Phosphomonoesterase
Phosphomonoesterase
Phosphomonoesterase is an enzyme that catalyzes the hydrolysis of phosphomonoester bonds, resulting in the release of a phosphate group and an alcohol. This enzyme plays a crucial role in various biological processes, including metabolism, signal transduction, and cellular regulation.
Function[edit | edit source]
Phosphomonoesterases are involved in the breakdown of phosphomonoesters, which are compounds containing a single esterified phosphate group. The enzyme's activity is essential for the recycling of phosphate within the cell, which is vital for maintaining cellular energy balance and nucleotide synthesis.
Types[edit | edit source]
There are several types of phosphomonoesterases, each with specific functions and substrate specificities. Some of the well-known types include:
- Alkaline phosphatase: Functions optimally at an alkaline pH and is involved in dephosphorylation processes.
- Acid phosphatase: Functions optimally at an acidic pH and is found in lysosomes.
- Phytase: Breaks down phytic acid to release phosphate and is important in plant and animal nutrition.
Mechanism[edit | edit source]
Phosphomonoesterases typically function by binding to the phosphomonoester substrate and facilitating the nucleophilic attack on the phosphorus atom by a water molecule. This reaction results in the cleavage of the phosphoester bond and the release of a free phosphate ion and an alcohol.
Clinical Significance[edit | edit source]
Abnormal levels of phosphomonoesterase activity can be indicative of various medical conditions. For example, elevated levels of alkaline phosphatase can be a marker for liver disease, bone disorders, and certain types of cancer. Conversely, low levels of this enzyme can indicate hypophosphatasia, a rare genetic disorder affecting bone mineralization.
Related Enzymes[edit | edit source]
Phosphomonoesterases are part of a larger family of enzymes known as phosphatases, which also include:
See Also[edit | edit source]
References[edit | edit source]
External Links[edit | edit source]
 | This enzyme-related article is a stub. You can help WikiMD by expanding it. |
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
