热己肽A和B是两种从海藻衍生的热链霉菌（Streptomyces thermomolineatus） NAK03196中获得的新六环肽

IF 1.5 4区化学 Q3 CHEMISTRY, ORGANIC

Tetrahedron Letters Pub Date : 2025-04-01 DOI:10.1016/j.tetlet.2025.155565

Guo Dong Zhang , Cheng Yuan Yuan , Ling Jiao Zou, Bo Zhang, Rui Hua Jiao

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引用次数: 0

摘要

本研究从海洋藻类相关细菌Streptomyces thermolineatus NAK03196发酵液中分离并鉴定了两个新的六环肽：热己素A(1)和B(2)。采用高分辨率电喷雾电离质谱法（HR-ESI-MS）、串联质谱法（MS/MS）、核磁共振（NMR）谱法和改进的Marfey法测定了它们的结构。基因组分析表明，tyrohexins是通过非核糖体肽合成酶（NRPS）途径生物合成的，并通过青霉素结合蛋白样硫酯酶介导大环化。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Thermohexins A and B, two new hexacyclicpeptides from marine algae-derived Streptomyces thermolineatus NAK03196

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Thermohexins A and B, two new hexacyclicpeptides from marine algae-derived Streptomyces thermolineatus NAK03196

This study describes the isolation and structural elucidation of two new hexacyclic peptides, thermohexins A (1) and B (2), from the fermentation broth of the marine algae-associated bacterium Streptomyces thermolineatus NAK03196. Their structures were determined using high-resolution electrospray ionization mass spectrometry (HR-ESI-MS), tandem mass spectrometry (MS/MS), nuclear magnetic resonance (NMR) spectroscopy, and the modified Marfey's method. Genomic analysis revealed that tyrohexins are biosynthesized via a nonribosomal peptide synthetase (NRPS) pathway and undergo macrocyclization mediated by a penicillin-binding protein-like thioesterase.

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来源期刊

Tetrahedron Letters 化学-有机化学

CiteScore

3.50

自引率

5.60%

发文量

521

审稿时长

28 days

期刊介绍： Tetrahedron Letters provides maximum dissemination of outstanding developments in organic chemistry. The journal is published weekly and covers developments in techniques, structures, methods and conclusions in experimental and theoretical organic chemistry. Rapid publication of timely and significant research results enables researchers from all over the world to transmit quickly their new contributions to large, international audiences.