Understanding and overcoming aminoglycoside resistance caused by N-6′-acetyltransferase

MedChemComm
2012.0

Abstract

Aminoglycosides occupy a special niche amongst antibiotics in part because of their broad spectrum of action. Bacterial resistance is however menacing to render these drugs obsolete. A significant amount of work has been devoted to understand and overcome aminoglycoside resistance. This mini-review will discuss aminoglycoside-modifying enzymes (AMEs), with a special emphasis on the efforts to comprehend and block resistance caused by aminoglycoside 6'-N-acetyltransferase (AAC(6')).

Knowledge Graph

Similar Paper

Understanding and overcoming aminoglycoside resistance caused by N-6′-acetyltransferase
MedChemComm 2012.0
The use of aminoglycoside derivatives to study the mechanism of aminoglycoside 6′-N-acetyltransferase and the role of 6′-NH2 in antibacterial activity
Bioorganic & Medicinal Chemistry 2007.0
6-O-Nucleotidyltransferase: an aminoglycoside-modifying enzyme specific for streptomycin/streptidine
MedChemComm 2015.0
Synthesis and Biological Activity of Mono- and Di-N-acylated Aminoglycosides
ACS Medicinal Chemistry Letters 2015.0
Overexpression and Characterization of an Aminoglycoside 6'-N-Acetyltransferase with Broad Specificity from an  -Poly-L-lysine Producer, Streptomyces albulus IFO14147
Journal of Biochemistry 2004.0
AAC(6′)-Iaf, a Novel Aminoglycoside 6′- N -Acetyltransferase from Multidrug-Resistant Pseudomonas aeruginosa Clinical Isolates
Antimicrobial Agents and Chemotherapy 2009.0
Structural hybridization of three aminoglycoside antibiotics yields a potent broad-spectrum bactericide that eludes bacterial resistance enzymes
MedChemComm 2015.0
New Broad-Spectrum Antibacterial Amphiphilic Aminoglycosides Active against Resistant Bacteria: From Neamine Derivatives to Smaller Neosamine Analogues
Journal of Medicinal Chemistry 2016.0
Secondary aminoglycoside resistance in aminoglycoside-producing strains of Streptomyces
Gene 1992.0
The use of neamine as a molecular template: Inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3′-phosphotransferase type IIa
Bioorganic & Medicinal Chemistry Letters 1998.0