A proof-reading mechanism for non-proteinogenic amino acid incorporation into glycopeptide antibiotics.

ABSTRACT: Non-ribosomal peptide biosynthesis produces highly diverse natural products through a complex cascade of enzymatic reactions that together function with high selectivity to produce bioactive peptides. The modification of non-ribosomal peptide synthetase (NRPS)-bound amino acids can introduce significant structural diversity into these peptides and has exciting potential for biosynthetic redesign. However, the control mechanisms ensuring selective modification of specific residues during NRPS biosynthesis have previously been unclear. Here, we have characterised the incorporation of the non-proteinogenic amino acid 3-chloro-β-hydroxytyrosine during glycopeptide antibiotic (GPA) biosynthesis. Our results demonstrate that the modification of this residue by trans-acting enzymes is cont

SUBMITTER: Kaniusaite M 

PROVIDER: S-EPMC6993612 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature