BIOCHEMISTRY AT MU
FACULTY RESEARCH
ACADEMICS
CONTACT LISTS
POSITION OPENINGS
| Email: | tiptonp@missouri.edu |
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| Phone: | (573) 882-7968 | |
| Lab: | (573) 882-1359 | |
| Fax: | (573) 884-4812 | |
| Office: | 204A Schlundt Annex | |
| Mailing Address: |
Biochemistry
117 Schweitzer Hall University of Missouri-Columbia Columbia, MO 65211 |
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| Research Areas: |
Mechanistic enzymology applied to agriculturally and medically important enzymes. |
Educational Background
| AB | Cornell University | Ithaca, N.Y. | Chemistry | |
| PhD | University of Wisconsin | Madison, Wis. | Biochemistry |
Notable Honors and Service
Research Description
We study the chemical mechanisms of enzyme-catalyzed reactions, to gain a deeper understanding of the physical basis for catalysis and, where appropriate, to provide guidelines for the development of specific and potent inhibitors. These goals come together in our study of enzymes from the opportunistic human pathogen Pseudomonas aeruginosa. We are studying the enzymes and proteins involved in the biosynthesis of the capsular polysaccharide alginate, which the bacteria secrete as a protective mechanism. We are also characterizing the enzymes responsible for synthesis of acylhomoserine lactones and alkylquinolones, which the bacteria use as communication molecules to coordinate infectious attacks and growth in biofilms.

We employ a variety of experimental approaches with an emphasis on kinetic studies. The projects offer the opportunity to utilize steady-state and transient-state kinetic methods, physical methods such as fluorescence and microcalorimetry, computational chemistry, and organic synthesis.
Selected Publications
Raychaudhuri, A., Jerga, A. and Tipton, P. A. (2005) Chemical Mechanism and Substrate Specificity of RhlI, an Acylhomoserine Lactone Synthase from Pseudomonas aeruginosa. Biochemistry 44, 2974-2981.
Naught, L. E. and Tipton, P. A. (2005) Formation and Reorientation of Glucose 1,6-Bisphosphate in the PMM/PGM Reaction: Transient-State Kinetic Studies. Biochemistry 44, 6831-6836.
Doll, C., Bell, A. F., Power, N., Tonge, P. J., and Tipton, P. A. (2005) Procatalytic Ligand Strain. Ionization and Perturbation of 8-Nitroxanthine at the Urate Oxidase Active Site. Biochemistry 44, 11440-11446.
Kimmel, J. L., and Tipton, P. A. (2005) Inactivation of GDP-mannose Dehydrogenase from Pseudomonas aeruginosa by penicillic acid identifies a critical active site loop. Arch. Biochem. Biophys. 441, 132-140.
Jerga, A., Raychaudhuri, A., and Tipton, P. A. (2006) Pseudomonas aeruginosa C5-Mannuronan Epimerase: Steady-State Kinetics and Characterization of the Product. Biochemistry, 45, 552-560.
Majumdar, P., Wu, H., Tipton, P., and Glaser, R. (2006) Oxanosine is a Substrate of Adenosine Deaminase. Implications for the Quest for a Toxicological Marker for Nitrosation Activity. Chemical Research in Toxicology, 18, 1830-1841.
Todd, C. D., Tipton, P. A., Blevins, D. G., Piedras, P., Pineda, M., and Polacco, J. C. (2006) Update on Ureide Degradation in Legumes. Journal of Experimental Botany 57, 5-12.
Jerga, A., Stanley, M. D., and Tipton, P. A. (2006) Chemical Mechanism and Specificity of the C5-Mannuronan Epimerase Reaction. Biochemistry 45, 9138-9144.