Office #: FH-125
Pharm.D., 1987, University of Buenos Aires, Argentina
Ph.D., 1993, Leloir Institute, University of Buenos Aires, Argentina
Postdoctoral, 1993-2000, Michigan State University
Assistant Professor (Research), 2000-2005, Michigan State University
Starch & Enzyme Evolution
Our research focuses on the enzymes of the synthesis of glycogen in bacteria, and starch in plants, with a particular interest in their molecular evolution. These metabolic pathways are excellent candidates to study evolution of molecular function. They are related and developed early in evolution. In addition, they are regulated and composed by few enzymes. We intend to find how regulation appeared and evolved in this pathway, how catalysis was modified, and how specificity for substrates originated. We use molecular modeling, phylogenetic analysis, protein chemistry, enzyme kinetics, and recombinant DNA technology to address these questions.
Our projects are very important not only for the basic knowledge of the evolution of these pathways, but also for more immediate purposes. Starch is the most abundant energy storage compound used by plants and determines the yield of important crops. A deeper knowledge of the enzymes of this pathway allows the rational manipulation of starch production. There is an increasing interest in this field because of its impact. The fruits of this basic science would serve to attack a critical problem of mankind: malnutrition. Funded by National Science Foundation Grants MCB 0615982 and MCB 1024945.
- Advanced Enzymology
- Current Concepts in Biochemistry
- Biochemistry laboratory
- Elementary Physiological Chemistry B
- International Workshop in "Modern Techniques in Protein Science"
- Modern Techniques in Protein Science
- Science and Society
Current Publications via PubMed
Kuhn, M.L., Figueroa C.M., Aleanzi, M., Olsen, K.W., Iglesias, A.A., and Ballicora, M.A. (2010) "Bi-national and interdisciplinary course in enzyme engineering", Biochem. Mol. Biol. Ed., 38: 370-379.
Kuhn, M.L., Falaschetti, C.A. and Ballicora, M.A. (2009) "Ostreococcus tauri ADP-glucose pyrophosphorylase reveals alternative paths for the evolution of subunit roles" J. Biol. Chem. 284:34092-34102.
Ziegler, A.J., Florián, J., Ballicora, M.A. and Herlinger, A.W. (2009) "Alkaline phosphatase inhibition by vanadyl-Beta-diketone complexes: electron density effects" J. Enzym. Inhib. Med. Chem.24:22-28.
Ventriglia, T., Kuhn, M.L., Ruiz, M.T., Ribeiro-Pedro, M., Valverde, F., Ballicora, M.A., Preiss, J., and Romero, J.M. (2008) "Two Arabidopsis ADP-glucose pyrophosphorylase large subunits (APL1 and APL2) are catalytic" Plant Physiol. 148:65-76.
Malarkey, C.S., Wang, G., Ballicora, M.A. and de Freitas, D.E.M. (2008) "Evidence for two distinct Mg2+ binding sites in G(s)alpha and G(i)alpha(1) proteins" Biochem. Biophys. Res. Commun. 372:866-869.
Ballicora, M.A., Erben, E.D., Yazaki, T., Bertolo, A.L., Demonte, A.M., Schmidt, J.R., Aleanzi, M., Bejar, C.M., Figueroa, C.M., Fusari, C.M., Iglesias, A.A. and Preiss, J. (2007) "Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis" J. Bacteriol. 189:5325-5333.
Ventriglia, T., Ballicora, M.A., Crevillén, P., Preiss, J. and Romero, J.M. (2007) "Regulatory properties of potato-Arabidopsis hybrid ADP-glucose pyrophosphorylase" Plant Cell Physiol. 48:875-880.
Bejar, C.M., Ballicora, M.A., Iglesias, A.A. and Preiss, J. (2006) "ADPglucose pyrophosphorylase's N-terminus: structural role in allosteric regulation" Biochem. Biophys. Res. Commun. 343:216-221.
Bejar, C.M., Jin, X., Ballicora, M.A. and Preiss, J. (2006) "Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases" J. Biol. Chem. 281:40473-40484.
Ballicora, M.A., Dubay, J.R., Devillers, C.H. and Preiss, J. (2005) "Resurrecting the ancestral enzymatic role of a modulatory subunit" J. Biol. Chem. 280:10189-10195. (Paper of the Week)