| Literature DB >> 25037641 |
Sarah L Lovelock1, Nicholas J Turner2.
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.Entities:
Keywords: Bacterial; Biocatalysis; Hydroamination; Kinetics; Phenylalanine ammonia lyase
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Year: 2014 PMID: 25037641 DOI: 10.1016/j.bmc.2014.06.035
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641