期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 1, 页码 429-435出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201910704
关键词
enzymes; biocatalysis; hydroamination; protein engineering; synthetic methods
资金
- Netherlands Organization of Scientific Research (VICI grant) [724.016.002]
- European Research Council (PoC grant) [713483]
- China Scholarship Council
- European Research Council (ERC) [713483] Funding Source: European Research Council (ERC)
Aspartic acid derivatives with branched N-alkyl or N-arylalkyl substituents are valuable precursors to artificial dipeptide sweeteners such as neotame and advantame. The development of a biocatalyst to synthesize these compounds in a single asymmetric step is an as yet unmet challenge. Reported here is 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. These results present new opportunities to develop practical multienzymatic processes for the more sustainable and step-economic synthesis of an important class of food additives.
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