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Literature summary for 2.2.1.1 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
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Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
F434A the mutation leads to 53% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal) Escherichia coli
F434L the mutation leads to 74% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
H261A the mutation leads to 75% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
H261F the mutation leads to 33% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
H261G the mutation leads to 59% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
H261L the mutation leads to 55% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
H261V the mutation leads to 65% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
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
H26A/H261A the mutation leads to 54% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal) Escherichia coli
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
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
L382A the mutation leads to 97% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
L382A/F434A the mutation leads to 66% ee (S) after 1 h in the reaction of 3-hydroxypyruvate and n-pentanal Escherichia coli
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P27302
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
TktA
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent on Escherichia coli