terminal domain I of chain A binds the diphosphate moiety of thiamine diphosphate, and domain II of chain B interacts with the aminopyrimidine ring. The diphosphate moiety of thiamine diphosphate is anchored in place through a number of hydrogen bonds formed with residues Thr48, His85, Ser176, Asp177, Gly178, Asn207, Ile209 and His283 from one monomer, crystallization data Mycobacterium tuberculosis