Publication Date

5-1973

Advisor(s) - Committee Chair

Robert Farina, David Hartman, Curtis Wilkins

Degree Program

Department of Chemistry

Degree Type

Master of Science

Abstract

Within the past few years kinetic studies of NADP+- specific isocitrate dehydrogenase have been conducted extensively following isolation from bacteria, yeast and vertebrates. However, the kinetic properties of NADP+ - specific isocitrate dehydrogenase have not been adequately characterized in filamentous fungi. Therefore, the present study was undertaken to examine the kinetic behavior of partially purified NADP+ - specific isocitrate dehydrogenase enzyme isolated from Phycomyces blakesleeanus.

During this study Michaelis constants (Km) and maximum velocities (Vmax) were determined for threo-Ds-isocitrate, NADP+, and Mn2+ as well as the number of binding sites of these components to the enzyme. The order of reaction with respect to enzyme was also established. The effects of ionic strength, metal ions, coenzymes, coordinating ligands, and some inhibitors on the rate of reaction were investigated. Some experiments were performed to elucidate a possible reaction mechanism for the conversion of D-isocitric acid to α-ketoglutaric acid in the presence of coenzyme, NADP+, and Mn2+.

Disciplines

Chemistry | Physical Sciences and Mathematics

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