The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction

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Science  28 Mar 2003:
Vol. 299, Issue 5615, pp. 2067-2071
DOI: 10.1126/science.1082710

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Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated β-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme–Mg(II)–glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate.

  • * To whom correspondence should be addressed. E-mail: allen{at} (K.N.A.); dd39{at} (D.D.-M.)

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