Structure of methionine gamma-lyase from Clostridium sporogenesстатья
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Дата последнего поиска статьи во внешних источниках: 14 февраля 2019 г.
Аннотация:Methionine γ-lyase (MGL) is a pyridoxal 5′-phosphate-dependent enzyme that catalyzes the γ-elimination reaction of L-methionine. The enzyme is a promising target for therapeutic intervention in some anaerobic pathogens and has attracted interest as a potential cancer treatment. The crystal structure of MGL from Clostridium sporogenes has been determined at 2.37 Å resolution. The fold of the protein is similar to those of homologous enzymes from Citrobacter freundii , Entamoeba histolytica , Pseudomonas putida and Trichomonas vaginalis . A comparison of these structures revealed differences in the conformation of two flexible regions of the N- and C-terminal domains involved in the active-site architecture.