Report

The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction

See allHide authors and affiliations

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

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Abstract

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}med-xtal.bu.edu (K.N.A.); dd39{at}unm.edu (D.D.-M.)

View Full Text