Literature summary for 2.2.1.1 extracted from

Subrizi, F.; Cardenas-Fernandez, M.; Lye, G.; Ward, J.; Dalby, P.; Sheppard, T.; Hailes, H.
Transketolase catalysed upgrading of L-arabinose The one-step stereoselective synthesis of L-gluco-heptulose (2016), Green Chem., 18, 3158-3165 .

No PubMed abstract available

Search for more literature for 2.2.1.1

Protein Variants

Protein Variants	Comment	Organism
H461Y	the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme	Escherichia coli
R358I	the mutant shows about 1.2fold increased activity with L-arabinose compared to the wild type enzyme	Escherichia coli
R358P	the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme	Escherichia coli
R358S	the mutant shows about 1.4fold increased activity with L-arabinose compared to the wild type enzyme	Escherichia coli
R520P	the mutant shows about 1.5fold increased activity with L-arabinose compared to the wild type enzyme	Escherichia coli
R520Y	the mutant shows about 2fold increased activity with L-arabinose compared to the wild type enzyme	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	6 mM used in assay conditions	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	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arabinose + lithium beta-hydroxypyruvate	48% conversion after 24 h	Escherichia coli	L-gluco-heptulose + CO2 + Li+	-	?
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	Escherichia coli	D-ribose 5-phosphate + D-xylulose 5-phosphate	-	r

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Escherichia coli

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Release 2023.1 (January 2023)