The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry.

The sequence of the enterococcal cytolysin imparts unusual lanthionine stereochemistry.
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DOI:
10.1038/nchembio.1162
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发表时间:
2013-03
影响因子:
14.8
通讯作者:
van der Donk, Wilfred A.
van der Donk, Wilfred A.
中科院分区:
生物学1区
文献类型:
--
作者:
Tang, Weixin;van der Donk, Wilfred A.

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肠球菌溶血素是一种结构未知的双组分抗生素,具有溶血活性,对毒力具有重要作用。我们利用合成酶CylM与各前体多肽在大肠杆菌中共表达,制备了溶细胞素,并对其结构进行了鉴定。令人惊讶的是,细胞溶血素是第一个含有羊毛硫氨酸和甲基羊毛硫氨酸结构的抗生素,它们在同一肽中具有不同的立体化学,这是由底物肽的序列决定的。
The enterococcal cytolysin is a two-component lantibiotic of unknown structure with hemolytic activity that is important for virulence. We prepared cytolysin by co-expression of each precursor peptide with the synthetase CylM in E. coli, and characterized its structure. Surprisingly, cytolysin is the first example of a lantibiotic containing lanthionine and methyllanthionine structures with different stereochemistries in the same peptide, which is determined by the sequence of the substrate peptide.
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