Biocatalytic enantioselective hydroaminations enabling synthesis of N-arylalkyl-substituted l-aspartic acids. Issue 29 (8th July 2021)

• Record Type: Journal Article
• Authors: Abidin, Mohammad Z.; Saravanan, Thangavelu; Bothof, Laura; Tepper, Pieter G.; Thunnissen, Andy-Mark W. H.; Poelarends, Gerrit J.
• Is Part Of: Organic & biomolecular chemistry. Volume 19:Issue 29(2021)
• Page Start: 6407
• Page End: 6411
• Publication Date: 2021-07-08
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/d1ob00748c
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : EDDS lyase has a broad substrate scope, accepting diverse arylalkylamines in the enantioselective hydroamination of fumarate enabling the facile synthesis of difficult N -arylalkyl-substituted l -aspartic acids with excellent optical purity. Abstract : N -Substituted l -aspartic acids are important chiral building blocks for pharmaceuticals and food additives. Here we report the asymmetric synthesis of various N -arylalkyl-substituted l -aspartic acids using ethylenediamine- N, N ′-disuccinic acid lyase (EDDS lyase) as a biocatalyst. This C–N lyase shows a broad non–natural amine substrate scope and outstanding enantioselectivity, allowing the efficient addition of structurally diverse arylalkylamines to fumarate to afford the corresponding N -arylalkyl-substituted l -aspartic acids in good isolated yield (up to 79%) and with excellent enantiopurity (>99% ee). These results further demonstrate that C–N lyases working in reverse constitute an extremely powerful synthetic tool to prepare difficult noncanonical amino acids.