Literature summary for 2.2.1.1 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 .

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Protein Variants

Protein Variants	Comment	Organism
D469E	the mutant shows about 4.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
H100F	the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
H100L	the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
H100Y	the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
H192P/A282P/I365L/G506A	the mutant shows about wild type activity with propionaldehyde and pyruvate	Escherichia coli
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
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
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
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
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
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
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
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
H192P/A282P/I365L/G506A/H473N	the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
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
H473N	the mutant shows about 2.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
H473S	the mutant shows about 1.5fold increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli
L116I	the mutant shows slightly increased activity with propionaldehyde and pyruvate as compared to the wild type enzyme	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P27302	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 pyruvate	-	Escherichia coli	erythrulose	-	?
3-formylbenzoic acid + pyruvate	-	Escherichia coli	3-(2-oxopropanoyl)benzoate + CO2	-	?
3-formylbenzoic acid + pyruvate	-	Escherichia coli	3-(2-oxopropanoyl)benzoic acid + CO2	-	ir
glycolaldehyde + pyruvate	-	Escherichia coli	3,4-dihydroxy-2-butanone + CO2	-	?
hexanal + 2-oxoheptanoic acid	-	Escherichia coli	7-hydroxydodecan-6-one + CO2	-	?
hexanal + pyruvate	-	Escherichia coli	2-hydroxyheptanal + CO2	-	?
pentanal + 2-oxohexanoic acid	-	Escherichia coli	6-hydroxydecan-5-one + CO2	-	?
pentanal + pyruvate	-	Escherichia coli	2-hydroxyhexanal + CO2	-	?
propionaldehyde + 2-oxobutanoic acid	-	Escherichia coli	4-hydroxyhexan-3-one + CO2	-	?
propionaldehyde + pyruvate	-	Escherichia coli	2-hydroxybutanal + CO2	-	?

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Escherichia coli

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Release 2023.1 (January 2023)