151139-88-7Relevant articles and documents
Chemoenzymatic synthesis of glutamic acid analogues: Substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli
Xian, Mo,Alaux, Sebastien,Sagot, Emmanuelle,Gefflaut, Thierry
, p. 7560 - 7566 (2008/03/11)
(Chemical Equation Presented) A new route to α-keto acids is described, based on the ozonolysis of enol acetates obtained from α-substituted β-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.
Synthesis of 4,4-Disubstituted L-Glutamic Acids by Enzymatic Transamination
Helaine, Virgil,Rossi, Joel,Gefflaut, Thierry,Alaux, Sebastien,Bolte, Jean
, p. 692 - 697 (2007/10/03)
The syntheses of optically pure 4,4-dimethyl-L-glutamic acid as well as (2S,4R)- and (2S,4S)-4-hydroxy-4-methylglutamic acids have been achieved by transamination of the corresponding 2-oxo-4,4-dimethyl- and rac-2-oxo-4-hydroxy-4-methylglutaric acids using glutamic oxalacetic transaminase (GOT).