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

Marie-Rose Abdo (1) , Pascale Joseph (2) , Rose-Anne Boigegrain (3) , Jean-Louis Montero (4) , Stephan Köhler (3) , Jean-Yves Winum (1)

1 IBMM - Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]
2 CPBS - Centre d’études d’Agents Pathogènes et Biotechologies pour la Santé
3 IRIM - Institut de Recherche en Infectiologie de Montpellier
4 LCB - Laboratoire de chimie biomoléculaire

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.

Domaines: Chimie; Chimie organique

Marie-Rose Abdo, Pascale Joseph, Rose-Anne Boigegrain, Jean-Louis Montero, Stephan Köhler, et al.. Brucella suis histidinol dehydrogenase: Synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide. Journal of Enzyme Inhibition and Medicinal Chemistry, 2008, 23 (3), pp.357-361. ⟨10.1080/14756360701617107⟩. ⟨hal-02424977⟩