NDLI: In vivo identification of the steps that control energy metabolism and survival of Entamoeba histolytica.

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In vivo identification of the steps that control energy metabolism and survival of Entamoeba histolytica.

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In vivo identification of the steps that control energy metabolism and survival of Entamoeba histolytica.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Pineda, Erika Encalada, Rusely Vázquez, Citlali Néquiz, Mario Olivos-García, Alfonso Moreno-Sánchez, Rafael Saavedra, Emma
Description	Author Affiliation: Pineda E ( Departamento de Bioquímica, Instituto Nacional de Cardiología Ignacio Chávez, México D.F, México.)
Abstract	The steps that control the Entamoeba histolytica glycolytic flux were here identified by elasticity analysis, an experimental approach of metabolic control analysis. The concentrations of glycolytic metabolites were gradually varied in live trophozoites by (a) feeding with different glucose concentrations and (b) inhibiting the final pathway steps; in parallel, the changes in the pathway flux were determined. From the metabolite concentration-flux relationship, the elasticity coefficients of individual or groups of pathway reactions were determined and used to calculate their respective degrees of control on the glycolytic flux (flux control coefficients). The results indicated that the pathway flux was mainly controlled (72-86%) by the glucose transport/hexokinase/glycogen degradation group of reactions and by bifunctional aldehyde-alcohol dehydrogenase (ADHE; 18%). Further, inhibition of the first pathway reactions with 2-deoxyglucose (2DOG) decreased the glycolytic flux and ATP content by 75% and 50%, respectively. Cell viability was also decreased by 2DOG (25%) and more potently (50%) by 2DOG plus the ADHE inhibitor tetraethylthiuram disulfide (disulfiram). Biosate as an alternative carbon (amino acid) source was unable to replace glucose for ATP supply, which indicated that glucose was the main nutrient for amoebal ATP synthesis and survival. These results indicated that glycolysis in the parasite is mainly controlled by the initial pathway reactions and that their inhibition can decrease the parasite energy load and survival.
File Format	HTM / HTML
ISSN	1742464X
Issue Number	2
Volume Number	282
e-ISSN	17424658
Journal	FEBS Journal
Language	English
Publisher	Wiley (on behalf of the Federation of European Biochemical Societies)
Publisher Date	2015-01-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Alcohol Dehydrogenase Metabolism Aldehyde Dehydrogenase Energy Metabolism Entamoeba Histolytica Biological Transport Genetics Growth & Development Pathogenicity Glycolysis Kinetics Models, Biological Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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The bifunctional Entamoeba histolytica alcohol dehydrogenase 2 (EhADH2) protein is necessary for amebic growth and survival and requires an intact C-terminal domain for both alcohol dahydrogenase and acetaldehyde dehydrogenase activity.

The Bifunctional Entamoeba histolytica Alcohol Dehydrogenase 2 (EhADH2) Protein Is Necessary for Amebic Growth and Survival and Requires an Intact C-terminal Domain for Both Alcohol Dehydrogenase and Acetaldehyde Dehydrogenase Activity

An Alcohol Dehydrogenase 3 (ADH3) From Entamoeba histolytica is Involved in the Detoxification of Toxic Aldehydes

The Bifunctional Entamoeba histolytica Alcohol Dehydrogenase 2 (EhADH2) Protein Is Necessary for Amebic Growth and Survival and Requires an Intact C-terminal Domain for Both Alcohol Dehydrogenase and Acetaldehyde Dehydrogenase Activity *

Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.

Cloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene of Entamoeba histolytica.

Roles of acetyl-CoA synthetase (ADP-forming) and acetate kinase (PPi-forming) in ATP and PPi Supplementary in Entamoeba histolytica

Complementation of an Escherichia coli adhE mutant by the Entamoeba histolytica EhADH2 gene provides a method for the identification of new antiamebic drugs.

Characterization of pH-induced transitions of Entamoeba histolytica D-phosphoglycerate dehydrogenase.

In vivo identification of the steps that control energy metabolism and survival of Entamoeba histolytica.

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