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 |
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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: |
Azides
Brucella suis Hydrazide Histidinol dehydrogenase 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship Biosynthesis Drug Discovery Moiety [CHIM]Chemical Sciences Histidine Sulfones Enzyme Inhibitors 030304 developmental biology Pharmacology 0303 health sciences biology 030306 microbiology [CHIM.ORGA]Chemical Sciences/Organic chemistry General Medicine biology.organism_classification Structural factor Anti-Bacterial Agents Alcohol Oxidoreductases chemistry Biochemistry Bacteria |
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 |
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