ゲノムマイニングにより、Aquimarina muelleri由来のスレオニノール含有アシルペプチドであるアクアマリノールが発見された
Zhihan Zhang1, Lihan Zhang2,3
1Zhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Science, Westlake University, 600 Dunyu Rd., Hangzhou, 310030, Zhejiang Province, China.
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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