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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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Main Authors: Wang, Jie, Kantrowitz, Evan R.
格式: Artigo
語言:Inglês
出版: Cold Spring Harbor Laboratory Press 2006
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在線閱讀: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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