Literature summary for 2.2.1.1 extracted from

Affaticati, P.E.; Dai, S.B.; Payongsri, P.; Hailes, H.C.; Tittmann, K.; Dalby, P.A.
Structural analysis of an evolved transketolase reveals divergent binding modes (2016), Sci. Rep., 6, 35716 .

Search for more literature for 2.2.1.1

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutant S385Y/D469T/R520Q, hanging drop vapor diffusion method, using 17-22% (w/v) PEG 6000, 2% (v/v) glycerol, 50 mM glycyl-glycine buffer, pH 7.9	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D469T	the mutant shows activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to the wild type enzyme	Escherichia coli
D469T/R520Q	the mutant shows improved activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to mutant enzyme D469T	Escherichia coli
S385Y/D469T/R520Q	the mutant shows improved activities towards the three benzaldehyde analogues, 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde compared to mutant enzyme D469T/R520Q	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	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P27302	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the wild type enzyme shows no activity with 3-formylbenzoic acid, 4-formylbenzoic acid and 3-hydroxybenzaldehyde	Escherichia coli	?	-	-
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	Escherichia coli	D-ribose 5-phosphate + D-xylulose 5-phosphate	-	?

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	-	Escherichia coli

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Release 2023.1 (January 2023)