title: Structural and Functional Aspects of Extended-Spectrum AmpC Cephalosporinases.
abstract: β-lactam antibiotics have revolutionized modern medicine, but resistance to these drugs is a major public health crisis. Traditionally, class C β-lactamases were referred to as cephalosporinases due to their substrate preference for this particular class of β-lactams. However, the emergence of AmpC enzymes with extended-spectrum activity (extended-spectrum cephalosporinases or ESACs) is particularly worrisome, especially given that most clinical β-lactamase inhibitors are ineffective against these enzymes. This review summarizes structures of several extended spectrum class C β-lactamases and analyzes the structure-function relationship observed among them.
authors.affiliation: Department of Chemistry, Grand Valley State University 1 Campus Drive, Allendale, MI 49401, USA. powersra@gvsu.edu.
authors.forename: Rachel A
authors.initials: RA
authors.lastname: Powers
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002510:Cephalosporinase / Q000737:chemistry* / Q000378:metabolism*; D015195:Drug Design; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation; D018440:beta-Lactam Resistance; D065093:beta-Lactamase Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D008024:Ligands; D065093:beta-Lactamase Inhibitors; D002510:Cephalosporinase; C048795:AmpC beta-lactamases; D001618:beta-Lactamases