α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.

ABSTRACT: N-Methylation of the peptide backbone confers pharmacologically beneficial characteristics to peptides that include greater membrane permeability and resistance to proteolytic degradation. The borosin family of ribosomally synthesized and post-translationally modified peptides offer a post-translational route to install amide backbone α-N-methylations. Previous work has elucidated the substrate scope and engineering potential of two examples of type I borosins, which feature autocatalytic precursors that encode N-methyltransferases that methylate their own C-termini in trans. We recently reported the first discrete N-methyltransferase and precursor peptide from Shewanella oneidensis MR-1, a minimally iterative, type IV borosin that allowed the first detailed kinetic analyses of borosin N-m

SUBMITTER: Crone KK 

PROVIDER: S-EPMC11751858 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature