Aspirin, acetaminophen, and ibuprofin all belong to a class of drugs called non-steriodal anti-inflammatory drugs (NSAIDs), which act on the cyclooxygenase portion of the enzyme prostaglandin synthase.  Two isoforms of cyclooxygenase exist, COX-1 and COX-2.   Both isoforms catalyze the reaction that convert arachadonic acid into a class of hormones called eicosinoids, including prostaglandins, prostacyclins, and thromboxanes.  COX-1 is constuitively in most mammalian tissues and is responsible for keeping the stomach lining intact and maintaining functional kidneys.  COX-1 appears to be the product of a 'housekeeping' gene responsible for homeostasis (1).  In contrast, COX-2 is only made under certain conditions and leads to the biosynthesis of prostaglandins triggering pain and inflammatory responses.  The NSAIDs currently in use bind with both forms of cyclooxygenase.  The results are drugs that relieve pain and reduce swelling, but eat away the stomach lining and damage the kidneys.  The demand for NSAIDs without the negative side effects associated with aspirin has prompted researchers to explore the differences between the two isoforms in an attempt to develop drugs with COX-2 specificity.  This site will provide information on the reactions catalyzed by cyclooxygenase and explore the structure and active site of the COX-1 portion of prostaglandin synthase.

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