title: Common clinical substitutions enhance the carbapenemase activity of OXA-51-like class D β-lactamases from Acinetobacter spp.
authors.affiliation: Department of Chemistry, Grand Valley State University, Allendale, Michigan, USA.
authors.forename: Joshua M
authors.initials: JM
authors.lastname: Mitchell
authors.affiliation: Department of Chemistry, Grand Valley State University, Allendale, Michigan, USA leonardd@gvsu.edu.
authors.forename: David A
authors.initials: DA
authors.lastname: Leonard
mesh_terms: D000150:Acinetobacter / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D000151:Acinetobacter Infections / Q000188:drug therapy / Q000382:microbiology; D000667:Ampicillin / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism*; D015780:Carbapenems / Q000378:metabolism / Q000494:pharmacology*; D020134:Catalytic Domain; D003428:Cross Infection / Q000188:drug therapy / Q000382:microbiology; D006801:Humans; D017510:Protein Folding; D001618:beta-Lactamases / Q000235:genetics* / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D015780:Carbapenems; D000667:Ampicillin; D001618:beta-Lactamases; C577373:beta-lactamase OXA-51, Acinetobacter baumannii; C063912:carbapenemase