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Literature summary for 2.2.1.1 extracted from

  • Smith, M.; Hibbert, E.; Jones, A.; Dalby, P.; Hailesa, H.
    Enhancing and reversing the stereoselectivity of Escherichia coli transketolase via single-point mutations (2008), Adv. Synth. Catal., 350, 2631-2638.
No PubMed abstract available
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Protein Variants

Protein Variants Comment Organism
D469E formation of (3S)-1,3-dihydroxypentan-2-one in 90% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate Escherichia coli
D469T formation of (3S)-1,3-dihydroxypentan-2-one in 64% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate Escherichia coli
D469Y formation of (3R)-1,3-dihydroxypentan-2-one in 53% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate Escherichia coli
H26Y formation of (3R)-1,3-dihydroxypentan-2-one in 88% enantiomeric excess in the reaction of propanal + beta-hydroxypyruvate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 propanal + 2 lithium beta-hydroxypyruvate use of lithium beta-hydroxypyruvate as a donor renders the reaction irreversible Escherichia coli (3S)-1,3-dihydroxypentan-2-one + (3R)-1,3-dihydroxypentan-2-one + 2 CO2 + 2 Li+ wild-type, 58% enantiomeric excess for 3S-product r