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Literature summary 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

Application

EC Number Application Comment Organism
2.2.1.1 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

EC Number Organism UniProt Comment Textmining
2.2.1.1 Saccharomyces cerevisiae
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.1 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
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pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.2.1.1 7.2 8.2
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 Saccharomyces cerevisiae