An enzymatic platform for the asymmetric amination of primary, secondary and tertiary C(sp³)-H bonds.

ABSTRACT: The ability to selectively functionalize ubiquitous C-H bonds streamlines the construction of complex molecular architectures from easily available precursors. Here we report enzyme catalysts derived from a cytochrome P450 that use a nitrene transfer mechanism for the enantioselective amination of primary, secondary and tertiary C(sp³)-H bonds. These fully genetically encoded enzymes are produced and function in bacteria, where they can be optimized by directed evolution for a broad spectrum of enantioselective C(sp³)-H amination reactions. These catalysts can aminate a variety of benzylic, allylic and aliphatic C-H bonds in excellent enantioselectivity with access to either antipode of product. Enantioselective amination of primary C(sp³)-H bonds in substr

SUBMITTER: Yang Y 

PROVIDER: S-EPMC6998391 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature