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Literature summary extracted from

  • Yu, H.; Hernandez Lopez, R.I.; Steadman, D.; Mendez-Sanchez, D.; Higson, S.; Cazares-Koerner, A.; Sheppard, T.D.; Ward, J.M.; Hailes, H.C.; Dalby, P.A.
    Engineering transketolase to accept both unnatural donor and acceptor substrates and produce alpha-hydroxyketones (2020), FEBS J., 287, 1758-1776 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.1 D469E the mutant shows about 4.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H100F the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H100L the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H100Y the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A the mutant shows about wild type activity with propionaldehyde and pyruvate Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/D469E the mutant shows about 6.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/D469E/H473S the mutant shows about 2fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H100L the mutant shows about 2fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H100L/D469E the mutant shows about 8fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H100L/D469E/R520Q the mutant shows about 9fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H100L/D469T the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H100L/H473N the mutant shows about 4fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H100L/H473S the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H473N the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H192P/A282P/I365L/G506A/H473S the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H473N the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 H473S the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli
2.2.1.1 L116I the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.1 Mg2+ required 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 2 pyruvate
-
 Escherichia coli erythrulose
-
 ?
2.2.1.1 3-formylbenzoic acid + pyruvate
-
 Escherichia coli 3-(2-oxopropanoyl)benzoate + CO2
-
 ?
2.2.1.1 3-formylbenzoic acid + pyruvate
-
 Escherichia coli 3-(2-oxopropanoyl)benzoic acid + CO2
-
 ir
2.2.1.1 glycolaldehyde + pyruvate
-
 Escherichia coli 3,4-dihydroxy-2-butanone + CO2
-
 ?
2.2.1.1 hexanal + 2-oxoheptanoic acid
-
 Escherichia coli 7-hydroxydodecan-6-one + CO2
-
 ?
2.2.1.1 hexanal + pyruvate
-
 Escherichia coli 2-hydroxyheptanal + CO2
-
 ?
2.2.1.1 pentanal + 2-oxohexanoic acid
-
 Escherichia coli 6-hydroxydecan-5-one + CO2
-
 ?
2.2.1.1 pentanal + pyruvate
-
 Escherichia coli 2-hydroxyhexanal + CO2
-
 ?
2.2.1.1 propionaldehyde + 2-oxobutanoic acid
-
 Escherichia coli 4-hydroxyhexan-3-one + CO2
-
 ?
2.2.1.1 propionaldehyde + pyruvate
-
 Escherichia coli 2-hydroxybutanal + CO2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.1 thiamine diphosphate
-
 Escherichia coli