Glycosyltransferases
Glycosyltransferases[edit | edit source]
Glycosyltransferases are a diverse group of enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. These enzymes play a crucial role in the biosynthesis of glycoconjugates, including glycoproteins, glycolipids, and polysaccharides.
Structure and Function[edit | edit source]
Glycosyltransferases are typically classified based on the type of glycosidic bond they form and the nature of their sugar donor and acceptor substrates. The donor molecules are usually nucleotide sugars, such as UDP-glucose or GDP-mannose. The acceptor molecules can be proteins, lipids, or other carbohydrates.
Mechanism[edit | edit source]
The catalytic mechanism of glycosyltransferases involves the formation of a glycosidic bond between the anomeric carbon of the sugar donor and a hydroxyl group of the acceptor. This process often requires the enzyme to undergo conformational changes to facilitate the transfer.
Biological Roles[edit | edit source]
Glycosyltransferases are essential for numerous biological processes, including:
- Cell-cell recognition and signaling
- Protein folding and stability
- Immune response modulation
- Pathogen-host interactions
Clinical Significance[edit | edit source]
Mutations or dysregulation of glycosyltransferases can lead to various diseases, such as congenital disorders of glycosylation (CDGs), cancer, and infectious diseases. Understanding the function and regulation of these enzymes is crucial for developing therapeutic strategies.
Research and Applications[edit | edit source]
Glycosyltransferases are valuable tools in biotechnology and synthetic biology. They are used in the synthesis of complex carbohydrates and glycoconjugates, which have applications in vaccine development and drug delivery.
See Also[edit | edit source]
References[edit | edit source]
- Varki, A., et al. (2009). Essentials of Glycobiology. Cold Spring Harbor Laboratory Press.
- Moremen, K. W., Tiemeyer, M., & Nairn, A. V. (2012). Vertebrate protein glycosylation: diversity, synthesis and function. Nature Reviews Molecular Cell Biology, 13(7), 448-462.
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