Literature summary extracted from

Gyamerah, M.; Willetts, A.J.
Kinetics of overexpressed transketolase from Escherichia coli JM 107/pQR 700 (1997), Enzyme Microb. Technol., 20, 127-134.

No PubMed abstract available

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.2.1.1	overexpression in Escherichia coli	Escherichia coli

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.2.1.1	L-erythrulose	competitive inhibition	Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.2.1.1	D-xylulose 5-phosphate + D-ribose 5-phosphate	Escherichia coli	ping pong bi bi mechanism	sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.2.1.1	Escherichia coli	-	JM 107/pQR 700	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.2.1.1	D-xylulose 5-phosphate + D-ribose 5-phosphate	-	Escherichia coli	sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	r
2.2.1.1	D-xylulose 5-phosphate + D-ribose 5-phosphate	ping pong bi bi mechanism	Escherichia coli	sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate	-	?

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Release 2023.1 (January 2023)