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Mechanistic Studies On Malate Dehydrogenase From Escherichia Coli, S. Kirk Wright
Mechanistic Studies On Malate Dehydrogenase From Escherichia Coli, S. Kirk Wright
Masters Theses
Kinetic studies and chemical modification studies were performed on malate dehydrogenase from Escherichia coli (eMDH). Chemical modification studies using diethylpyrocarbonate and iodoacetic acid, along with log V/K profiles indicate that one ionizing group with a pKa between 7.9 and 8.5 acts as a general acid/base in the catalytic mechanism. Log V profiles suggest that malate binds to the correctly protonated form of the enzyme. These results imply that a histidine residue is required for catalysis.
A primary deuterium kinetic isotope effect of 1.43 (±0.14) was observed on V/K using malate-2-d, while no isotope effect was measured on Vmax …