Abstract
Prostaglandin H2 synthase (PGHS; EC 1.14.99.1; cyclooxygenase or COX) catalyses the two-step conversion of arachidonic acid to prostaglandin G2 and thence to prostaglandin H2, the first committed steps in the biosynthesis of prostaglandins1,2. While COX catalyses both steps of this catalytic process (known as the cyclooxygenase and peroxidase steps, respectively), the reactions are carried out in two spatially distinct active sites2. At least two isoforms of the enzyme, COX-1 and COX-2, are expressed in mammalian tissues1,3. The COX activity is specifically inhibited by the class of compounds known as non-steroid anti-inflammatory drugs (NSAIDs), which includes the commercially and pharmacologically important agents aspirin, ibuprofen, naproxen and indomethacin4. NSAIDs have been the common way to treat certain symptoms of inflammatory5 and cardiovascular diseases6. Moreover, a role for aspirin as an anticancer prophylaxis is now quite established7−9 although the precise molecular basis for this effect is still unclear.
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Garavito, R.M. (1996). The three-dimensional structure of cyclooxygenases. In: Vane, J., Botting, J., Botting, R. (eds) Improved Non-Steroid Anti-Inflammatory Drugs: COX-2 Enzyme Inhibitors. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-9029-2_2
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DOI: https://doi.org/10.1007/978-94-010-9029-2_2
Publisher Name: Springer, Dordrecht
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