Article
Crystal structure of arachidonic acid bound to a mutant of prostaglandin endoperoxide H synthase-1 that forms predominantly 11-hydroperoxyeicosatetraenoic acid.
The Journal of biological chemistry - 8 Oct 2004
Harman Christine A, Rieke Caroline Jill, Garavito R Michael, Smith William L
Abstract excerpt
Kinetic studies and analysis of the products formed by native and mutant forms of ovine prostaglandin endoperoxide H synthase-1 (oPGHS-1) have suggested that arachidonic acid (AA) can exist in the cyclooxygenase active site of the enzyme in three different, catalytically competent conformations that lead to prostaglandin G2 (PGG2), 11R-hydroperoxyeicosatetraenoic acid (HPETE), and 15R,S-HPETE, respectively. We...
Topics
- Animals
- Arachidonic Acid
- Arachidonic Acids
- Binding Sites
- Carbon
- Catalysis
- Cell Line
- Chromatography, Thin Layer
- Cobalt
- Crystallography, X-Ray
- Cyclooxygenase 1