催化激活硫酸盐酸酶的结构基础,涉及金属结合氨酸修饰的金属结合氨酸
Takatoshi Arakawa1, Yoshiaki Kawano, Yoko Katayama
1Department of Biotechnology and Life Science, Graduate School of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
Journal of the American Chemical Society
|September 30, 2009
概括
硫酸酸酸酶 (SCNase) 的活性是由氨酸修饰的氨酸修饰的gammaCys133.3.决定的. 这种修改发生在储存过程中,增强重组SCNase功能.
科学领域:
- 生物化学 生物化学
- 酶学 是一种酶学.
- 结构生物学 结构生物学
背景情况:
- 酸盐酸酶 (SCNase) 属于酸盐酸酶家族.
- 它具有独特的非科林中心与两个翻译后修改的氨酸连接体:氨酸-硫酸 (Cys-SO(H)) 和氨酸-硫酸 (Cys-SO(2)).
研究的目的:
- 研究复合SCNase的成熟过程和活性决定因素.
- 阐明氨酸修饰在SCNase催化功能中的作用.
主要方法:
- 在储存前后对SCNase的结晶结构进行比较分析.
- 酶活性与氨酸修饰程度的相关性.
主要成果:
- 部分成熟的重组SCNase在储存期间显示激活.
- 在储存之前,gammaCys131的Cys-SO(2)(-) 修饰已经完成.
- 在储存过程中发生了gammaCys133的Cys-SO(H) 修饰,对活性至关重要.
- 进一步将gammaCys133氧化为Cys-SO(2)(-) 抑制了SCNase的活性.
结论:
- 氨酸硫酸修饰的gammaCys133对于SCNase活性至关重要.
- 储存期间的酶激活与gammaCys133.3.的现场修饰有关.
- 了解这些修改,可以了解酸酸酶机制.
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