Aph(3′)-IIc, an Aminoglycoside Resistance Determinant from Stenotrophomonas maltophilia

Aph(3′)-IIc, an Aminoglycoside Resistance Determinant from Stenotrophomonas maltophilia Overexpression and Initial Characterization of the Chromosomal Aminoglycoside 3′- O -Phosphotransferase APH(3′)-IIb from Pseudomonas aeruginosa Nucleotide sequence of a streptomycete aminoglycoside phosphotransferase gene and its relationship to phosphotransferases encoded by resistance plasmids. Mutant APH(2″)-IIa Enzymes with Increased Activity against Amikacin and Isepamicin The use of neamine as a molecular template: Inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3′-phosphotransferase type IIa AmpD_IIs Involved in Expression of the Chromosomal L1 and L2 β-Lactamases ofStenotrophomonas maltophilia AAC(6′)-Iaf, a Novel Aminoglycoside 6′- N -Acetyltransferase from Multidrug-Resistant Pseudomonas aeruginosa Clinical Isolates AmpN-AmpG Operon Is Essential for Expression of L1 and L2 β-Lactamases inStenotrophomonas maltophilia Novel Apramycin Resistance Gene apmA in Bovine and Porcine Methicillin-Resistant Staphylococcus aureus ST398 Isolates Biochemical characterization of resistance determinants cloned from antibiotic-producing streptomycetes