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• W1964812851 startingPage "78" @default.
• W1964812851 abstract "The structural and catalytic similarities between modular nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) inspired us to search for hybrid NRPS-PKS systems. By examining the biochemical and genetic data known to date for the biosynthesis of hybrid peptide-polyketide natural products, we show (1) that the same catalytic sites are conserved between the hybrid NRPS-PKS and normal NRPS or PKS systems, although the ketoacyl synthase domain in NRPS/PKS hybrids is unique, and (2) that specific interpolypeptide linkers exist at both the C- and N-termini of the NRPS and PKS proteins, which presumably play a critical role in facilitating the transfer of the growing peptide or polyketide intermediate between NRPS and PKS modules in hybrid NRPS-PKS systems. These findings provide new insights for intermodular communications in hybrid NRPS-PKS systems and should now be taken into consideration in engineering hybrid peptide-polyketide biosynthetic pathways for making novel unnatural natural products." @default.
• W1964812851 created "2016-06-24" @default.
• W1964812851 creator A5084055011 @default.
• W1964812851 creator A5087514362 @default.
• W1964812851 creator A5088207322 @default.
• W1964812851 date "2001-01-01" @default.
• W1964812851 modified "2023-10-14" @default.
• W1964812851 title "Hybrid Peptide–Polyketide Natural Products: Biosynthesis and Prospects toward Engineering Novel Molecules" @default.
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• W1964812851 doi "https://doi.org/10.1006/mben.2000.0171" @default.
• W1964812851 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11162234" @default.
• W1964812851 hasPublicationYear "2001" @default.
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