Identification of Holrhizins E-Q Reveals the Diversity of Nonribosomal Lipopeptides in Paraburkholderia rhizoxinica
Identification of Holrhizins E-Q Reveals the Diversity of Nonribosomal Lipopeptides in Paraburkholderia rhizoxinica
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Holrhizins E-Q 的鉴定揭示了 Paraburkholderia rhizoxinica 中非核糖体脂肽的多样性。
DOI：
10.1021/acs.jnatprod.9b00927
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发表时间：
2020-02-01
影响因子：
5.1
通讯作者：
Bian, Xiaoying
中科院分区：
文献类型：
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作者：
Chen, Hanna;Zhou, Haibo;Bian, Xiaoying
利用我们最近建立的重组工程技术，从副伯克霍尔德氏菌rhizoxinica的非核糖体肽合成酶基因，holA的产品进行了研究。在激活的突变体中检测到15种产物，包括13种新的线性脂肽，holrhizins E-Q（2 - 8，10 - 15），以及两种已知的holrhizins A和B（1，9），并使用HRESIMS，NMR光谱，Marvis分析和标记氨基酸的喂养实验鉴定了它们的结构。脂六肽1 - 3和7 - 14的不同之处在于三个氨基酸残基和N-末端脂肪酸链。holrhizins的多样性来源于A（4）、A（5）和A（6）结构域以及生物合成途径中的起始C结构域的底物灵活性。
The products of a nonribosomal peptide synthetase gene, holA, from Paraburkholderia rhizoxinica were investigated using our recently established recombineering technique. Fifteen products, including 13 new linear lipopeptides, holrhizins E-Q (2-8, 10-15), together with the two known holrhizins A and B (1, 9), were detected in the activated mutant, and their structures were identified using HRESIMS, NMR spectroscopy, Marfey's analysis, and feeding experiments with labeled amino acids. The lipohexapeptides 1-3 and 7-14 differ in three amino acid residues and the N-terminal fatty acid chains. The diversity of the holrhizins originates from the substrate flexibility of the A(4), A(5), and A(6) domains as well as the starter C domain in the biosynthetic pathway.