Arginine amidinase
Arginine Amidinase is an enzyme that catalyzes the hydrolysis of arginine into citrulline and ammonia. This enzyme is part of the urea cycle, which is a series of biochemical reactions that occur in many organisms. The urea cycle is crucial for the removal of ammonia and the production of urea.
Function[edit | edit source]
Arginine Amidinase, also known as L-arginine deiminase, is primarily found in microorganisms and plays a significant role in their nitrogen metabolism. The enzyme catalyzes the conversion of arginine to citrulline, releasing ammonia in the process. This reaction is a part of the broader urea cycle, which is essential for the detoxification of ammonia in the body.
Structure[edit | edit source]
The structure of Arginine Amidinase is complex and consists of multiple subunits. Each subunit contains a catalytic site where the reaction takes place. The enzyme's structure is crucial for its function, as it allows the enzyme to bind to arginine and catalyze its conversion into citrulline and ammonia.
Clinical Significance[edit | edit source]
Arginine Amidinase has potential therapeutic applications, particularly in the treatment of certain types of cancer. Some cancer cells are deficient in argininosuccinate synthetase, an enzyme that synthesizes arginine. Therefore, these cells rely on external sources of arginine for survival. Arginine Amidinase can deplete these external sources of arginine, leading to the death of the cancer cells.
See Also[edit | edit source]
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 The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes.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 Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD