Design of an enantioselective artificial metallo-hydratase enzyme containing an unnatural metal-binding amino acid.

ABSTRACT: The design of artificial metalloenzymes is a challenging, yet ultimately highly rewarding objective because of the potential for accessing new-to-nature reactions. One of the main challenges is identifying catalytically active substrate-metal cofactor-host geometries. The advent of expanded genetic code methods for the in vivo incorporation of non-canonical metal-binding amino acids into proteins allow to address an important aspect of this challenge: the creation of a stable, well-defined metal-binding site. Here, we report a designed artificial metallohydratase, based on the transcriptional repressor lactococcal multidrug resistance regulator (LmrR), in which the non-canonical amino acid (2,2'-bipyridin-5yl)alanine is used to bind the catalytic Cu(ii) ion. Starting from a set of e

SUBMITTER: Drienovska I 

PROVIDER: S-EPMC5633786 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature