Article
The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases.
The Journal of biological chemistry - 25 Mar 1990
DeWitt D L, el-Harith E A, Kraemer S A, Andrews M J, Yao E F, Armstrong R L, Smith W L
Abstract excerpt
Acetylation of Ser-530 of sheep prostaglandin endoperoxide (PGG/H) synthase by aspirin causes irreversible inactivation of the cyclooxygenase activity of the enzyme. To determine the catalytic function of the hydroxyl group of Ser-530, we used site-directed mutagenesis to replace Ser-530 with an alanine. Cos-1 cells transfected with expression vectors containing the native (Ser-530) or mutant (Ala-530) cDNAs for...
Topics
- Amino Acid Sequence
- Animals
- Aspirin
- Base Sequence
- Binding Sites
- Blotting, Western
- DNA
- Genetic Vectors
- Heme
- Mice
- Molecular Sequence Data