Chemoenzymatic synthesis of glutamic acid analogues: substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli.
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.
Xian
Mo
M
UMR 6504, Université Blaise Pascal, F-63177 Aubière Cedex, France.
Alaux
Sébastien
S
Sagot
Emmanuelle
E
Gefflaut
Thierry
T
D004926:Escherichia coli / Q000201:enzymology*; D018698:Glutamic Acid / Q000031:analogs & derivatives* / Q000138:chemical synthesis; D007656:Ketoglutaric Acids / Q000138:chemical synthesis*; D007700:Kinetics; D013379:Substrate Specificity; D000637:Transaminases / Q000737:chemistry* / Q000378:metabolism
D007656:Ketoglutaric Acids; D018698:Glutamic Acid; D000637:Transaminases; C019798:branched-chain-amino-acid transaminase