Corey Johnson joined Samford in 2012. Prior to that, he was an American Heart Association research fellow with the Oklahoma Medical Research Foundation for and a senior research fellow in Medicinal Chemistry at the University of Texas at Austin for three years. 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.

Applying enzymatic catalysis to industrial and environmental concerns is another area of interest in the Johnson lab. Recent work on the enzyme laccase characterizes the ability of this enzyme to catalyze degradation of wastewater pollutants. In a collaborative effort, this enzyme is being used as a model toward the development of biosensors and biofuel cells.

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, spectroscopy and enzyme assays.

Outside of Samford, Johnson enjoys spending time with his wife, Julie, and his kids, Charlotte and Sam, traveling and playing the guitar.

Degrees and Certifications

• BS, Chemistry, East Central University, 1998
• PhD, Biochemistry, University of Oklahoma, 2004

Publications

• Johnson, C.M. and Fast, W. (2022) On the Kinetic Mechanism of Dimethylarginine Dimethylaminohydrolase (DDAH). Bioorganic and Medicinal Chemistry 66: 116816.
• Beck, S., Berry, E., Duke, S., Milliken, A., Patterson, H., Prewett, D., Rae, C., Sridhar, S., Wendland, N., Gregory, B.W. and Johnson, C.M. (2018) Characterization of Trametes versicolor laccase-catalyzed oxidation of estrogenic pollutants: substrate inhibition and product identification. International Journal of Biodeterioration and Biodegradation 127: 146-159.
• Eldridge, H.C., Milliken, A., Farmer, C., Hampton, A.-S., Wendland, N., Coward, L., Gregory, D.J. and Johnson, C.M. (2017) Efficient Remediation of 17alpha-ethinylestradiol by Lentinula edodes (shiitake) Laccase. Biocatalysis and Agricultural Biotechnology 10: 64-68.
• 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.