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• W2060997255 abstract "The proposed double in‐line displacement mechanism of Escherichia coli alkaline phosphatase (AP) involving two‐metal ion catalysis is based on NMR spectroscopic and X‐ray crystallographic studies. This mechanism is further supported by the X‐ray crystal structures of the covalent phospho‐enzyme intermediate of the H331Q mutant AP and of the transition state complex between the wild‐type enzyme and vanadate, a transition state analog. Kinetic and structural studies on several genetically engineered versions of AP illustrate the overall importance of the active site's metal geometry, hydrogen bonding network and electrostatic potential in the catalytic mechanism." @default.
• W2060997255 created "2016-06-24" @default.
• W2060997255 creator A5059952544 @default.
• W2060997255 creator A5070309634 @default.
• W2060997255 date "1999-11-22" @default.
• W2060997255 modified "2023-10-18" @default.
• W2060997255 title "The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site‐specific mutagenesis" @default.
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• W2060997255 doi "https://doi.org/10.1016/s0014-5793(99)01448-9" @default.
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