| Literature DB >> 31712217 |
Andrew R Mack1,2, Melissa D Barnes3,2, Magdalena A Taracila3,2, Andrea M Hujer3,2, Kristine M Hujer3,2, Gabriel Cabot4,5, Michael Feldgarden6, Daniel H Haft6, William Klimke6, Focco van den Akker7, Alejandro J Vila8,9,10,11, Andrea Smania12,13, Shozeb Haider14, Krisztina M Papp-Wallace3,7,15,2, Patricia A Bradford16, Gian Maria Rossolini17,18, Jean-Denis Docquier19, Jean-Marie Frère20, Moreno Galleni20, Nancy D Hanson21, Antonio Oliver4,5, Patrick Plésiat22,23,24, Laurent Poirel25,26, Patrice Nordmann25,26, Timothy G Palzkill27,28, George A Jacoby29, Karen Bush30, Robert A Bonomo31,3,32,7,15,2,8,33.
Abstract
Unlike for classes A and B, a standardized amino acid numbering scheme has not been proposed for the class C (AmpC) β-lactamases, which complicates communication in the field. Here, we propose a scheme developed through a collaborative approach that considers both sequence and structure, preserves traditional numbering of catalytically important residues (Ser64, Lys67, Tyr150, and Lys315), is adaptable to new variants or enzymes yet to be discovered and includes a variation for genetic and epidemiological applications.Entities:
Keywords: AmpC; amino acid numbering; beta-lactamases; class C beta-lactamase; conserved residue; nomenclature; structure-activity relationships
Mesh:
Substances:
Year: 2020 PMID: 31712217 PMCID: PMC7038296 DOI: 10.1128/AAC.01841-19
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191