title: Blurring the lines between ribosomal and nonribosomal peptide scaffolds.
abstract: Two of the canons of protein science have been (1) that there are 20-22 amino acids that are proteinogenic and (2), with the exception of achiral glycine, that the other residues are L-amino acids. By contrast, the presence of nonproteinogenic amino acid residues and D-enantiomers has been regarded as hallmarks of nonribosomal peptides. The recent discoveries that bottromycins and polytheonamides, containing β-methyl and D-amino acid residues, are of ribosomal origin blur the distinctions between peptide structures derivable by ribosomal and nonribosomal assembly lines and reveal new chemistry for posttranslational maturation of proteins.
authors.affiliation: Department of Biological Chemistry & Molecular Pharmacology Harvard Medical School, Boston, Massachusetts 02115, United States.
authors.forename: Christopher T
authors.initials: CT
authors.lastname: Walsh
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D008745:Methylation; D010455:Peptides / Q000737:chemistry*; D012269:Ribosomal Proteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D010455:Peptides; D012269:Ribosomal Proteins