4.7 Article

Modulation of Flexible Loops in Catalytic Cavities Reveals the Thermal Activation Mechanism of a Glycogen-Debranching Enzyme

期刊

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 70, 期 41, 页码 13358-13366

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.2c04487

关键词

glycogen-debranching enzyme; molecular dynamics simulations; structure modulation; thermal activation; thermophilic enzyme

资金

  1. National Key R&D Program of China
  2. Science and Technology Support Program (Modern Agriculture) of Jiangsu Province
  3. National Natural Science Foundation of China
  4. National First-class Discipline Program of Food Science and Technology
  5. [2019YFD0901901]
  6. [BE2022323]
  7. [32272263]
  8. [31901628]
  9. [JUFSTR20180204]

向作者/读者索取更多资源

In this study, a thermophilic glycogen-debranching enzyme with thermal activation property was simulated, revealing that temperature-induced structural modulation can open up the catalytic cavity and activate the enzyme's catalytic function. This provides new insights for enzyme engineering to achieve higher catalytic performance and stability.
Some thermophilic enzymes not only exhibit high thermostability at high temperatures but also have an activation effect by thermal incubation. However, the correlations between temperature-induced structural modulation and thermal activation are still unclear. In this study, we selected a thermophilic glycogen-debranching enzyme from Saccharolobus solfataricus STB09 (SsGDE), which was a promising starch-debranching enzyme with a thermal activation property at temperatures ranging from 50 to 70 degrees C, to explore the thermal activation mechanism. Molecular dynamics simulations were performed for SsGDE at 30, 50, or 70 degrees C to reveal the temperature dependence of structure modulation and catalytic function. The results revealed that four loops (loop1 313-337, loop2 399-418, loop3 481-513, and loop4 540-574) in SsGDE were reshaped, which made the catalytic cavity more open. The internal residues, including the catalytic triad Asp3631, Glu399, and Asp471, could be exposed, due to the structural modulation, to exert catalytic functions. We proposed that the thermal activation effect of SsGDE was closely associated with the temperature-induced modulation of the catalytic cavity, which paved the way for further engineering enzymes to achieve higher catalytic performance and stability.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据