Lanthipeptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that display a wide variety of biological activities, from antimicrobial to antiallodynic. Lanthipeptides that display antimicrobial activity are called lantibiotics. The post-translational modification reactions of lanthipeptides include dehydration of Ser and Thr residues to dehydroalanine and dehydrobutyrine, a transformation that is carried out in three unique ways in different classes of lanthipeptides. In a cyclization process, Cys residues then attack the dehydrated residues to generate the lanthionine and methyllanthionine thioether cross-linked amino acids from which lanthipeptides derive their name. The resulting polycyclic peptides have constrained conformations that confer their biological activities. After installation of the characteristic thioether cross-links, tailoring enzymes introduce additional post-translational modifications that are unique to each lanthipeptide and that fine-tune their activities and/or stability. This review focuses on studies published over the past decade that have provided much insight into the mechanisms of the enzymes that carry out the post-translational modifications.

中文翻译：

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多肽多肽生物合成酶的机理理解。

脂肽是核糖体合成的和翻译后修饰的肽（RiPPs），具有从抗微生物到抗异常性疼痛的多种生物学活性。显示抗菌活性的羊毛肽被称为羊毛硫抗生素。多肽肽的翻译后修饰反应包括将Ser和Thr残基脱水为脱氢丙氨酸和脱氢丁胺，这是在三种不同的多肽肽中以三种独特的方式进行的转化。在环化过程中，Cys残基随后攻击脱水的残基，以生成羊毛硫氨酸和甲基羊毛硫氨酸硫醚交联的氨基酸，由此来命名长肽。所得的多环肽具有限制的构象，这些构象赋予了它们的生物学活性。在安装了特征性硫醚交联键后，定制酶会引入额外的翻译后修饰，这些修饰对于每种长肽都是独特的，并且可以微调它们的活性和/或稳定性。这篇综述的重点是过去十年发表的研究，这些研究对进行翻译后修饰的酶的机理提供了很多见识。