Abstract

docking simulations were performed on the open and the closed conformations of (S)-adenosyl-Lhomocysteine- hydrolase with a series of L-adeninylalanine analogues. Theoretical Ki values were calculated and compared to experimental Kis, determined after enzymatic assay. These results suggest that the competitive inhibitors evaluated bind reversibly to the open form of SAH-hydrolase and do not induce the conformational transition to the closed conformation.

Keywords: Docking study, SAH-hydrolase, inhibitors, antiviral agents, nucleoside analogues