Journal article
Molecular Mechanism of the Enterococcal Aminoglycoside 6‘-N-Acetyltransferase‘: Role of GNAT-Conserved Residues in the Chemistry of Antibiotic Inactivation †
Abstract
The Gram-positive pathogen Enterococcus faecium is intrinsically resistant to aminoglycoside antibiotics due to the presence of a chromosomally encoded aminoglycoside 6'-N-acetyltransferase [AAC(6')-Ii]. This enzyme is a member of the GCN5-related N-acetyltransferase (GNAT) superfamily and is therefore structurally homologous to proteins that catalyze acetyl transfer to diverse acyl-accepting substrates. This study reports the investigation of …
Authors
Draker K-A; Wright GD
Journal
Biochemistry, Vol. 43, No. 2, pp. 446–454
Publisher
American Chemical Society (ACS)
Publication Date
January 1, 2004
DOI
10.1021/bi035667n
ISSN
0006-2960
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AcetyltransferasesAmino Acid SequenceAmino Acid SubstitutionAminoglycosidesAnti-Bacterial AgentsConserved SequenceDrug Resistance, BacterialEnterococcus faeciumEnzyme ActivationGlutamic AcidHistidineHistone AcetyltransferasesHydrogen-Ion ConcentrationKineticsLeucineMicrobial Sensitivity TestsMolecular Sequence DataMutagenesis, Site-DirectedTyrosine