期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 18, 页码 4652-4656出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201311061
关键词
hydroamination; amino acids; enzymes; isotopic labeling; reaction mechanisms
资金
- Centre of Excellence in Biocatalysis, Biotransformation and Biocatalytic Manufacture (CoEBio3)
- Royal Society
- Biotechnology and Biological Sciences Research Council [BB/K00199X/1] Funding Source: researchfish
- BBSRC [BB/K00199X/1] Funding Source: UKRI
Phenylalanine ammonia lyases (PALs) belong to a family of 4-methylideneimidazole-5-one (MIO) cofactor dependent enzymes which are responsible for the conversion of L-phenylalanine into trans-cinnamic acid in eukaryotic and prokaryotic organisms. Under conditions of high ammonia concentration, this deamination reaction is reversible and hence there is considerable interest in the development of PALs as biocatalysts for the enantioselective synthesis of non-natural amino acids. Herein the discovery of a previously unobserved competing MIO-independent reaction pathway, which proceeds in a non-stereoselective manner and results in the generation of both L- and D-phenylalanine derivatives, is described. The mechanism of the MIO-independent pathway is explored through isotopic-labeling studies and mutagenesis of key active-site residues. The results obtained are consistent with amino acid deamination occurring by a stepwise E(1)cB elimination mechanism.
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