Biocatalytic reductive amination as a route to isotopically labelled amino acids suitable for analysis of large proteins by NMR.

ABSTRACT: We demonstrate an atom-efficient and easy to use H₂-driven biocatalytic platform for the enantioselective incorporation of ²H-atoms into amino acids. By combining the biocatalytic deuteration catalyst with amino acid dehydrogenase enzymes capable of reductive amination, we synthesised a library of multiply isotopically labelled amino acids from low-cost isotopic precursors, such as ²H₂O and ¹⁵NH₄⁺. The chosen approach avoids the use of pre-labeled ²H-reducing agents, and therefore vastly simplifies product cleanup. Notably, this strategy enables ²H, ¹⁵N, and an asymmetric centre to be introduced at a molecular site in a single step, with full selectivity, under benign conditions, a

SUBMITTER: Rowbotham JS 

PROVIDER: S-EPMC10631221 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature