title: Multistep enzyme catalyzed reactions for unnatural amino acids.
abstract: The use of unnatural amino acids, particularly synthetic α-amino acids, for modern drug discovery research requires the availability of enantiomerically pure isomers. Starting from a racemate, one single enantiomer can be obtained using a deracemization process. The two more common strategies of deracemization are those obtained by stereoinversion and by dynamic kinetic resolution. Both techniques will be here described using as a substrate the D,L-3-(2-naphthyl)-alanine, a non-natural amino acid: the first one employing a multi-enzymatic redox system, the second one combining an hydrolytic enzyme together with a base-catalyzed substrate racemization. In both cases, the final product, L-3-(2-naphthyl)alanine, is recovered with good yield and excellent enantiomeric excess.
authors.affiliation: Dipartimento di Chimica, Materiali ed Ingegneria Chimica Giulio Natta Politecnico di Milano, The Protein Factory, Politecnico di Milano and Università degli Studi dell'Insubria, Milano, Italy. davide.tessaro@polimi.it
authors.forename: Paola
authors.initials: P
authors.lastname: D'Arrigo
authors.forename: Davide
authors.initials: D
authors.lastname: Tessaro
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy
chemical_list: D000596:Amino Acids; D004798:Enzymes