Literature summary for 2.2.1.1 extracted from

Charmantray, F.; Helaine, V.; Lasikova, A.; Legeret, B.; Hecquet, L.
Chemoenzymatic synthesis of L-tyrosine derivative for a transketolase assay (2008), Tetrahedron Lett., 49, 3229-3233.

No PubMed abstract available

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Application

Application	Comment	Organism
biotechnology	substrate specificity of transketolase for the donor substrate is broader than expected. Possibility of detecting wild-type transketolase activity in vitro from a L-tyrosine derivative bearing a D-threo ketose, based on the release of L-tyrosine. For cells both auxotrophic for L-tyrosine and expressing transketolase, it shall be possible to carry out this assay in vivo. This strategy may offer the first stereospecific selection test for transketolase mutants	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester + D-ribose 5-phosphate	transketolase catalyzes the hydroxyacetyl group transfer from the donor substrate N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester to D-ribose-5-phosphate, the natural acceptor substrate of transketolase. Transketolase catalyzes C2-C3 bond cleavage from N-acetyl-O'-(2R,3S,5-trihydroxy-4-oxopentyl)-L-tyrosine ethyl ester	Saccharomyces cerevisiae	N-acetyl-O-[(2R)-2-hydroxy-3-oxopropyl]-L-tyrosine + D-sedoheptulose 7-phosphate	-	?

pH Range

pH Minimum	pH Maximum	Comment	Organism
7.2	8.2	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)