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The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme
Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they...
Tallennettuna:
| Päätekijät: | , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
The National Academy of Sciences
2002
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC122163/ https://ncbi.nlm.nih.gov/pubmed/11818529 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.022628599 |
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