Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity
Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity
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DOI：
10.1126/science.1092600
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发表时间：
2004-01-30
期刊：
影响因子：
56.9
通讯作者：
van der Donk, WA
中科院分区：
文献类型：
--
作者：
Xie, LL;Miller, LM;van der Donk, WA
lantibiotic lacticin 481是在核糖体上合成的前肽（pre - peptide, LctA），经翻译后修饰为成熟形式。这些修改。阳离子包括丝氨酸和苏氨酸的脱水，然后在分子内将半胱氨酸加成到不饱和氨基酸中，生成环硫醚。这个过程打破8个化学键，形成6个新键，由一种酶LctM催化。我们已经描述了LctM的体外活性，它完全处理了一系列LctA突变体，显示出允许的底物特异性，有望用于抗生素工程。
The lantibiotic lacticin 481 is synthesized on ribosomes as a prepeptide (LctA) and posttranslationally modified to its mature form. These modi. cations include dehydration of serines and threonines, followed by intramolecular addition of cysteines to the unsaturated amino acids, which generates cyclic thioethers. This process breaks eight chemical bonds and forms six newbonds and is catalyzed by one enzyme, LctM. We have characterized the in vitro activity of LctM, which completely processed a series of LctA mutants, displaying a permissive substrate specificity that holds promise for antibiotic engineering.