Characterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics.

ABSTRACT: The peptide natural product nisin has been used as a food preservative for 6 decades with minimal development of resistance. Nisin contains the unusual amino acids dehydroalanine and dehydrobutyrine, which are posttranslationally installed by class I lanthipeptide dehydratases (LanBs) on a linear peptide substrate through an unusual glutamyl-tRNA-dependent dehydration of Ser and Thr. To date, little is known about how LanBs catalyze the transfer of glutamate from charged tRNA^Glu to the peptide substrate, or how they carry out the subsequent elimination of the peptide-glutamyl adducts to afford dehydro amino acids. Here, we describe the synthesis of inert analogs that mimic substrate glutamyl-tRNA^Glu and the glutamylated peptide intermediate, and determine the crystal

SUBMITTER: Bothwell IR 

PROVIDER: S-EPMC6717260 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature