Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis
Abstract Understanding enzyme catalysis as connected to protein motions is a major challenge. Here, based on temperature kinetic studies combined with isotope effect measurements, we obtain energetic description of C-H activation in NAD-dependent UDP-glucuronic acid C4 epimerase. Approach from the e...
محفوظ في:
| المؤلفون الرئيسيون: | , , |
|---|---|
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
Nature Portfolio
2024-05-01
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| سلاسل: | Nature Communications |
| الوصول للمادة أونلاين: | https://doi.org/10.1038/s41467-024-48281-6 |
| الوسوم: |
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