不同寻常的proline的α-碳化促进了活性位点的成熟
Vasiliki E Fadouloglou1, Stavroula Balomenou1,2, Michalis Aivaliotis1
1Institute of Molecular Biology and Biotechnology , 70013 Heraklion, Crete, Greece.
Journal of the American Chemical Society
|March 24, 2017
概括
一种新型的氧化蛋白 (Pro) 活性改变了细菌多糖脱酶 (PDA). 这种脊椎修饰增强了酶功能,代表了细菌中独特的活性位点成熟过程.
科学领域:
- 生物化学
- 分子生物学
- 酵素学
背景情况:
- 在细菌中,氨酸 (Pro) 氧化在很大程度上是未被探索的.
- 多糖脱乙酶 (PDA) 是细菌病原体中的关键酶.
研究的目的:
- 在细菌PDA中识别和表征一种新的氧化活性.
- 了解这种修改的机制和功能影响.
主要方法:
- 位点定向的突变生成以确定催化残留物.
- 用于测量酶活性的生物化学测试.
- 质谱测试以确认产品的形成.
主要成果:
- 在细菌PDA的活性部位中发现了以前未知的Pro化活性.
- 这种活性特别改变了蛋白质骨架上的保存的Pro残留物,产生2-基 (2-Hyp).
- 通过改善过渡状态稳定性,Pro→2-Hyp转换增强了PDA活动.
结论:
- 这种化代表了一种新型的活性位点成熟,它修改了蛋白质骨干而不是侧链.
- 这些发现揭示了细菌的转化后修饰的新层, 具有重要的功能后果.
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