title: Preparation of glutamate analogues by enzymatic transamination.
abstract: Aminotransferases are key enzymes of the metabolism of proteinogenic amino acids. These ubiquitous biocatalysts show high specific activities and relaxed substrate specificities making them valuable tools for the stereoselective synthesis of unnatural amino acids. We describe here the application of aspartate aminotransferase and branched chain aminotransferase from E. coli for the synthesis of various glutamate analogues, molecules of particular interest regarding the neuroactive properties of glutamic acid.
authors.affiliation: Lab SEESIB, Clermont Université, Université Blaise Pascal - CNRS, Aubière, France. Thierry.gefflaut@univ-bpclermont.fr
authors.forename: Thierry
authors.initials: T
authors.lastname: Gefflaut
authors.forename: Zeinab
authors.initials: Z
authors.lastname: Assaf
authors.forename: Martine
authors.initials: M
authors.lastname: Sancelme
mesh_terms: D000586:Amination; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D018698:Glutamic Acid / Q000378:metabolism*; D000637:Transaminases / Q000378:metabolism*
chemical_list: D018698:Glutamic Acid; D000637:Transaminases; D001219:Aspartate Aminotransferases; C019798:branched-chain-amino-acid transaminase