动氨酸细菌 pyranose 和 C-glycoside-3-oxidases 的演变和分离
Anja Kostelac1,2, André Taborda3, Lígia O Martins3
1Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Vienna, Austria.
Applied and environmental microbiology
|January 5, 2024
概括
FAD依赖的氧化酶 (POx) 和C-糖化-3-氧化酶 (CGOx) 酶从一个共同的祖先进化. 祖先酶的复活揭示了在某些基团中向C-糖化物特异性的进化,而另一些基团则保持单糖的偏好.
科学领域:
- 生物化学 生化学
- 酶学 是一种酶学.
- 进化生物学 进化生物学
背景情况:
- 依赖FAD的氧化酶 (POx) 和C-葡萄糖-3-氧化酶 (CGOx) 是葡萄糖-甲醇-胆超级家族中的氧化降解酶.
- 最近发现的细菌CGOx,在遗传学上与POx相关,与C-糖化物反应,表明它们具有共同的进化起源.
研究的目的:
- 为了研究POx/CGOx序列空间内的基质偏好的进化轨迹.
- 为了复活和描述祖先的酶,以了解单糖与C-糖化特异性的演变.
主要方法:
- 动态细菌POx/CGOx序列的遗传学分析.
- 七种祖先酶的复活和生化特征.
- 祖先酶形式的结构预测.
主要成果:
- 活性细菌的POx/CGOx酶进化为四个分类,具有不同的基质偏好.
- 类 I 酶表现出严格的单糖特异性,而类 III 和 IV 酶则是一般性酶,氧化单糖和C-糖化物.
- 对祖先酶的动态分析表明,在III和IV类中,向更高的C-糖化物偏好逐渐演变.
结论:
- POx/CGOx家族从一个通用祖先进化,随后的多样化导致了专门的酶.
- 由特定蛋白质域驱动的寡合化被假定有助于在Clade I POx酶中观察到的严格单糖特异性.
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