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Enzymatic Synthesis of a Polyketide/Nonribosomal Peptide Hybrid Antibiotic, Salivabactin

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Biochemistry 2024, 63, 24, 3213-3219
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    Enzymatic Synthesis of a Polyketide/Nonribosomal Peptide Hybrid Antibiotic, Salivabactin
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    • Di Gu
      Di Gu
      Department of Chemistry, University of California, Berkeley, California 94720, United States
      More by Di Gu
      Orcidhttps://orcid.org/0000-0003-4860-7701
    • Rui Zhai
      Rui Zhai
      Department of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, United States
      More by Rui Zhai
      Orcidhttps://orcid.org/0000-0001-5032-9689
    • Bailey Daymo
      Bailey Daymo
      Department of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, United States
      More by Bailey Daymo
    • Yuxin Xie
      Yuxin Xie
      Department of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, United States
      More by Yuxin Xie
    • Caroline Luo
      Caroline Luo
      Department of Chemistry, University of California, Berkeley, California 94720, United States
      More by Caroline Luo
    • Wenjun Zhang*
      Wenjun Zhang
      Department of Chemical and Biomolecular Engineering, University of California, Berkeley, California 94720, United States
      *Email: [email protected]
      More by Wenjun Zhang
      Orcidhttps://orcid.org/0000-0001-9348-972X
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    Biochemistry

    Cite this: Biochemistry 2024, 63, 24, 3213–3219
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    https://doi.org/10.1021/acs.biochem.4c00515
    Published December 4, 2024
    Copyright © 2024 American Chemical Society
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    Abstract

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    Salivabactin is a newly identified polyketide/nonribosomal peptide (PK/NRP) from a human oral probiotic, possessing a unique chemical structure and outstanding antibiotic activities. Although the biosynthetic gene cluster for salivabactin is known, the enzymatic logic that governs the synthesis of salivabactin has not yet been fully studied. In this work, we dissected the biosynthetic pathway for salivabactin using biochemical analysis. We successfully reconstituted the enzymatic synthesis of salivabactin in vitro, identified the minimal set of enzymes required for its biosynthesis, and revealed an unusual thioesterase domain involved in terminal olefin formation.

    Copyright © 2024 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.biochem.4c00515.

    • Oligonucleotides, plasmids, and bacterial strains used in this study; SDS-PAGE gels; protein sequence alignment; and supplementary LC-HRMS data (PDF)

    Accession Codes

    SarD: WP_002892325.1 (NCBI), J7T4A6 (Uniprot); SarE: WP_002892326.1 (NCBI), J7TEX7 (Uniprot); SarF: WP_002892327.1 (NCBI), J7SHL7 (Uniprot); SarG: WP_050989617.1 (NCBI); SarH: WP_002892331.1 (NCBI), J7TMG5 (Uniprot); SarJ: WP_002892335.1 (NCBI), J7TEY0 (Uniprot); DEBS_TE: Q03133 (Uniprot); 1KEZ (PDB).

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    Biochemistry

    Cite this: Biochemistry 2024, 63, 24, 3213–3219
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.biochem.4c00515
    Published December 4, 2024
    Copyright © 2024 American Chemical Society
    Request reuse permissions

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