Leishmania infantum 5'-Methylthioadenosine Phosphorylase presents relevant structural divergence to constitute a potential drug target

H Abid, E Harigua-Souiai, T Mejri, M Barhoumi… - BMC structural …, 2017 - Springer
Abstract Background 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 (Li …

O11-LEISHMANIA INFANTUM 5'-METHYLTHIOADENOSINE PHOSPHORYLASE PRESENTS RELEVANT STRUCTURAL DIVERGENCE TO CONSTITUTE A …

H Abid, E Harigua-Souiai, T Mejri… - Archives de l'Institut …, 2018 - search.proquest.com
Abstract 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. Here, Abid e al propose the first comprehensive bioinformatic and
structural characterization of the putative Leishmania infantum MTAP (LiMTAP), using a …
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