|
|||||
|
|
Brucella suis histidinol dehydrogenase: Synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide |
|
| Authors: | Marie-Rose Abdo Pascale Joseph Rose-Anne Boigegrain Jean-Louis Montero Stephan Köhler Jean-Yves Winum |
| Affiliation: | 1. Institut des Biomolécules Max Mousseron (IBMM) UMR 5247 CNRS-UM1-UM2 Batiment de Recherche Max Mousseron, Ecole Nationale Supérieure de Chimie de Montpellier, 8 rue de l'Ecole Normale, 34296, Montpellier Cedex, France;2. Centre d'Etudes d'Agents Pathogènes et Biotechnologies pour la Santé (CPBS) UMR 5236 CNRS-UM1-UM2, Université Montpellier II, cc100, Place E. Bataillon, 34095, Montpellier, France |
| Abstract: | 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. |
| Keywords: | Brucella suis histidinol dehydrogenase enzyme inhibitors histidinylphenylsulfonyl hydrazide |