title: Bacterial Anabaena variabilis phenylalanine ammonia lyase: a biocatalyst with broad substrate specificity.
abstract: Phenylalanine ammonia lyases (PALs) catalyse the regio- and stereoselective hydroamination of cinnamic acid analogues to yield optically enriched α-amino acids. Herein, we demonstrate that a bacterial PAL from Anabaena variabilis (AvPAL) displays significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. Biotransformations performed on a preparative scale led to the synthesis of the 2-chloro- and 4-trifluoromethyl-phenylalanine derivatives in excellent ee, highlighting the enormous potential of bacterial PALs as biocatalysts for the synthesis of high value, non-natural amino acids.
authors.affiliation: School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
authors.forename: Sarah L
authors.initials: SL
authors.lastname: Lovelock
authors.affiliation: School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK. Electronic address: nicholas.turner@manchester.ac.uk.
authors.forename: Nicholas J
authors.initials: NJ
authors.lastname: Turner
mesh_terms: D046870:Anabaena variabilis / Q000201:enzymology*; D055162:Biocatalysis; D007700:Kinetics; D008958:Models, Molecular; D010650:Phenylalanine Ammonia-Lyase / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D010650:Phenylalanine Ammonia-Lyase
keywords: Bacterial; Biocatalysis; Hydroamination; Kinetics; Phenylalanine ammonia lyase