Event Title
Probing the Binding Site in the Antibiotic Resistance Enzyme, AmpC Beta-lactamase
Presentation Type
Poster/Portfolio
Presenter Major(s)
Chemistry
Mentor Information
Brad Wallar
Department
Chemistry
Location
Henry Hall Atrium 42
Start Date
10-4-2013 1:00 PM
End Date
10-4-2013 2:00 PM
Keywords
Health, Life Science, Physical Science
Abstract
Beta-lactam drugs, such as penicillins and cephalosporins, are widely used to treat bacterial infections, but resistance to these drugs is increasingly becoming a problem. One of the main causes of resistance to these beta-lactam drugs is the bacterial production of beta-lactamase enzymes, such as AmpC. These enzymes are capable of breaking down the drug within their active sites, rendering the antibiotic unable to harm the bacteria. The exact roles that the active site amino acid residues play in the recognition and breakdown of the drug are not fully understood. Here, we investigate the role of the active site residue asparagine-152 (Asn152) in AmpC by mutating it to a glycine, serine, or threonine residue and examining the effect that these mutations have on kinetic and structural properties. Uncovering the specific role of Asn152 in the function of AmpC will be useful in the development of inhibitors to these enzymes in order to combat bacterial resistance.
Probing the Binding Site in the Antibiotic Resistance Enzyme, AmpC Beta-lactamase
Henry Hall Atrium 42
Beta-lactam drugs, such as penicillins and cephalosporins, are widely used to treat bacterial infections, but resistance to these drugs is increasingly becoming a problem. One of the main causes of resistance to these beta-lactam drugs is the bacterial production of beta-lactamase enzymes, such as AmpC. These enzymes are capable of breaking down the drug within their active sites, rendering the antibiotic unable to harm the bacteria. The exact roles that the active site amino acid residues play in the recognition and breakdown of the drug are not fully understood. Here, we investigate the role of the active site residue asparagine-152 (Asn152) in AmpC by mutating it to a glycine, serine, or threonine residue and examining the effect that these mutations have on kinetic and structural properties. Uncovering the specific role of Asn152 in the function of AmpC will be useful in the development of inhibitors to these enzymes in order to combat bacterial resistance.