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- W2103254492 abstract "This study demonstrates a critical role for N-methylation in cyclosporin biosynthesis and maintenance of the biologically active cyclosporin conformation. The structural requirements for the AdoMet binding to CySyn were defined. N-methylation of specific amide positions in the cyclosporin backbone is critical for the complete assembly and cyclization of the cyclosporin peptide. A maximum of two desmethyl positions is tolerated before peptide assembly stalls. Subinhibitory concentrations of AdoMet analogs directed peptide assembly towards cyclosporins with less than seven N-methylated amide bonds. Molecular modeling and nuclear magnetic resonance analyses indicate that N-methylation of specific amide bond positions in the cyclosporin backbone is mandatory for the formation of a product-like conformation and recognition by the acceptor site of the downstream peptide bond forming C-domain." @default.
- W2103254492 created "2016-06-24" @default.
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- W2103254492 date "2011-04-01" @default.
- W2103254492 modified "2023-10-16" @default.
- W2103254492 title "Characterization of the N-Methyltransferase Activities of the Multifunctional Polypeptide Cyclosporin Synthetase" @default.
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- W2103254492 doi "https://doi.org/10.1016/j.chembiol.2011.01.017" @default.
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