Pyruvate:ferredoxin oxidoreductase and bifunctional aldehyde-alcohol dehydrogenase are essential for energy metabolism under oxidative stress in Entamoeba histolytica

The FEBS Journal
Erika PinedaEmma Saavedra

Abstract

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 O(2) exposure (IC(50) 0.034 mm), whereas short-term exposure (< 30 min) leading to > 90% inhibition allowed for partial restoration by addition of Fe(2+). CoA and acetyl-CoA prevented, whereas pyruvate exacerbated, inactivation induced by short-term saturating O(2) 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 Fe(2+)-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 provided by coenzymes could be attributable to their proximity to the Fe-S clusters. After O(2) exposure, live parasites displayed decreased enzyme activities only for PFOR (90%) and aldehyde dehydrogena...Continue Reading

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Apr 30, 2015·Biotechnology Advances·Brendan R E AnsellAaron R Jex
Apr 13, 2013·Molecular & Cellular Proteomics : MCP·Laura Itzel Quintas-GranadosMaría Elizbeth Alvarez-Sánchez
Mar 16, 2017·Frontiers in Cellular and Infection Microbiology·Javier Cázares-ApátigaMario A Rodríguez
Dec 5, 2015·PLoS Neglected Tropical Diseases·Brendan R E AnsellAaron R Jex
Aug 8, 2021·Biochemical and Biophysical Research Communications·Lu XiaoYin Li

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