Using a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate.
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Murphy, J., Stec, B., Ma, L. et al. Trapping and visualization of a covalent enzyme–phosphate intermediate. Nat Struct Mol Biol 4, 618–622 (1997). https://doi.org/10.1038/nsb0897-618
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DOI: https://doi.org/10.1038/nsb0897-618
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