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The bifunctional aldehyde–alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions
Author(s) -
Pineda Erika,
Encalada Rusely,
Olivos-García Alfonso,
Néquiz Mario,
Moreno-Sánchez Rafael,
Saavedra Emma
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.11.020
Subject(s) - chemistry , aldehyde dehydrogenase , biochemistry , ethanol , glycolysis , flux (metallurgy) , acetaldehyde , alcohol dehydrogenase , alcohol , nad+ kinase , metabolism , organic chemistry , enzyme
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.