Dr. Corey M. Johnson
Assistant Professor of Biochemistry
- B.S., Chemistry, East Central University, 1998
- Ph.D., Biochemistry, University of Oklahoma, 2004
Dr. Johnson joined the Samford faculty in 2012. Before coming to Samford, he was an American Heart Association research fellow with the Oklahoma Medical Research Foundation for three years and a senior research fellow in Medicinal Chemistry at the University of Texas at Austin for three years. Dr. Johnson is a protein biochemist with a focus in enzymology.
Enzymes are fascinating biological catalysts and most often the target of designed therapeutics. Research projects in the Johnson lab are directed toward the functional characterization of enzymes. Kinetic analyses determine the order of addition of reactants to and release of products from the enzyme and can locate the slow steps along the reaction pathway. The detailed chemical mechanism of the enzyme is elucidated by testing substrate specificity, pH dependence, inhibition and the effects of mutation. One enzyme currently under study is Tetrahydrodipicolinate N-succinyltransferase (DapD). This enzyme is in the biosynthetic pathway for lysine in bacteria, but does not exist in humans. While DapD has great potential as a target for the development of new antibiotics, very little is known about its catalytic mechanism.
Another area of interest in the Johnson lab is developing new tools for functionally characterizing enzymes inside cells and tissues. Previously, Dr. Johnson identified some novel protein modifiers that are currently being used in biological and proteomic applications. The design and modification of enzyme inhibitors for in vivo functional characterization continues to be an approach employed by the Johnson lab. These studies employ chemical biology and cell biology techniques to compliment the classical biochemical research.
Research projects allow students to experience a broad spectrum of essential laboratory techniques, including recombinant DNA and molecular biology techniques, protein expression and purification techniques and enzyme assays.
Outside of Samford, Dr. Johnson enjoys spending time with his wife, Julie, and daughter, Charlotte, running with his dog, Clementine, and playing the guitar.
Johnson, C.M. and Fast, W. (2012) Pre-Steady State Kinetic Analysis of Dimethylarginine Dimethylaminohydrolase (DDAH) from Pseudomonas aeruginosa: Characterization of a Competent Thio-alkyluronium Intermediate (in preparation).
Johnson, C.M., Mozingo, A.F., Ke, Z., Yoon, D.-W., Linsky, T.W., Guo, H., Robertus, J.D., Fast, W. (2011) On the Mechanism of Dimethylarginine Dimethylaminohydrolase Inactivation by 4-Halopyridines. Journal of the American Chemical Society 133(28): 10951-9.
Johnson, C.M., Linsky, T., Yoon, D.-W., Person, M., and Fast, W. (2011) Discovery of Halopyridines as Quiescent Affinity Labels: Inactivation of Dimethylarginine Dimethylaminohydrolase. Journal of the American Chemical Society 133(5): 1553-62.
Johnson, C.M., and Rodgers, W.A. (2008) Spatial Segregation of Phosphatidylinositol 4,5-Bisphosphate (PIP2) Signaling in Immune Cell Functions. Immunology, Endocrine, and Metabolic Agents in Medicinal Chemistry 8: 349-357.
Johnson, C.M., Chichili, G.R., and Rodgers, W.A. (2008) Compartmentalization of Phoshpatidylinositol 4,5-Bisphosphate (PIP2) Signaling Evidenced using Targeted Phosphatases. Journal of Biological Chemistry 283(44):29920-29928.
Johnson, C.M., Roderick, S.L., and Cook, P.F. (2005) The Serine Acetyltransferase Reaction: Acetyl Transfer from an Acylpantothenyl Donor to an Alcohol. Archives of Biochemistry and Biophysics 433(1):85-95.
Johnson, C.M., Huang, B., Roderick, S.L., and Cook, P.F. (2004): Chemical Mechanism and Solvent Deuterium Isotope Effects of the Serine Acetyltransferase from Haemophilus Influenzae. Biochemistry 43(49): 15534-15539.
Johnson, C.M., Huang, B., Roderick, S.L., and Cook, P.F. (2004): Kinetic Mechanism of the Serine Acetyltransferase from Haemophilus Influenzae. Archives of Biochemistry and Biophysics 429(2) 115-122.
Tai, C.–H, Burkhard, P., Gani, D., Jenn, T., Johnson, C., and Cook, P.F. (2001): Characterization of the Allosteric Anion-Binding Site of O-Acetylserine Sulfhydyrlase. Biochemistry 40: 7446-7452.
Howard College of Arts and Sciences
Chemistry and Biochemistry Department
800 Lakeshore Drive
Birmingham, AL 35229
Office: PROPST 319
Phone: (205) 726-0000