PMID:10085061
| Citation |
Holtz, KM, Stec, B and Kantrowitz, ER (1999) A model of the transition state in the alkaline phosphatase reaction. J. Biol. Chem. 274:8351-4 |
|---|---|
| Abstract |
A high resolution crystal structure of Escherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 A resolution. The vanadate ion takes on a trigonal bipyramidal geometry and is covalently bound by the active site serine nucleophile. A coordinated water molecule occupies the axial position opposite the serine nucleophile, whereas the equatorial oxygen atoms of the vanadate ion are stabilized by interactions with both Arg-166 and the zinc metal ions of the active site. This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction. |
| Links | |
| Keywords |
Alkaline Phosphatase/chemistry; Binding Sites; Crystallography, X-Ray; Escherichia coli; Kinetics; Models, Molecular; Vanadates/chemistry; Water/chemistry; Zinc/chemistry |
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