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

J. Org. Chem.2007 Sep 28;72(20):7560-6. doi:10.1021/jo070805q. Epub 2007 Aug 24

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A new route to alpha-keto acids is described, based on the ozonolysis of enol acetates obtained from alpha-substituted beta-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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Chemoenzymatic synthesis of glutamic acid analogues: substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli.

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