Molecular orbital studies of enzyme activity: catalytic mechanism of serine proteinases.
The catalytic activity of the serine proteinases is studied using molecular orbital methods on a model of the enzyme-substrate complex. A mechanism is employed in which Ser-195, upon donating a proton to the His-57-Asp-102 dyad, attacks the substrate to form the tetrahedral intermediate. As His-57 t...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1976
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC335923/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1061145/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.73.2.432 |
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