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Trapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine
We report here the construction of a mutant version of Escherichia coli alkaline phosphatase (AP) in which the active site Ser was replaced by Thr (S102T), in order to investigate whether the enzyme can utilize Thr as the nucleophile and whether the rates of the critical steps in the mechanism are a...
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| Hlavní autoři: | , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2006
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| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2242381/ https://ncbi.nlm.nih.gov/pubmed/17008720 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.062351506 |
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