Professor Office: A314B Life Sciences Contact Phone Number: 542-1773 Lab: A316 Life Sciences Lab Phone: 542-1776 E-mail: brewer@bmb.uga.edu

Research Interests

I am interested in protein structure, particularly subunit structure, and how these are related to protein function.  The general experimental approaches employed are protein chemistry, enzymology and physical techniques, such as calorimetric and differential scanning calorimetric analyses, sedimentation velocity and equilibrium studies, stopped-flow measurements, fluorescence lifetime determinations and conventional spectroscopic experiments.

Most of my work currently is on enolase, mostly an isozyme from yeast and an isozyme from humans.  I am particularly interested in the relation of enzyme activity to their subunit association (the enzymes are dimers).  I have been collaborating with a protein crystallographer at the University of South Carolina, Dr. Lukasz Lebioda, preparing enolase mutants using site-directed mutagenesis techniques.  The residues altered are those that interact between subunits.  Once prepared, physical and enzymatic analyses are carried out to test their behavior, then the mutant enolases are sent to Dr. Lebioda for determination of the structure of their complexes with substrate.

The subunits appear to interact in an anticooperative fashion with a movable loop of each subunit interacting so that only one is near its substrate at a time.  Mutations of the residue(s) forming a hydrogen-bonded link between subunits in the yeast enzyme which keeps both loops from coming near the bound substrate molecules at the same time show effects related to, but different from, effects of mutation of a residue in the loop that interacts with bound substrate.

Recent Selected Publications

• Kataeva, I.A., Brewer, J.M., Uversky, V.N. and Ljungdahl, L.G.  Domain coupling in a multimodular cellobiohydrolase CbhA from Clostridium thermocellum.  FEBS Lett. 579 4367-4373 (2005).
  
  
• Brewer, J.M.  Electrophoresis.  In “Encyclopedia of Medical Devices and Instrumentation”.  Second Edition (Webster, J.G., ed.) John Wiley & Sons, Hoboken, New Jersey, Vol. 3, pp. 132-141 (2006).
  
  
• Qin, J., Chai, G., Brewer, J.M., Lovelace, L.L. and Lebioda, L.  Fluoride Inhibition of Enolase: Crystal Structure and Thermodynamics.  Biochemistry 45 793-800 (2006).
  
  
• Song, L., Teng, Q., Phillips, R.S., Brewer, J.M. and Summers, A.O.  19F-NMR reveals metal and operator-induced allostery in MeR.  J. Mol. Biol. in press.