Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.

ABSTRACT: Enzymes that can catalyze the macrocyclization of linear peptide substrates have long been sought for the production of libraries of structurally diverse scaffolds via combinatorial gene assembly as well as to afford rapid in vivo screening methods. Orbitides are plant ribosomally synthesized and posttranslationally modified peptides (RiPPs) of various sizes and topologies, several of which are shown to be biologically active. The diversity in size and sequence of orbitides suggests that the corresponding macrocyclases may be ideal catalysts for production of cyclic peptides. Here we present the biochemical characterization and crystal structures of the plant enzyme PCY1 involved in orbitide macrocyclization. These studies demonstrate how the PCY1 S9A protease fold has been adapted for tra

SUBMITTER: Chekan JR 

PROVIDER: S-EPMC5488928 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature