羊毛硫肽类化合物(lanthipeptides)是一大类含有特征硫醚键的环肽类化合物。这类化合物广泛的分布于自然界中，具有多样的化学结构和生物活性。本项目研究集中于一个耐盐放线菌Streptomyces thermolilacinus SPC6来源的特殊的羊毛硫肽化合物。该化合物生物合成基因簇编码一个特殊的独立存在的SpaB_C家族蛋白TherB2。更为重要的是，其基因簇中可能的脱水酶TherB与目前所有已知的脱水酶序列相似性非常低，表明这可能是一类全新的羊毛硫肽脱水酶。特色和创新之处是拟以。该研究不仅将阐明一类全新的羊毛硫肽脱水酶机制，丰富我们对于tRNA参与天然产物生物合成的机制认识，同时也将极大的方便未来放线菌羊毛硫肽类化合物的结构和功能研究，为放线菌天然产物的研究提供重要的思路。

Lanthionine-containing peptides (lanthipeptides) are a rapidly growing family of polycyclic peptide natural products belonging to the large class of ribosomally synthesized and posttranslationally modified peptides (RiPPs). These natural products are widely distributed in taxonomically distant species, and their biosynthetic systems and biological activities are diverse. Our study focuses on a unusal lanthipeptide biosynthetic gene cluster from halophilic actinobacteria Streptomyces thermolilacinus SPC6. This gene cluster contains an unusal standalone SpaB_C-like protein TherB2, which is unprecedented in lanthipeptide literature. More intriguingly, the putative LanB dehydratase has very poor sequence similarity with all the known LanB-type enzymes, suggesting this enzyme may like involve novel tRNA-dependent biochemistry. Study of this intriuging lanthipeptide will facilate future efforts in study of lanthipeptides in actinobacteria, which represent a new and promising field for new antibiotic discovery.