Catalase
Catalase is an enzyme that plays a crucial role in the protection of the cellular organelles from oxidative damage by reactive oxygen species (ROS). It catalyzes the decomposition of hydrogen peroxide to water and oxygen, a critical reaction in the cells of nearly all living organisms exposed to oxygen. This enzyme is present in the peroxisomes of cells, which are involved in the metabolism of fatty acids and the detoxification of hydrogen peroxide.
Function
Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second. Hydrogen peroxide is a harmful by-product of many normal metabolic processes: to prevent damage, it must be quickly converted into other, less dangerous substances. By efficiently removing hydrogen peroxide, catalase allows cellular metabolic processes to proceed with minimal oxidative damage.
Structure
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four iron-containing heme groups that allow the enzyme to react with the hydrogen peroxide. The structure of catalase is highly conserved across different species, indicating its essential role in life.
Biological Role
Beyond its fundamental role in detoxifying hydrogen peroxide, catalase also has various other biological functions. It is involved in the signaling pathways related to the oxidative stress response and is implicated in some plant defense mechanisms. In humans and other animals, catalase deficiency can lead to a variety of health issues, including the rare genetic disorder acatalasemia, which involves the complete absence of catalase activity.
Clinical Significance
In medicine, catalase activity is a diagnostic marker for certain diseases and conditions. For example, a lack of catalase can lead to an accumulation of hydrogen peroxide in the body, causing damage to tissues and contributing to the development of diabetes, atherosclerosis, and other diseases. Additionally, the study of catalase has implications for cancer research, as cancer cells often exhibit altered catalase activity.
Applications
Catalase has industrial applications, including its use in the textile industry to remove hydrogen peroxide from fabrics after bleaching and in the food industry to prevent the oxidation of food. In scientific research, catalase activity is a common assay for the presence of blood and the quantification of bacterial load.
See Also
Transform your life with W8MD's budget GLP-1 injections from $125.
W8MD offers a medical weight loss program to lose weight in Philadelphia. Our physician-supervised medical weight loss provides:
- Most insurances accepted or discounted self-pay rates. We will obtain insurance prior authorizations if needed.
- Generic GLP1 weight loss injections from $125 for the starting dose.
- Also offer prescription weight loss medications including Phentermine, Qsymia, Diethylpropion, Contrave etc.
NYC weight loss doctor appointments
Start your NYC weight loss journey today at our NYC medical weight loss and Philadelphia medical weight loss clinics.
- Call 718-946-5500 to lose weight in NYC or for medical weight loss in Philadelphia 215-676-2334.
- Tags:NYC medical weight loss, Philadelphia lose weight Zepbound NYC, Budget GLP1 weight loss injections, Wegovy Philadelphia, Wegovy NYC, Philadelphia medical weight loss, Brookly weight loss and Wegovy NYC
|
WikiMD's Wellness Encyclopedia |
| Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
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