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Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site
Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable enzyme-pro...
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| 出版年: | Nat Commun |
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| 主要な著者: | , , , , , , , , , , , , , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group UK
2019
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6527550/ https://ncbi.nlm.nih.gov/pubmed/31110237 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-019-09691-z |
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