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The last steps of alcoholic fermentation in bacteria, plants, and yeast involve the conversion of pyruvate into acetaldehyde and carbon dioxide by the enzyme pyruvate decarboxylase, followed by the conversion of acetaldehyde into ethanol. The latter reaction is again catalyzed by an alcohol dehydrogenase, now operating in the opposite direction.
Individuals with two copies of the ALDH2*2 allele are known to have high blood acetaldehyde levels and experience “hangover” symptoms such as heart palpitations for longer durations, even with low alcohol consumption. [15] [16] [2] Individuals who work with DMF have shown a dose-related increase in alcohol intolerance complaints. [26]
After alcohol intake under the influence of disulfiram, the concentration of acetaldehyde in the blood may be five to 10 times higher than that found during metabolism of the same amount of alcohol alone. As acetaldehyde is one of the major causes of the symptoms of a hangover, this produces immediate and severe negative reaction to alcohol ...
[1] [2] The reaction has been variously termed a disulfiram-like reaction, alcohol intolerance, and acetaldehyde syndrome. [ 3 ] The prototypical drug of this group is disulfiram (brand name Antabuse), which acts as an acetaldehyde dehydrogenase inhibitor , preventing the metabolism of acetaldehyde into acetic acid , and is used in the ...
Chronic alcohol consumption leads to the accumulation of toxic metabolites, such as acetaldehyde and reactive oxygen species, in the heart muscle cells. [2] These toxic substances can cause oxidative stress, inflammation, and damage to the cardiomyocytes, leading to the development of ACM.
The best-known consequence of ALDH2 dysfunction is in relation to the consumption of ethanol. People heterozygous or homozygous for the ALDH2*2 metabolize ethanol to acetaldehyde normally but metabolize acetaldehyde poorly. As a result, they accumulate increased levels of acetaldehyde after consumption of alcoholic beverages.
The main alcohol dehydrogenase in yeast is larger than the human one, consisting of four rather than just two subunits. It also contains zinc at its catalytic site. Together with the zinc-containing alcohol dehydrogenases of animals and humans, these enzymes from yeasts and many bacteria form the family of "long-chain"-alcohol dehydrogenases.
Alcohol is removed from the bloodstream by a combination of metabolism, excretion, and evaporation. 90-98% of ingested ethanol is metabolized into carbon dioxide and water. [4] Around 5 to 10% of ethanol that is ingested is excreted unchanged in urine, breath, and sweat. [2]