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

Abstract

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.

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Acknowledgements

This work was supported by the Zhejiang Key Laboratory Construction Project and the National Natural Science Foundation of China General Program (22177092) to L.Z.

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Correspondence to Lihan Zhang.

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Zhang, Z., Zhang, L. Genome mining discovery of aquimarinols, threoninol-containing acylpeptides from Aquimarina muelleri. J Antibiot 79, 221–226 (2026). https://doi.org/10.1038/s41429-026-00894-3

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