Glycosyltransferases are essential tools for in vitro glycoengineering. Bacteria harbor an unexplored variety of protein glycosyltransferases. Here, we describe a peptide glycosyltransferase (EntS) encoded by ORF0417 of Enterococcus faecalis TX0104. EntS di-glycosylates linear peptide of enterocin 96 - a known antibacterial, in vitro. It is capable of transferring as well as extending the glycan onto the peptide in an iterative sequential dissociative manner. It can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(β)Glc/Gal(-O/S)Ser/Thr/Cys, in one pot. Using EntS generated glycovariants of enterocin 96 peptide, size and identity of the glycan are found to influence bioactivity of the peptide. The study identifies EntS as an enzyme worth pursuing, for in vitro peptide glycoengineering.

中文翻译：

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迭代糖基转移酶EntS催化肠球蛋白96中O和S联单糖的转移和延伸。

糖基转移酶是用于体外糖工程的必不可少的工具。细菌带有未开发的各种蛋白质糖基转移酶。在这里，我们描述了由粪肠球菌TX0104的ORF0417编码的肽糖基转移酶（EntS）。EntS二糖基化肠球蛋白96的线性肽-一种已知的体外抗菌剂。它能够以迭代顺序解离的方式将聚糖转移以及扩展到肽上。它可以在一锅中催化多种连接：Glc / Gal（-O）Ser / Thr，Glc / Gal（-S）Cys和Glc / Gal（β）Glc / Gal（-O / S）Ser / Thr / Cys 。使用EntS产生的肠球蛋白96肽糖变异体，发现聚糖的大小和特性会影响该肽的生物活性。这项研究确定了EntS是一种值得追求的酶，用于体外肽糖工程。