Event Title
Structure and Function of AmpC Beta-Lactamases
Presentation Type
Poster/Portfolio
Presenter Major(s)
Chemistry
Mentor Information
Brad Wallar
Department
Chemistry
Location
Henry Hall Atrium 99
Start Date
11-4-2012 9:00 AM
Keywords
Life Science
Abstract
Beta-lactamases are enzymes that are produced by bacteria that hydrolyze the beta-lactam ring in many different types of antibiotics (such as amoxicillin, cephalosporin, etc.) and thus play an important role in antibiotic resistance. These clinical applications are primarily focused on determining how to inhibit this hydrolysis and ultimately sustain the antibiotic well enough for it to complete its intended use. The research project in question has been focusing on AmpC, which is a class C beta-lactamase that can inactivate a range of known antibiotics. AmpC has been the focus for research due to the fact that, in a similar class C enzyme, P99, a mutant at the asparagine-152 residue has been found to completely change the profile of antibiotics that can bind in the active site. Using a combination of site-directed mutagenesis, protein purification, enzyme kinetics, and x-ray crystallography, we have been developing a structure-function relationship for the asparagine-152 residue.
Structure and Function of AmpC Beta-Lactamases
Henry Hall Atrium 99
Beta-lactamases are enzymes that are produced by bacteria that hydrolyze the beta-lactam ring in many different types of antibiotics (such as amoxicillin, cephalosporin, etc.) and thus play an important role in antibiotic resistance. These clinical applications are primarily focused on determining how to inhibit this hydrolysis and ultimately sustain the antibiotic well enough for it to complete its intended use. The research project in question has been focusing on AmpC, which is a class C beta-lactamase that can inactivate a range of known antibiotics. AmpC has been the focus for research due to the fact that, in a similar class C enzyme, P99, a mutant at the asparagine-152 residue has been found to completely change the profile of antibiotics that can bind in the active site. Using a combination of site-directed mutagenesis, protein purification, enzyme kinetics, and x-ray crystallography, we have been developing a structure-function relationship for the asparagine-152 residue.