EC Number   |
General Information |
Reference  |
|---|
    1.14.99.1 | physiological function |
periovulatory expression of the Ptgs2 gene is essential for ovulation |
697636 |
| 1.14.99.1 | more |
aqueous extracts of Chromoleana odorata, commonly used in traditional medicine as antiinflammatory drug against pains or as cataplasm to stop hemorrhage in Ivory Coast, the essential oil extracted from the fresh leaves activates the cyclooxygenase activity of the PGHS, overview |
713706 |
| 1.14.99.1 | physiological function |
PGHS is involved in inflammation processes |
713706 |
| 1.14.99.1 | metabolism |
the enzyme catalyzes the committed step in prostaglandin biosynthesis |
714124 |
| 1.14.99.1 | more |
PHS is involved in the mechanism of thalidomide to cause increased embryonic DNA oxidation measured as 8-oxoguanine leading to embryopathies, phenotype, overview. A prostaglandin H synthase-dependent, reactive oxygen species-mediated mechanism. Thalidomide teratogenicity was blocked by maternal pretreatment with acetylsalicylic acid, an irreversible inhibitor of prostaglandin H synthase |
714943 |
| 1.14.99.1 | physiological function |
PHS isozyme-dependent oxidative damage to proteins and DNA, and cytotoxicity, overview. hPHS-1- and hPHS-2-expressing cells incubated with dopamine, L-dihydroxyphenylalanine, dihydroxyphenylacetic acid, or homovanillic acid exhibit increased cytotoxicity compared to untransfected cells, and cytotoxicity is increased further by exogenous arachidonic acid, which increases hPHS activity. Isozyme-specific, PHS-dependent oxidative damage and cytotoxicity caused by neurotransmitters, their precursors, and their metabolites may contribute to neurodegeneration associated with aging |
715090 |
| 1.14.99.1 | physiological function |
PGHS-2 also shows cyclooxygenase activity, which is implicated in colorectal cancer |
716434 |
| 1.14.99.1 | more |
neurotoxicity of the amphetamine analogues methamphetamine and 3,4-methylenedioxyamphetamine, the active metabolite of ecstasy, may involve their prostaglandin H synthase-dependent bioactivation to free radical intermediates that generate reactive oxygen species and oxidatively damage cellular macromolecules. The activation effect is blocked by irreversible enzyme inhibitor acetylsalicylic acid, overview |
716959 |
| 1.14.99.1 | evolution |
the algal PGHS lacks structural elements identified in all known animal PGHSs, such as epidermal growth factor-like domain and helix B in the membrane binding domain. The key residues of animal PGHS, like catalytic Tyr385 and heme liganding His388 are conserved in the algal enzyme, but the amino acid residues shown to be important for substrate binding and coordination, and the target residues for nonsteroidal anti-inflammatory drugs, Arg120, Tyr355, and Ser530, are not found at the appropriate positions in the algal sequences. The preferred substrate for the algal PGHS is arachidonic acid with cyclooxygenase reaction rate remarkably higher than values reported for mammalian PGHS isoforms |
727083 |
| 1.14.99.1 | more |
seminal plasma-induced PTGS2 expression is mediated by intracellular signaling pathways involving MAPKs and NF-kappaB. Depending on cell type and stimulus, different intracellular signaling pathways are involved in inflammation and PTGS2 expression |
727121 |
