Brucella suis histidinol dehydrogenase: synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide.
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.
Abdo
Marie-Rose
MR
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.
Joseph
Pascale
P
Boigegrain
Rose-Anne
RA
Montero
Jean-Louis
JL
Köhler
Stephan
S
Winum
Jean-Yves
JY
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors*; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D001386:Azides; D041021:Brucella suis / Q000201:enzymology*; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D006639:Histidine / Q000031:analogs & derivatives* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013450:Sulfones
D000900:Anti-Bacterial Agents; D001386:Azides; D004791:Enzyme Inhibitors; D013450:Sulfones; D006639:Histidine; D000429:Alcohol Oxidoreductases; C021358:histidinol dehydrogenase