Brucella suis histidinol dehydrogenase: synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide

Autor: Jean-Yves Winum, Pascale Joseph, Marie-Rose Abdo, Stephan Köhler, Rose-Anne Boigegrain, Jean-Louis Montero
Přispěvatelé: Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Centre d’études d’Agents Pathogènes et Biotechologies pour la Santé (CPBS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche en Infectiologie de Montpellier (IRIM), Laboratoire de chimie biomoléculaire (LCB), Université Montpellier 2 - Sciences et Techniques (UM2)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-MAYOLI SPINDLER SA-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2008
Předmět:
Zdroj: Journal of Enzyme Inhibition and Medicinal Chemistry
Journal of Enzyme Inhibition and Medicinal Chemistry, Informa Healthcare, 2008, 23 (3), pp.357-361. ⟨10.1080/14756360701617107⟩
ISSN: 1475-6374
1475-6366
DOI: 10.1080/14756360701617107⟩
Popis: International audience; Histidinol dehydrogenase (HDH, EC EC1.1.1.23) catalyses the final step in the biosynthesis of histidine and constitutes an attractive novel target for the development of new agents against the pathogenous, bacteria Brucella suis. A small library of new HDH inhibitors based on the L-histidinylphenylsulfonyl hydrazide scaffold has been synthesized and their inhibitory activity investigated. The obtained results demonstrate that modification of the group between the histidinyl moiety and the phenyl ring constitutes an important structural factor for the design of effective HDH inhibitors.
Databáze: OpenAIRE
Nepřihlášeným uživatelům se plný text nezobrazuje