Exopeptidase
Exopeptidase
Exopeptidases are a type of enzyme that catalyze the cleavage of amino acids from the ends of polypeptide chains. These enzymes play a crucial role in the process of protein degradation and protein metabolism by breaking down proteins into their constituent amino acids. Exopeptidases are classified based on the position at which they cleave the peptide bond: they can be either aminopeptidases or carboxypeptidases.
Types of Exopeptidases[edit | edit source]
Exopeptidases are broadly categorized into two main types:
- Aminopeptidases: These enzymes remove amino acids from the N-terminus (the end of the polypeptide chain that has a free amino group). Examples include leucine aminopeptidase and alanine aminopeptidase.
- Carboxypeptidases: These enzymes cleave amino acids from the C-terminus (the end of the polypeptide chain that has a free carboxyl group). Examples include carboxypeptidase A and carboxypeptidase B.
Function[edit | edit source]
Exopeptidases are essential for various biological processes, including:
- Protein digestion: They help in the breakdown of dietary proteins into absorbable amino acids.
- Cellular protein turnover: They are involved in the degradation of misfolded or damaged proteins within cells.
- Regulation of biological activity: By processing precursor proteins into their active forms, exopeptidases regulate the activity of various hormones and neuropeptides.
Mechanism of Action[edit | edit source]
Exopeptidases function by hydrolyzing the peptide bonds at the terminal ends of polypeptides. The specific mechanism can vary depending on the type of exopeptidase:
- Aminopeptidases typically use a zinc ion in their active site to facilitate the hydrolysis of the peptide bond.
- Carboxypeptidases often rely on a metal ion such as zinc or manganese to assist in the catalytic process.
Clinical Significance[edit | edit source]
Exopeptidases have significant clinical implications. Abnormal activity of these enzymes can be associated with various diseases, including:
- Cancer: Altered exopeptidase activity can affect tumor growth and metastasis.
- Neurological disorders: Dysregulation of exopeptidases can impact the processing of neuropeptides, contributing to conditions like Alzheimer's disease.
- Metabolic disorders: Deficiencies in specific exopeptidases can lead to metabolic imbalances and related diseases.
Related Pages[edit | edit source]
References[edit | edit source]
External Links[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