Although I do not yet have a specific thesis topic, I have been considering several projects. The area of research in which I am most interested is the study of the bacterial enzyme Beta-lactamase, which catalyzes the hydrolysis of Beta-lactam antibiotics such as penicillins and cephalosporins. Mutations at positions 237-241 in the active-site have been shown to improve catalytic activity greater than 100-fold over the wild-type enzyme. I am interested in doing x-ray crystallography and computer-based molecular modeling to study the effects of mutation in this region and to better understand the enzyme-substrate interactions that are involved. Hopefully, this research will provide insight that will lead to improved antibiotic therapy.
| Petrosino, J; Cantu 3rd, C; Palzkill, T (1998) beta-Lactamases: protein evolution in real time. Trends Microbiol 6:323-7 |
| Cantu 3rd, C; Palzkill, T (1998) The role of residue 238 of TEM-1 beta-lactamase in the hydrolysis of extended-spectrum antibiotics. J Biol Chem 273:26603-9 |
| Cantu 3rd, C; Huang, W; Palzkill, T (1997) Cephalosporin substrate specificity determinants of TEM-1 beta-lactamase. J Biol Chem 272:29144-50 |
| Cantu III, C; Huang, W; Palzkill, T (1996) Selection and characterization of amino acid substitutions at residues 237-240 of TEM-1 beta-lactamase with altered substrate specificity for aztreonam and ceftazidime. J Biol Chem 271:22538-45 |
