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J Biol Chem, Vol. 273, Issue 8, 4443-4448, February 20, 1998

Isolation and Characterization of the Carbon-Phosphorus Bond-forming Enzyme Phosphoenolpyruvate Mutase from the Mollusk Mytilus edulis

Alexander Kim, Jaebong Kim, Brian M. Martin^§, and Debra Dunaway-Mariano

From the  Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742 and the ^§ Molecular Neurogenetics Unit, Clinical Neuroscience Branch, National Institute of Mental Health, Bethesda, Maryland 20892

The enzyme phosphoenolpyruvate mutase was purified to homogeneity from the mollusk Mytilus edulis. The subunit size of the native homotetramer was determined to be 34,000 Da. The steady-state kinetic constants for catalysis of the conversion of phosphonopyruvate to phosphoenolpyruvate at pH 7.5 and 25 °C were measured at k_cat = 34 s¹, phosphonopyruvate K_m = 3 µM, and Mg²⁺ K_m = 4 µM. The enzyme displayed a broad specificity for divalent metal ion activation; Co²⁺, Mn²⁺, Zn²⁺, and Ni²⁺ are activators, whereas Ca²⁺ is not. Analysis of the pH dependence of the Mg²⁺-activated mutase-catalyzed reaction of phosphonopyruvate revealed one residue that must be protonated (apparent pK_a = 8.3) and a second residue that must be unprotonated (apparent pK_a = 7.7) for maximal catalytic activity.

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