在RiPP生物合成中扩大非正规氨基酸的面貌
Brooke A Johnson1, Kenzie A Clark1, Leah B Bushin1
1Department of Chemistry, Princeton University, Princeton, New Jersey 08544, United States.
Journal of the American Chemical Society
|February 5, 2024
概括
研究人员在Streptococcus pneumoniae的细菌天然产物中发现了新的修饰. 这项研究详细介绍了不同寻常的氨基酸的生物合成,扩大了RiPP及其酶的已知多样性.
科学领域:
- 微生物学
- 生物化学
- 自然产品化学
背景情况:
- 在DNA测序和生物信息学方面的进步揭示了微生物的新代谢途径.
- 之前的研究发现了链球菌中RiPPs的定数感知调节基因集群网络,包括Streptococcus pneumoniae独特的GRC亚系.
研究的目的:
- 阐明RiPPs的GRC亚家族的生物合成途径和酶修饰.
- 描述由GRC集群酶产生的新型非正规氨基酸.
主要方法:
- 在体内和体外生化测试.
- 用于基因集群识别的生物信息共发生策略.
主要成果:
- 一个类似ThiF的酶的化,安装一个C端的thiolactone宏循环.
- 两种激素S-adenosylmethionine (RaS) 酶的特征,它们负责l-allo-Thr和didehydrohistidine的形成.
- GRC产品产生了两个非正规的氨基酸,与其他具有异国情调宏循环的RaS-RiPP不同.
结论:
- 在RiPP生物合成中,GRC集群扩展了已知的非蛋白质氨基酸谱.
- 这些已识别的酶在天然产品合成中具有生物催化应用的潜力.
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