Sublancin is a 37-amino acid antimicrobial peptide belonging to the glycocin family of natural products. It contains two helices that are held together by two disulfide bonds as well as an unusual S-glucosidic linkage to a Cys in a loop connecting the helices. We report the reconstitution of the biosynthetic pathway to this natural product in Escherichia coli. This technology enabled the evaluation of the structure–activity relationships of the solvent-exposed residues in the helices. The biosynthetic machinery proved tolerant of changes in both helices, and the bioactivity studies of the resulting mutants show that two residues in helix B are important for bioactivity, Asn31 and Arg33.

中文翻译：

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S-连接的糖蛋白Sublancin的结构-活性关系。

Sublancin是一种37个氨基酸的抗菌肽，属于天然产物糖蛋白家族。它包含两个通过两个二硫键连接在一起的螺旋，以及一个在连接螺旋的环中与Cys异常连接的S-糖苷键。我们报告到这种天然产物在大肠杆菌中的生物合成途径的重建。这项技术能够评估螺旋中溶剂暴露的残基的构效关系。生物合成机制证明可以耐受两个螺旋的变化，对所得突变体的生物活性研究表明，螺旋B中的两个残基对生物活性至关重要，Asn31和Arg33。