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  • The bifunctional aldehyde-alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions.

The bifunctional aldehyde-alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions.

FEBS letters (2012-12-04)
Erika Pineda, Rusely Encalada, Alfonso Olivos-García, Mario Néquiz, Rafael Moreno-Sánchez, Emma Saavedra
ABSTRACT

By applying metabolic control analysis and inhibitor titration we determined the degree of control (flux control coefficient) of pyruvate:ferredoxin oxidoreductase (PFOR) and bifunctional aldehyde-alcohol dehydrogenase (ADHE) over the fluxes of fermentative glycolysis of Entamoeba histolytica subjected to aerobic conditions. The flux-control coefficients towards ethanol and acetate formation determined for PFOR titrated with diphenyleneiodonium were 0.07 and 0.09, whereas for ADHE titrated with disulfiram were 0.33 and -0.19, respectively. ADHE inhibition induced significant accumulation of glycolytic intermediates and lower ATP content. These results indicate that ADHE exerts significant flux-control on the carbon end-product formation of amoebas subjected to aerobic conditions.

MATERIALS
Product Number
Brand
Product Description

Disulfiram, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
Alcohol Dehydrogenase equine, recombinant, expressed in E. coli, ≥0.5 U/mg
Sigma-Aldrich
Tetraethylthiuram disulfide, ≥97.0% (S)
Sigma-Aldrich
Alcohol Dehydrogenase from Saccharomyces cerevisiae, powder, ≥300 units/mg protein, mol wt ~141,000 (four subunits)
Sigma-Aldrich
Alcohol Dehydrogenase from Saccharomyces cerevisiae
Sigma-Aldrich
Alcohol Dehydrogenase from Saccharomyces cerevisiae, ≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa