ADH-1
Alcohol Dehydrogenase 1 (ADH-1)[edit | edit source]
Alcohol Dehydrogenase 1 (ADH-1) is an enzyme that plays a crucial role in the metabolism of alcohols within the human body. It is part of the alcohol dehydrogenase family, which is responsible for the oxidation of alcohols to aldehydes and ketones. ADH-1 is primarily found in the liver, where it catalyzes the conversion of ethanol to acetaldehyde, a key step in the metabolic pathway of alcohol.
Structure[edit | edit source]
ADH-1 is a zinc-dependent enzyme, meaning it requires zinc ions to function properly. The enzyme is a dimer, consisting of two identical subunits. Each subunit contains a zinc ion that is essential for its catalytic activity. The structure of ADH-1 allows it to bind to alcohol molecules and facilitate their conversion to aldehydes.
Function[edit | edit source]
The primary function of ADH-1 is to metabolize ethanol, the type of alcohol found in alcoholic beverages. When ethanol is consumed, ADH-1 oxidizes it to acetaldehyde, which is then further metabolized by aldehyde dehydrogenase to acetic acid. This process is crucial for the detoxification of alcohol in the body.
Genetic Variability[edit | edit source]
There is significant genetic variability in the ADH-1 gene among different populations. This variability can affect the enzyme's activity and, consequently, an individual's ability to metabolize alcohol. Some variants of ADH-1 are associated with faster or slower metabolism of ethanol, which can influence susceptibility to alcohol use disorder and other alcohol-related health issues.
Clinical Significance[edit | edit source]
ADH-1 is of clinical interest due to its role in alcohol metabolism. Variations in the ADH-1 gene can lead to differences in alcohol tolerance and the risk of developing alcohol-related diseases. Understanding these genetic differences can help in the development of personalized medical approaches to treating alcohol use disorders.
Related Enzymes[edit | edit source]
ADH-1 is one of several alcohol dehydrogenases in humans. Other members of the family include ADH-2 and ADH-3, which also participate in alcohol metabolism but have different substrate specificities and tissue distributions.
Related Pages[edit | edit source]
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Contributors: Prab R. Tumpati, MD
