Abdo Marie-Rose, Joseph Pascale, Boigegrain Rose-Anne, Montero Jean-Louis, Köhler Stephan, Winum Jean-Yves
Institut des Biomolécules Max Mousseron (IBMM) UMR 5247 CNRS-UM1-UM2 Bâtiment de Recherche Max Mousseron, Ecole Nationale Supérieure de Chimie de Montpellier, 8 rue de l'Ecole Normale, 34296 Montpellier Cedex, France.
J Enzyme Inhib Med Chem. 2008 Jun;23(3):357-61. doi: 10.1080/14756360701617107.
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.
组氨醇脱氢酶（HDH，EC 1.1.1.23）催化组氨酸生物合成的最后一步，是开发抗猪布鲁氏菌病病原体新药物的一个有吸引力的新靶点。基于L-组氨酰苯磺酰肼支架合成了一个新的HDH抑制剂小型文库，并研究了它们的抑制活性。所得结果表明，组氨酰部分和苯环之间基团的修饰是设计有效HDH抑制剂的一个重要结构因素。
