On January 15, 2021, Kaniusaite, Milda; Tailhades, Julien; Kittilae, Tiia; Fage, Christopher D.; Goode, Robert J. A.; Schittenhelm, Ralf B.; Cryle, Max J. published an article.Synthetic Route of 32462-30-9 The title of the article was Understanding the early stages of peptide formation during the biosynthesis of teicoplanin and related glycopeptide antibiotics. And the article contained the following:
The biosynthesis of the glycopeptide antibiotics (GPAs) demonstrates the exceptional ability of nonribosomal peptide (NRP) synthesis to generate diverse and complex structures from an expanded array of amino acid precursors. While the heptapeptide cores of GPAs share a conserved C terminus, including the aromatic residues involved crosslinking and that are essential for the antibiotic activity of GPAs, most structural diversity is found within the N terminus of the peptide. Furthermore, the origin of the (D)-stereochem. of residue 1 of all GPAs is currently unclear, despite its importance for antibiotic activity. Given these important features, we have now reconstituted modules (M) 1-4 of the NRP synthetase (NRPS) assembly lines that synthesize the clin. relevant type IV GPA teicoplanin and the related compound A40926. Our results show that important roles in amino acid modification during the NRPS-mediated biosynthesis of GPAs can be ascribed to the actions of condensation domains present within these modules, including the incorporation of (D)-amino acids at position 1 of the peptide. Our results also indicate that hybrid NRPS assembly lines can be generated in a facile manner by mixing NRPS proteins from different systems and that uncoupling of peptide formation due to different rates of activity seen for NRPS modules can be controlled by varying the ratio of NRPS modules. Taken together, this indicates that NRPS assembly lines function as dynamic peptide assembly lines and not static megaenzyme complexes, which has significant implications for biosynthetic redesign of these important biosynthetic systems. The experimental process involved the reaction of H-Phg(4-OH)-OH(cas: 32462-30-9).Synthetic Route of 32462-30-9
The Article related to nonribosomal peptide synthetase teicoplanin biosynthesis stereochem glycopeptide antibiotic, biosynthesis, epimerisation, glycopeptide antibiotics, nonribosomal peptide synthetase, teicoplanin and other aspects.Synthetic Route of 32462-30-9
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