Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/87459
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

Synthesis and biological evaluation of new nanomolar competitive inhibitors of Helicobacter pylori type II dehydroquinase. Structural details of the role of the aromatic moieties with essential residues

AutorPrazeres, Verónica F. V.; van Raaij, Mark J. CSIC ORCID ; González-Bello, Concepción
Fecha de publicación2010
EditorAmerican Chemical Society
CitaciónJournal of Medicinal Chemistry 53(1): 191-200 (2010)
ResumenThe shikimic acid pathway is essential to many pathogens but absent in mammals. Enzymes in its pathway are therefore appropriate targets for the development of novel antibiotics. Dehydroquinase is the third enzyme of the pathway, catalyzing the reversible dehydratation of 3-dehydroquinic acid to form 3-dehydroshikimic acid. Here we present the synthesis of novel inhibitors with high affinity for Helicobacter pylori type II dehydroquinase and efficient inhibition characteristics. The structure of Helicobacter pylori type II dehydroquinase in complex with the most potent inhibitor shows that the aromatic functional group interacts with the catalytic Tyr22 by π-stacking, expelling the Arg17 side chain, which is essential for catalysis, from the active site. The structure therefore explains the favorable properties of the inhibitor and will aid in design of improved antibiotics. © 2009 American Chemical Society.
URIhttp://hdl.handle.net/10261/87459
DOI10.1021/jm9010466
Identificadoresdoi: 10.1021/jm9010466
issn: 0022-2623
e-issn: 1520-4804
Aparece en las colecciones: (IBMB) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

CORE Recommender

SCOPUSTM   
Citations

19
checked on 18-mar-2024

WEB OF SCIENCETM
Citations

19
checked on 26-feb-2024

Page view(s)

245
checked on 28-mar-2024

Download(s)

104
checked on 28-mar-2024

Google ScholarTM

Check

Altmetric

Altmetric


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.