Malate dehydrogenase (MDH) is the enzyme which catalyzes the conversion of malate to oxaloacetate in the TCA cycle. The object of this research was to discipher the mechanism of the reaction and the function of the enzyme. MDH from E. Coli was purified and analyzed by chemical modification studies using diethylpyrocarbonate. Results indicate the existence of a histidine residue at the active site necessary for catalysis. From kinetic studies, a group required for catalysis with a pKa of 8.5 was observed, which we believe to be a histidine residue. These studies indicate that MDH from E. Coli has a chemical and kinetic mechanism similar to MDH\u27s from other sources
