在RiPP生物合成中,S9蛋白酶WprP2催化在前体上的均裂解
Jabal Rahmat Haedar1, Abujunaid Habib Khan1, Suze Ma2
1Latvian Institute of Organic Synthesis, Aizkraukles Street 21, LV-1006, Riga, Latvia.
Communications chemistry
|January 29, 2026
概括
研究人员发现了一种来自Streptomyces venezuelae的新型血清蛋白酶,WprP2. 这种酶均地分裂前体,扩大了S9蛋白酶在核糖体合成和翻译后修改的生物合成中的已知功能.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 自然产品生物合成 自然产品生物合成
背景情况:
- 核糖体合成和翻译后改性 (RiPPs) 是通过复杂途径合成的自然产物.
- 血清蛋白酶通过分裂前体在RiPP生物合成中发挥着至关重要的作用.
- RiPP结构的多样性表明尚未发现的酶和途径.
研究的目的:
- 识别和描述参与RiPP生物合成的新型血清蛋白酶.
- 为了研究来自Streptomyces venezuelae的非特征化血清蛋白酶WprP2的功能.
- 扩大对S9蛋白酶家族在天然产品合成中的理解.
主要方法:
- 生物信息分析以确定潜在的血清蛋白酶.
- 基因克隆和WprP2.2的异质表达
- 在体外生化测试中使用前体WprA2.2.
- 质谱测量以确认裂痕部位.
主要成果:
- 鉴定和表征了WprP2,一种来自Streptomyces venezuelae的新型血清蛋白酶.
- 证明WprP2在体外均地切割前体WprA2.
- 观察到WprP2的独特裂变活性,以前没有在其他血清蛋白酶中观察到.
- 已确认的WprP2被编码在一个激进的S-adenosyl-L-methionine酶 (WprB2) 旁边,该酶参与了循环生物合成.
结论:
- WprP2代表了S9血清蛋白酶家族的新成员,在RiPP生物合成中发挥着独特的作用.
- 发现WprP2扩大了RiPP前体处理的已知酶谱.
- 这一发现有助于理解天然产品生物合成的多样性和机制.
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