The 5'-methylthioadenosine phosphorylase (MTAP)， an enzyme involved in purine and polyamine metabolism and in the methionine salvage pathway， is considered as a potential drug target against cancer and trypanosomiasis. In fact， Trypanosoma and Leishmania parasites lack de novo purine pathways and rely on purine salvage pathways to meet their requirements. Herein， we propose the first comprehensive bioinformatic and structural characterization of the putative Leishmania infantum MTAP (LiMTAP)， using a comparative computational approach.
The 5'-methylthioadenosine phosphorylase (MTAP)， an enzyme involved in purine and polyamine metabolism and in the methionine salvage pathway， is considered as a potential drug target against cancer and trypanosomiasis. In fact， Trypanosoma and Leishmania parasites lack de novo purine pathways and rely on purine salvage pathways to meet their requirements. Herein， we propose the first comprehensive bioinformatic and structural characterization of the putative Leishmania infantum MTAP (LiMTAP)， using a comparative computational approach.
