Báo cáo khoa học: Molecular and biochemical characterization ofD-phosphoglycerate dehydrogenase fromEntamoeba histolytica A unique enteric protozoan parasite that possesses both phosphorylated and nonphosphorylated serine metabolic pathways
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A putative phosphoglycerate dehydrogenase (PGDH), which catalyzes the oxidation ofD-phosphoglycerate to 3-phosphohydroxypyruvate in the so-called phosphorylated serine metabolic pathway, from the enteric protozoan parasite Entamoeba histolytica was characterized. The E. histolyticaPGDH gene (EhPGDH) encodes a protein of 299 amino acids with a calculated molecular mass of 33.5 kDa and an isoelectric point of8.11. EhPGDHshowed high homology to PGDH from bacteroides and another enteric protozoan ciliate,Entodinium caudatum. ...
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