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<p>Thioester reductase domain in nonribosomal peptide synthetases catalyzes reductive offloading to produce aldehyde- or alcohol-containing peptides. By genome mining focusing on thioester reductase domains, we isolated aquimarinols A-D, four novel polyketide-peptide hybrid metabolites isolated from the sponge-derived strain <i>Aquimarina muelleri</i> LMG 22569. Structural elucidation of aquimarinols revealed a β-formamidated fatty acid (FA) moiety and a threoninol unit linked by a peptide bond or an ester bond. The biosynthesis of aquimarinols is proposed to proceed via a hybrid <i>trans</i>-AT polyketide synthase-nonribosomal peptide synthetase pathway coupled with modification enzymes.</p>

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Genome mining discovery of aquimarinols, threoninol-containing acylpeptides from Aquimarina muelleri

  • 期刊论文

  • 发表日期：

    2026年1月22日

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  • Zhihan Zhang,
  • Lihan Zhang

摘要

Thioester reductase domain in nonribosomal peptide synthetases catalyzes reductive offloading to produce aldehyde- or alcohol-containing peptides. By genome mining focusing on thioester reductase domains, we isolated aquimarinols A-D, four novel polyketide-peptide hybrid metabolites isolated from the sponge-derived strain Aquimarina muelleri LMG 22569. Structural elucidation of aquimarinols revealed a β-formamidated fatty acid (FA) moiety and a threoninol unit linked by a peptide bond or an ester bond. The biosynthesis of aquimarinols is proposed to proceed via a hybrid trans-AT polyketide synthase-nonribosomal peptide synthetase pathway coupled with modification enzymes.