激进方法对酶β-乙烯结合的形成
Alessio Caruso1, Leah B Bushin1, Kenzie A Clark1
1Department of Chemistry , Princeton University , Princeton , New Jersey 08544 , United States.
Journal of the American Chemical Society
|December 7, 2018
概括
研究人员发现了一种新酶NxxcB, 这种激进的S-adenosylmethionine (RaS) 酶扩展了自然界的改和宏循环化方法.
科学领域:
- 生物化学
- 自然产品化学
- 酵素学
背景情况:
- 核糖体合成和转化后改性 (RiPP) 是一类多样化的天然产品.
- 定制酶为RiPP带来独特的化学功能.
- 在RiPP基因集群中异常的金属酶可能导致新的修饰.
研究的目的:
- 调查含有未经表征的激素S-adenosylmethionine (RaS) 金属酶的尚未探索的RiPP基因集群.
- 描述一个新的RaS酶NxxcB的催化活性.
- 识别新的型宏循环化策略并扩大RaS酶超级家族的库存.
主要方法:
- 生物信息搜索策略用于识别RiPP基因集群.
- 对RaS酶活性进行生物化学研究.
- 基质分析以确定酶特异性.
主要成果:
- 识别了由定数感知调节的RiPP基因集群与未表征的RaS金属酶.
- NxxcB通过将Cys-thiol与Asn残留物的β-碳连接而建立了分子内β-thioether键.
- NxxcB接受各种氨基酸,在未激活的位置创建非自然的β-thioether链接.
结论:
- 发现了一种由RaS酶NxxcB催化的新型β-thioether键形成.
- 这一发现扩大了已知的宏循环化策略.
- 证明了RaS酶超级家族的显著催化多功能性.
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