English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/127960
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

6-O-Nucleotidyltransferase: an aminoglycoside-modifying enzyme specific for streptomycin/streptidine

AuthorsLatorre, Montserrat; Revuelta, Julia ; García-Junceda, Eduardo ; Bastida, Agatha
KeywordsAminoglycosides
Antibiotics
Resistance enzymes
Decoy acceptor
Issue Date2016
PublisherRoyal Society of Chemistry (UK)
CitationMedChemCommun (7) : 177-183 (2016)
AbstractAminoglycosides are especially useful for the treatment of hospital-acquired infections. The main problem for the application of these antibiotics is the presence of bacterial resistance enzymes, in particular, nucleotidyltransferases (ANTs). These enzymes catalyze the transfer of an adenylyl group from the MgATP complex to different positions of the antibiotic. To understand the mechanisms that lead to antibiotic inactivation, we have performed a comprehensive experimental analysis of one of those enzymes. The 6-O- nucleotidyltransferase enzyme (ANT(6)) from Bacillus subtilis was cloned, overexpressed and purified in E. coli. The kinetic parameters revealed a narrow specificity of the ANT(6) for MgATP/streptomycin as substrates. The binding epitope of the streptomycin recognized by the ANT(6) is the streptidine moiety. Therefore, the use of streptidine as a “decoy acceptor” allows the recovery of the antibiotic activity of streptomycin E. coli cells that are overexpressing the ANT(6).
Publisher version (URL)http://dx.doi.org/10.1039/C5MD00496A
URIhttp://hdl.handle.net/10261/127960
DOI10.1039/C5MD00496A
ISSN2040-2503
E-ISSN2040-2511
Appears in Collections:(IQOG) Artículos
Files in This Item:
File Description SizeFormat 
Med. Chem. Commun., 2016, 7, 177–183.pdfArtículo principal1,85 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.