Bacterial Alkaloid Biosynthesis: Structural Diversity via a Minimalistic Nonribosomal Peptide Synthetase
Bacterial Alkaloid Biosynthesis: Structural Diversity via a Minimalistic Nonribosomal Peptide Synthetase
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DOI：
10.1016/j.chembiol.2018.02.013
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发表时间：
2018-06-21
影响因子：
8.6
通讯作者：
Stallforth, Pierre
中科院分区：
文献类型：
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作者：
Klapper, Martin;Braga, Daniel;Stallforth, Pierre
对荧光假单胞菌（Pseudomonasfluorescens）的一种最基本的非核糖体肽合成酶（NRPS）进行了化学和生物化学分析，发现其具有惊人的可塑性。潜在底物范围的确定使我们能够预测新的次级代谢产物，随后可以分离和测试其生物活性。详细分析的单峰的pyreudione合成酶表明，细菌pyreudione生物碱的生物合成不需要额外的生物合成酶。一个类似的和功能性的，但神秘的，NRPS的嗜虫假单胞菌的异源表达是成功的，并允许我们进行系统发育分析，他们的硫酯酶结构域。
Chemical and biochemical analyses of one of the most basic nonribosomal peptide synthetases (NRPS) from a Pseudomonas fluorescens strain revealed its striking plasticity. Determination of the potential substrate scope enabled us to anticipate novel secondary metabolites that could subsequently be isolated and tested for their bioactivities. Detailed analyses of the monomodular pyreudione synthetase showed that the biosynthesis of the bacterial pyreudione alkaloids does not require additional biosynthetic enzymes. Heterologous expression of a similar and functional, yet cryptic, NRPS of Pseudomonas entomophila was successful and allowed us to perform a phylogenetic analysis of their thioesterase domains.