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Structural and functional studies of proline catabolic enzymes
(University of Missouri--Columbia, 2007)
Catabolism is the oxidation of organic nutrients into simple end molecules to extract energy. For proline, the catabolic pathway involves two enzymes, Lproline dehydrogenase (PRODH, EC 1.5.99.8) and L-[delta]¹-pyrroline- ...
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 ...
Bioinformatics of protein bound water
(University of Missouri--Columbia, 2005)
Protein-bound water molecules are important components of protein structure, and therefore, protein function and energetics. Here we present a semi-automated computational approach for identifying conserved (i.e. structurally ...
Structural studies of glyceraldehyde-3-phosphate dehydrogenase complexes and the E. coli PutA DNA binding domain
(University of Missouri--Columbia, 2006)
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the formation of 1,3-bisphosphoglycerate from glyceraldehyde-3-phosphate. We have solved a high-resolution (1.75 Å) structure of a ...
Structural characterization of UDP-galactopyranose mutase from eukaryotic pathogens
(University of Missouri--Columbia, 2013)
UDP-galactopyranose mutase (UGM) is a unique flavoenzyme that catalyzes the interconversion between UDP-galactopyranose (UDP-Galp) and UDP-galactofuranose (UDP-Galf), without any net transfer of electrons. UGM is a central ...
Understanding substrate binding and movement in proline catabolic enzymesUnderstanding substrate binding and movement in proline catabolic enzymes
(University of Missouri--Columbia, 2014)
Proline catabolism is the breakdown of proline to glutamate. This is catalyzed by two enzymes that can be either distinct, monofunctional enzymes or fused into one bifunctional enzyme. When the two enzymes are fused together ...
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 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 and functional studies of proline catabolic enzymes and human aldehyde dehydrogenases
(University of Missouri--Columbia, 2015)
Oxidation of amino acids, like proline catabolism, is a central part of energy metabolism. Proline is oxidized to glutamate by two enzymes: proline dehydrogenase (PRODH) and 1-pyrroline-5-carboxylate dehydrogenase (P5CDH). ...
Structural, biochemical, and inhibition studies of proline biosynthetic enzymes
(University of Missouri--Columbia, 2019)
[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] Pyrroline-5-carboxylate reductase (PYCR) is the final enzyme in proline biosynthesis, catalyzing the NAD(P)H-dependent reduction of [Delta]1-pyrroli ...
Structural studies of flavoprotein inhibitors and inactivators
(University of Missouri--Columbia, 2020)
[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI--COLUMBIA AT REQUEST OF AUTHOR.] Flavoenzymes have a versatile capacity to catalyze a wide range of reactions, using their flavin cofactor. In this thesis, work on two ...