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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
摘要

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.

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Sigma-Aldrich
醇脱氢酶 来源于酿酒酵母, ≥300 units/mg protein, lyophilized powder (contains buffer salts), Mw 141-151 kDa
Sigma-Aldrich
醇脱氢酶 来源于酿酒酵母, powder, ≥300 units/mg protein, mol wt ~141,000 (four subunits)
Sigma-Aldrich
醇脱氢酶 来源于酿酒酵母
Sigma-Aldrich
二硫化四乙基秋兰姆, ≥97.0% (S)
Sigma-Aldrich
乙醇脱氢酶 马, recombinant, expressed in E. coli, ≥0.5 U/mg
双硫仑, European Pharmacopoeia (EP) Reference Standard