COX-1
Enzyme found in many tissues of the body
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| Identifiers | |
|---|---|
| EC number | 1.14.99.1 |
| CAS number | 9035-69-2 |
| Alt. names | |
| IntEnz | IntEnz view |
| BRENDA | BRENDA entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
Cyclooxygenase-1 (COX-1) is an enzyme that is encoded by the PTGS1 gene in humans. It is one of the two isoenzymes of cyclooxygenase, the other being COX-2. COX-1 is a key enzyme in the biosynthesis of prostaglandins, which are involved in various physiological processes such as inflammation, pain, and fever.
Function[edit | edit source]
COX-1 is constitutively expressed in most tissues and is involved in the regulation of normal cellular processes. It plays a crucial role in the maintenance of the gastric mucosa, renal blood flow, and platelet function. The enzyme catalyzes the conversion of arachidonic acid to prostaglandin H2 (PGH2), which is a precursor for other prostaglandins and thromboxanes.
Structure[edit | edit source]
COX-1 is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit has a heme group that is essential for its enzymatic activity. The enzyme has a hydrophobic channel that allows the substrate, arachidonic acid, to access the active site.
Inhibition[edit | edit source]
COX-1 can be inhibited by nonsteroidal anti-inflammatory drugs (NSAIDs) such as aspirin and ibuprofen. These drugs reduce the production of prostaglandins, thereby alleviating pain and inflammation. However, inhibition of COX-1 can also lead to side effects such as gastric ulcers and renal impairment due to its role in protecting the gastric lining and maintaining renal function.
Clinical Significance[edit | edit source]
The inhibition of COX-1 is associated with various therapeutic and adverse effects. For instance, low-dose aspirin is commonly used for its antiplatelet effects to prevent cardiovascular diseases such as myocardial infarction and stroke. However, chronic use of NSAIDs can lead to gastrointestinal complications due to the inhibition of COX-1.
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References[edit | edit source]
External Links[edit | edit source]
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Contributors: Prab R. Tumpati, MD
