Journal article
Domain−Domain Interactions in the Aminoglycoside Antibiotic Resistance Enzyme AAC(6‘)-APH(2‘ ‘) †
Abstract
The most common determinant of aminoglycoside antibiotic resistance in Gram positive bacterial pathogens, such as Staphylococcus aureus, is a modifying enzyme, AAC(6')-APH(2' '), capable of acetylating and phosphorylating a wide range of antibiotics. This enzyme is unique in that it is composed of two separable modification domains, and although a number of studies have been conducted on the acetyltransferase and phosphotransferase activities …
Authors
Boehr DD; Daigle DM; Wright GD
Journal
Biochemistry, Vol. 43, No. 30, pp. 9846–9855
Publisher
American Chemical Society (ACS)
Publication Date
August 1, 2004
DOI
10.1021/bi049135y
ISSN
0006-2960
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AcetyltransferasesAminoglycosidesAnti-Bacterial AgentsBacillus subtilisBlotting, WesternChromatography, GelDNA Mutational AnalysisDrug Resistance, BacterialEnterococcus faecalisEnzyme StabilityEscherichia coliGuanosine TriphosphateHot TemperatureKineticsMicrobial Sensitivity TestsMultienzyme ComplexesPeptide FragmentsPhosphotransferases (Alcohol Group Acceptor)Protein Structure, SecondaryProtein Structure, TertiarySequence DeletionStaphylococcus aureus