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- W1978222017 abstract "To study the function of pantetheine in gramicidin S and tyrocidine biosynthesis, pepsin digests of the polymerizing enzymes, of which only the heavy ones contain pantetheine, were analyzed. The digests of gramicidin S enzymes charged with either [(14)C]proline or with D-phenylalanyl-[(14)C]proline, were analyzed by thin-layer chromatography; only the dipeptide showed a derivative associated with pantetheine. Similar results were obtained from the heavy tyrocidine enzyme charged with either [(14)C]asparagine alone or with the pentapeptide D-Phe-Pro-Phe-D-Phe-[(14)C]Asn. Several radioactive products appeared on the thin-layer chromatograms of both these digests; association with pantetheine was found only in the case of the pentapeptide. Exposure of the chromatogram from the pentapeptide-labeled digest to performic acid and development in a second direction separated the peptide from pantetheine, indicating that a nascent peptide was originally linked to the cofactor by a thioester bond. The connection of pantetheine only with peptide residues appears to confirm its role in transpeptidation during peptide chain growth." @default.
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- W1978222017 date "1971-09-01" @default.
- W1978222017 modified "2023-10-18" @default.
- W1978222017 title "Pantetheine-Linked Peptide Intermediates in Gramicidin S and Tyrocidine Biosynthesis" @default.
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- W1978222017 doi "https://doi.org/10.1073/pnas.68.9.2069" @default.
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