Uncovering a Glycosyltransferase Provides Insights into the Glycosylation Step during Macrolactin and Bacillaene Biosynthesis
Uncovering a Glycosyltransferase Provides Insights into the Glycosylation Step during Macrolactin and Bacillaene Biosynthesis
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DOI：
10.1002/cbic.201402384
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发表时间：
2014-12-15
期刊：
影响因子：
3.2
通讯作者：
Li, Wenli
中科院分区：
文献类型：
--
作者：
Qin, Wen;Liu, Yang;Li, Wenli
大环内酯类化合物具有独特的24元环内酯结构和多种生物活性。MLN骨架通过反式酰基转移酶（AT）I型聚酮合酶（PKS）途径生物合成，但剪裁步骤仍然未知。在此，我们报告的糖基转移酶（GT）基因bmmGT 1，这是位于不同的位点从MLN基因簇的海洋来源的海洋芽孢杆菌B-9987的基因组中，其功能特性作为MLN GT，从而提供五个新的MLN类似物的鉴定。令人惊讶的是，这种GT也能够催化作为反式AT聚酮原型的芽孢杆菌（BAE）的糖基化，从而表明广泛的底物灵活性。这些结果提供了MLN和BAE生物合成途径中糖基化步骤的第一个重要见解。
Macrolactins (MLNs) have unique structural patterns containing a 24-membered ring lactone and diverse bioactivities. The MLN skeleton is biosynthesized via a trans-acyl transferase (AT) type I polyketide synthase (PKS) pathway, but the tailoring steps are still unknown. Herein, we report the identification of a glycosyltransferase (GT) gene bmmGT1, which is located at different locus from the MLN gene cluster in the genome of marine-derived Bacillus marinus B-9987, and its functional characterization as an MLN GT, thus affording five novel MLNs analogues. Surprisingly, this GT is also capable of catalyzing the glycosylation of bacillaenes (BAEs), which are the prototypes of trans-AT polyketides, thus suggesting broad substrate flexibility. These results provide the first significant insights into the glycosylation step in MLN and BAE biosynthetic pathways.