Alcohol dehydrogenase
Alcohol dehydrogenase (ADH) is a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during the synthesis of various metabolites.
Structure[edit | edit source]
Alcohol dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during the synthesis of various metabolites.
Function[edit | edit source]
The main function of alcohol dehydrogenase is the metabolism of alcohol in the body. This enzyme catalyzes the conversion of alcohol into acetaldehyde, a highly toxic substance and carcinogen. The acetaldehyde is then further metabolized by acetaldehyde dehydrogenase into acetic acid, a relatively non-toxic substance.
Clinical significance[edit | edit source]
Alcohol dehydrogenase plays a crucial role in alcohol metabolism and alcoholism. The activity of this enzyme differs between individuals and can be influenced by genetic factors. Certain variants of the ADH gene are associated with a higher risk of alcoholism, while others are associated with a lower risk.
See also[edit | edit source]
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