Thermodynamic properties of leukotriene A hydrolase inhibitors.

The leukotriene A hydrolase (LTAH) is a bifunctional enzyme, containing a peptidase and a hydrolase activity both activities having opposing functions regulating inflammatory response. The hydrolase activity is responsible for the conversion of leukotriene A to pro-inflammatory leukotriene B, and hence, selective inhibitors of the hydrolase activity are of high pharmacological interest. Here we present the thermodynamic characterization of structurally distinct inhibitors of the LTAH that occupy different regions of the binding site using different biophysical methods.