Alcohol dehydrogenase
Alcohol dehydrogenase[edit | edit source]
Alcohol dehydrogenase (ADH) is a group of enzymes that catalyze the conversion of alcohols to aldehydes or ketones with the reduction of NAD+ to NADH. These enzymes play a crucial role in the metabolism of alcohols in various organisms, including humans.
Structure[edit | edit source]
Alcohol dehydrogenases are typically dimeric or tetrameric enzymes, with each subunit containing a zinc ion that is essential for their catalytic activity. The zinc ion is coordinated by cysteine residues, as shown in the image
.
Function[edit | edit source]
The primary function of alcohol dehydrogenase is to facilitate the oxidation of alcohols to aldehydes or ketones. This reaction is important in the metabolism of ethanol in the liver, where ethanol is converted to acetaldehyde, a process that is crucial for the detoxification of alcohol in the body.
Types[edit | edit source]
There are several classes of alcohol dehydrogenases, each with different substrate specificities and tissue distributions. In humans, the most well-known is the class I alcohol dehydrogenase, which is primarily found in the liver.
Mechanism[edit | edit source]
The catalytic mechanism of alcohol dehydrogenase involves the transfer of a hydride ion from the alcohol to the NAD+ cofactor, forming NADH. The active site of the enzyme, depicted in
, is where this reaction takes place.
Clinical significance[edit | edit source]
Mutations or polymorphisms in alcohol dehydrogenase genes can affect an individual's ability to metabolize alcohol, influencing susceptibility to alcoholism and alcohol-related liver disease.
Related pages[edit | edit source]
Gallery[edit | edit source]
Liver alcohol dehydrogenase
Alcohol dehydrogenase structure
Crystal structure of alcohol dehydrogenase
Alcohol dehydrogenase[edit | edit source]
Structure of Alcohol Dehydrogenase 5
Liver Alcohol Dehydrogenase
Active site of Alcohol Dehydrogenase
Zinc interaction with Cysteine in Alcohol Dehydrogenase
Alcohol Dehydrogenase structure from PDB 1A4U
Alcohol Dehydrogenase structure from PDB 1JQA
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
|
WikiMD's Wellness Encyclopedia |
| Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates, categories Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD
