PMID:9253408
| Citation |
Murphy, JE, Stec, B, Ma, L and Kantrowitz, ER (1997) Trapping and visualization of a covalent enzyme-phosphate intermediate. Nat. Struct. Biol. 4:618-22 |
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| Abstract |
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. |
| Links | |
| Keywords |
Alkaline Phosphatase/chemistry; Alkaline Phosphatase/genetics; Alkaline Phosphatase/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Hydrolysis; Metalloproteins/chemistry; Mutagenesis, Site-Directed; Phosphates/metabolism; Phosphoproteins/chemistry; Phosphoproteins/genetics; Phosphoproteins/metabolism; Recombinant Proteins/chemistry; Water/chemistry; Zinc/chemistry |
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