Kinetic and Chemical Modification Studies on Malate Dehydrogenase from E. coli

Author

Fang Jenny Zhao, Eastern Illinois University

Degree Name

Master of Science (MS)

Semester of Degree Completion

1994

Thesis Director

Norbert C. Furumo

Abstract

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 pK_a 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's from other sources.

Recommended Citation

Zhao, Fang Jenny, "Kinetic and Chemical Modification Studies on Malate Dehydrogenase from E. coli" (1994). Masters Theses. 2323.
https://thekeep.eiu.edu/theses/2323