Superoxide dismutase
Superoxide Dismutase
Superoxide dismutase (pronounced soo-per-ox-ide dis-mu-tase), often abbreviated as SOD, is an enzyme that plays a crucial role in protecting the body from harmful free radicals. The term "superoxide dismutase" is derived from the enzyme's function: "super" refers to its superior ability to neutralize harmful substances, "oxide" refers to the type of substances it targets, and "dismutase" refers to its ability to accelerate chemical reactions.
Function
Superoxide dismutase is responsible for catalyzing the dismutation of the superoxide (O2−) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). This process is critical for preventing damage to tissues and cells caused by free radicals.
Types
There are three types of superoxide dismutase in humans:
- SOD1: Also known as copper-zinc SOD, it is primarily found in the cytoplasm of cells.
- SOD2: Also known as manganese SOD, it is located in the mitochondria.
- SOD3: Also known as extracellular SOD, it is secreted into the extracellular space.
Clinical Significance
Mutations in the genes that produce superoxide dismutase have been linked to certain diseases. For example, mutations in the SOD1 gene are associated with Amyotrophic lateral sclerosis (ALS), a neurodegenerative disease.
Related Terms
- Antioxidant: A substance that inhibits oxidation, especially one used to counteract the deterioration of stored food products or remove potentially damaging oxidizing agents in a living organism.
- Oxidative stress: An imbalance between the production of free radicals and the ability of the body to counteract or detoxify their harmful effects through neutralization by antioxidants.
External links
- Medical encyclopedia article on Superoxide dismutase
- Wikipedia's article - Superoxide dismutase
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