Chemoenzymatic synthesis of glutamic acid analogues : Substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Organic Chemistry Année : 2007

Chemoenzymatic synthesis of glutamic acid analogues : Substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli.

Résumé

A new route to -keto acids is described, based on the ozonolysis of enol acetates obtained from -substituted -keto esters. Escherichia coli branched chain aminotransferase (BCAT) activity toward a variety of substituted 2-oxoglutaric acids was demonstrated analytically. BCAT was shown to have a broad substrate spectrum, complementary to that of aspartate aminotransferase, and to offer access to a variety of glutamic acid analogues. The usefulness of BCAT was demonstrated through the synthesis of several 3- and 4-substituted derivatives.
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Dates et versions

hal-00182848 , version 1 (29-10-2007)

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  • HAL Id : hal-00182848 , version 1

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Mo Xian, Sébastien Alaux, Emmanuelle Sagot, Thierry Gefflaut. Chemoenzymatic synthesis of glutamic acid analogues : Substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli.. Journal of Organic Chemistry, 2007, 72, pp.7560-7566. ⟨hal-00182848⟩
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