TAILIEUCHUNG - Báo cáo khoa học: Pyruvate:ferredoxin oxidoreductase and bifunctional aldehyde–alcohol dehydrogenase are essential for energy metabolism under oxidative stress in Entamoeba histolytica

The in vitro Entamoeba histolytica pyruvate:ferredoxin oxidoreductase (EhPFOR) kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were showed a strong preference for pyruvate as substrate over other oxoacids. | Pyruvate ferredoxin oxidoreductase and bifunctional aldehyde-alcohol dehydrogenase are essential for energy metabolism under oxidative stress in Entamoeba histolytica Erika Pineda1 Rusely Encalada1 Jose S. Rodriguez-Zavala1 Alfonso Olivos-Garcia2 Rafael Moreno-Sanchez1 and Emma Saavedra1 1 Departamento de Bioquimica Institute Nacionalde Cardiologia Ignacio Chavez Mexico . Mexico 2 Departamento de Medicina Experimental Facultad de Medicina Universidad NacionalAutonoma de Mexico Mexico . Mexico Keywords Fe-S cluster glycolysis oxidative stress pyruvate ferredoxin oxidoreductase PFOR reactive oxygen species ROS Correspondence E. Saavedra Departamento de Bioquimica Instituto Nacionalde Cardiologia Ignacio Chavez Juan Badiano No. 1 Col. Seccion XVI CP 14080 Tlalpan Mexico . Mexico Fax 5255 55730994 Tel 5255 5573 2911 ext 1298 E-mail emma_saavedra2002@ Received 9 February 2010 revised 4 June 2010 accepted 17 June 2010 doi The in vitro Entamoeba histolytica pyruvate ferredoxin oxidoreductase EhPFOR kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were evaluated. EhPFOR showed a strong preference for pyruvate as substrate over other oxoacids. The enzyme was irreversibly inactivated by a long period of saturating O2 exposure IC50 mm whereas short-term exposure 30 min leading to 90 inhibition allowed for partial restoration by addition of Fe2 . CoA and acetyl-CoA prevented whereas pyruvate exacerbated inactivation induced by short-term saturating O2 exposure. Superoxide dismutase was more effective than catalase in preventing the inactivation indicating that reactive oxygen species ROS were involved. Hydrogen peroxide caused inactivation in an Fe2 -reversible fashion that was not prevented by the coenzymes suggesting different mechanisms of enzyme inactivation by ROS. Structural analysis on an EhPFOR 3D model suggested that the protection against ROS .

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