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Literature summary extracted from

  • Baierl, A.; Theorell, A.; Mackfeld, U.; Marquardt, P.; Hoffmann, F.; Moers, S.; Noeh, K.; Buchholz, P.; Pleiss, J.; Pohl, M.
    Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase (2018), ChemCatChem, 10, 2601-2611 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.1 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.1 F434A the mutation leads to 53% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal) Escherichia coli
2.2.1.1 F434L the mutation leads to 74% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 H261A the mutation leads to 75% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 H261F the mutation leads to 33% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 H261G the mutation leads to 59% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 H261L the mutation leads to 55% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 H261V the mutation leads to 65% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 H26A the mutation results in stereoinversion for the formation of 1,3-dihydroxy-2-heptanone, with a lower ee-value of 18% (R) as compared to the wild type enzyme Escherichia coli
2.2.1.1 H26A/H261A the mutation leads to 54% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal) Escherichia coli
2.2.1.1 H26W the mutant shows an 8fold decreased formation of (R)-1,3-dihydroxy-2-heptanone and an ee-value of 30% (S) after 1 h reaction time Escherichia coli
2.2.1.1 H26Y the mutant catalyzes the formation of (R)-1,3-dihydroxy-2-heptanone with an ee-value of 98% and a yield of 8% after 1 h Escherichia coli
2.2.1.1 L382A the mutation leads to 97% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 L382A/F434A the mutation leads to 66% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
2.2.1.1 L382A/F434L the mutation leads to 10% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.1 Mg2+ required for activity Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.1 sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate Escherichia coli
-
 D-ribose 5-phosphate + D-xylulose 5-phosphate
-
 r

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.2.1.1 Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.1 3-hydroxypyruvate + n-pentanal 3% yield after 1 h (92% (S)), 12% yield after 3 h (87% (S)) Escherichia coli 1,3-dihydroxy-2-heptanone + CO2
-
 ir
2.2.1.1 3-hydroxypyruvate + propanal 12% yield after 1 h (57% (S)), 32% yield after 3 h (53% (S)) Escherichia coli 1,3-dihydroxy-2-pentanone + CO2
-
 ir
2.2.1.1 D-erythrose 4-phosphate + D-xylulose 5-phosphate
-
 Escherichia coli D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
-
 r
2.2.1.1 sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 Escherichia coli D-ribose 5-phosphate + D-xylulose 5-phosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.2.1.1 TktA
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.1 thiamine diphosphate dependent on Escherichia coli