Browsing College of Arts and Sciences (MU) by Thesis Advisor "Tanner, John J."
Now showing items 1-5 of 5
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Structural and kinetic studies of bifunctional and monofunctional proline catabolic enzymes
(University of Missouri--Columbia, 2011)PutAs, Proline dehydrogenase and P5C dehydrogenase are involved in the oxidation of proline to glutamate. Mutations in proline dehydrogenase and P5C dehydrogenase cause a disease condition known as hyperprolinemia. In this ... -
Structural basis of substrate recognition and inactivation in phosphatases
(University of Missouri--Columbia, 2011)Phosphatases are ubiquitous enzymes that catalyze the transfer of phosphoryl group to water. In addition to being one of the most important and fundamental reactions in biological systems, phosphatases are critical to ... -
Structural diversity of proline catabolic enzymes revealed by small angle x-ray scattering, x-ray crystallography and light scattering
(University of Missouri--Columbia, 2012)The proline catabolic enzymes catalyze the 4-electron oxidation of proline to glutamate. The reaction involves two enzymes, proline dehydrogenase (PRODH) and Δ1-pyrroline -5-carboxylate dehydrogenase (P5CDH). Some bacterial ... -
Structural studies of acid phosphatases from pathogenic bacteria
(University of Missouri--Columbia, 2007)Acid phosphatases are important, ubiquitous, and diverse group of enzymes that catalyze the transfer of phosphoryl from phosphomonoester to water forming inorganic phosphate and alcohol. These enzymes play critical roles ... -
Structural studies of type B proline utilization A (PutA) proteins
(University of Missouri--Columbia, 2016)[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT AUTHOR'S REQUEST.] This thesis addresses the structural studies of the type B proline utilization A (PutA) proteins. Proline utilization A (PutA) catalyzes the oxidation ...