Biocatalytic Enantioselective Hydroaminations Enabling Synthesis of N-Arylalkyl-Substituted L-Aspartic Acids
- Resource Type
- Authors
- Thangavelu Saravanan; Andy-Mark W. H. Thunnissen; Laura Bothof; Pieter G. Tepper; Mohammad Zainal Abidin; Gerrit J. Poelarends
- Source
- Organic & Biomolecular Chemistry, 19(29). ROYAL SOC CHEMISTRY
Organic & Biomolecular Chemistry
- Subject
- chemistry.chemical_classification
Aspartic Acid
010405 organic chemistry
Chemistry
Organic Chemistry
Enantioselective synthesis
Substrate (chemistry)
010402 general chemistry
Lyase
01 natural sciences
Biochemistry
0104 chemical sciences
Amino acid
chemistry.chemical_compound
EDDS
Biocatalysis
Yield (chemistry)
Organic chemistry
Amine gas treating
Physical and Theoretical Chemistry
- Language
- English
- ISSN
- 1477-0520
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.
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.