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NosN, a Radical S-Adenosylmethionine Methylase, Catalyzes Both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide.

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Affiliations

  • 1. Departments of Chemistry and ‡Biochemistry and Molecular Biology, and the §Howard Hughes Medical Institute, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.
      Authors
    • LaMattina JW 1
    • Wang B 1
    • Badding ED 1
    • Gadsby LK 1
    • Grove TL 1
    • Booker SJ 1
    (6 authors)

ORCIDs linked to this article

Journal of the American Chemical Society, 21 Nov 2017, 139(48):17438-17445
https://doi.org/10.1021/jacs.7b08492 PMID: 29039940 PMCID: PMC5938625

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Abstract 

Nosiheptide, a member of the e series of macrocyclic thiopeptide natural products, contains a side-ring system composed of a 3,4-dimethylindolic acid (DMIA) moiety connected to Glu6 and Cys8 of the thiopeptide backbone via ester and thioester linkages, respectively. Herein, we show that NosN, a predicted class C radical S-adenosylmethionine (SAM) methylase, catalyzes both the transfer of a C1 unit from SAM to 3-methylindolic acid linked to Cys8 of a synthetic substrate surrogate as well as the formation of the ester linkage between Glu6 and the nascent C4 methylene moiety of DMIA. In contrast to previous studies that indicated that 5'-methylthioadenosine is the immediate methyl donor in the reaction, in our studies, SAM itself plays this role, giving rise to S-adenosylhomocysteine as a coproduct of the reaction.

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Funding 

Funders who supported this work.

NIAID NIH HHS (2)

NIGMS NIH HHS (1)

National Institute of Allergy and Infectious Diseases (2)

National Institute of General Medical Sciences (1)