激进SAM酶WprB在前体上催化Trp-C5和Arg-Cγ之间的统一交叉链接拓
Abujunaid Habib Khan1, Jabal Rahmat Haedar1, Vic Kiselov1
1Latvian Institute of Organic Synthesis, Aizkraukles Street 21, LV-1006 Riga, Latvia.
ACS chemical biology
|February 2, 2025
概括
研究人员发现了一种新型酶,WprB,它在中产生独特的交叉链接. 这一发现扩大了在翻译后修改中激进SAM (rSAM) 酶的已知功能.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 酶学 是一种酶学.
背景情况:
- 核糖体合成和翻译后改性 (RiPPs) 是一类多样化的天然产品.
- 已知激进SAM (rSAM) 酶可催化RiPP中的复杂修饰,包括交叉链的形成.
- 了解rSAM酶的多样性和机制对于发现新的生物活性化合物至关重要.
研究的目的:
- 在生物信息学上识别新的激进SAM (rSAM) 酶.
- 为了功能性地表征一种新发现的rSAM酶,WprB,来自Xenorhabdus* sp. 这是一个PSL,PSL.
- 阐明WprB对其前体,WprA.的特定交联活性.
主要方法:
- 对已知rSAM酶家族 (StrB,NxxcB,WgkB,RrrB,TqqB,GggB) 的生物信息分析,以确定新的候选者.
- 在大肠杆菌中发现的 WprB 酶的异质表达和功能特征.
- 分析以确定由WprB.催化交叉链的位置和性质.
主要成果:
- 通过生物信息查扩大rSAM酶谱.
- 来自 *Xenorhabdus* sp. 的 WprB 的识别和功能验证. 这是一个PSL,PSL.
- 证明WprB在WprA的三个WPR动机中催化了Trp-C5和Arg-Cγ之间的新型交叉链接.
结论:
- WprB代表了一个新发现的rSAM酶,具有独特的催化活性.
- 已识别的交叉链接扩大了已知由rSAM酶催化的修饰表.
- 这一发现为探索RiPP多样性和设计新的新途径打开了大门.
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