10133-22-9Relevant articles and documents
THERAPEUTIC COMPOUNDS AND METHODS TO TREAT INFECTION
-
Paragraph 0454-0455, (2019/02/13)
Disclosed herein are compounds of formula I: or a salt thereof and compositions comprising a compound of formula I or a pharmaceutically acceptable salt thereof. Also disclosed herein are methods for treating or preventing a bacterial infection in an animal comprising administering to the animal a compound of formula I or a pharmaceutically acceptable salt thereof, alone or in combination with a bacterial efflux pump inhibitor.
COMPETITIVE INHIBITORS OF TYPE II DEHYDROQUINASE ENZYME
-
Page/Page column 23, (2012/01/13)
The present invention is directed to a compound of formula (I), its diastereoisomers, its enantiomers or its pharmaceutically acceptable salts or solvates, formula (I), to procedures of obtaining the same, to intermediates thereof, and use as competitive inhibitors of the third enzyme of the shikimic acid pathway, the type II dehydroquinase.
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
Prazeres, Verónica F. V.,Tizón, Lorena,Otero, José M.,Guardado-Calvo, Pablo,Llamas-Saiz, Antonio L.,Van Raaij, Mark J.,Castedo, Luis,Lamb, Heather,Hawkins, Alastair R.,González-Bello, Concepción
experimental part, p. 191 - 200 (2010/05/19)
The 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.
