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RSS FeedsIJMS, Vol. 19, Pages 3946: Sulfonamide Inhibition Studies of a New ?-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica (International Journal of Molecular Sciences)

 
 

8 december 2018 18:00:15

 
IJMS, Vol. 19, Pages 3946: Sulfonamide Inhibition Studies of a New ?-Carbonic Anhydrase from the Pathogenic Protozoan Entamoeba histolytica (International Journal of Molecular Sciences)
 




A newly described β-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was recently shown to possess a significant catalytic activity for the physiologic CO2 hydration reaction (kcat of 6.7 × 105 s−1 and a kcat/Km of 8.9 × 107 M−1 s−1). A panel of sulphonamides and one sulfamate, some of which are clinically used drugs, were investigated for their inhibitory properties against EhiCA. The best inhibitors detected in the study were 4-hydroxymethyl/ethyl-benzenesulfonamide (KIs of 36–89 nM), whereas some sulfanilyl-sulfonamides showed activities in the range of 285–331 nM. Acetazolamide, methazolamide, ethoxzolamide, and dichlorophenamide were less effective inhibitors (KIs of 509–845 nM) compared to other sulfonamides investigated here. As β-CAs are not present in vertebrates, the present study may be useful for detecting lead compounds for the design of more effective inhibitors with potential to develop anti-infectives with alternative mechanisms of action.


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9 viewsCategory: Biochemistry, Biophysics, Molecular Biology
 
IJMS, Vol. 19, Pages 3947: Proteomic Characterization of Bradyrhizobium diazoefficiens Bacteroids Reveals a Post-Symbiotic, Hemibiotrophic-Like Lifestyle of the Bacteria within Senescing Soybean Nodules (International Journal of Molecular Sciences)
IJMS, Vol. 19, Pages 3945: The Cytomegalovirus-Specific IL-21 ELISpot Correlates with Allograft Function of Kidney Transplant Recipients (International Journal of Molecular Sciences)
 
 
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