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Tungstate as a Transition State Analog for Catalysis by Alkaline Phosphatase
The catalytic mechanisms underlying Escherichia coli alkaline phosphatase’s (AP) remarkable rate enhancement have been probed extensively. Past work indicated that whereas the serine nucleophile (Ser102) electrostatically repels the product phosphate, another oxyanion, tungstate, binds more strongly...
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| Vydáno v: | J Mol Biol |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2016
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6169531/ https://ncbi.nlm.nih.gov/pubmed/27189921 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2016.05.007 |
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