6rx8 | pdb_00006rx8
EDDS lyase variant D290M/Y320M with bound fumarate
Structural highlights
FunctionPublication Abstract from PubMedAspartic acid derivatives with branched N -alkyl or N -arylalkyl substituents are valuable precursors to artificial dipeptide sweeteners such as neotame and advantame, which have wide-ranging applications in the food industry. Despite the potential applications of these amino acid precursors to aspartame-based sweeteners, the development of a biocatalyst to synthesize these compounds in a single asymmetric step is an as yet unmet challenge. Herein we report an enantioselective biocatalytic synthesis of various difficult N -substituted aspartic acids including N -(3,3-dimethylbutyl)-L-aspartic acid and N -[3-(3-hydroxy-4-methoxyphenyl)propyl]-L-aspartic acid, precursors to neotame and advantame respectively, using an engineered variant of ethylenediamine- N , N '-disuccinic acid (EDDS) lyase from Chelativorans sp. BNC1. This engineered C-N lyase (mutant D290M/Y320M) displayed a remarkable 1140-fold increase in activity for the selective hydroamination of fumarate compared to that of the wild-type enzyme, which could be rationalized from the analysis of crystal structures. These results open up new opportunities to develop practical multienzymatic processes for the more sustainable and step-economic synthesis of an important class of food additives. Enantioselective Synthesis of Chiral Synthons for Artificial Dipeptide Sweeteners Catalyzed by an Engineered C-N Lyase.,Zhang J, Grandi E, Fu H, Saravanan T, Bothof L, Tepper PG, Thunnissen AWH, Poelarends GJ Angew Chem Int Ed Engl. 2019 Oct 18. doi: 10.1002/anie.201910704. PMID:31625664[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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