EC Number |
Inhibitors |
Structure |
---|
1.14.99.1 | 1,10-phenanthroline |
weak |
|
1.14.99.1 | 1-Mercapto-9,11,15-trihydroxyprosta-5,13-diene |
inhibition of prostaglandin G1 synthesis |
|
1.14.99.1 | 1-Mercapto-9-oxo-11,15-dihydroxyprosta-5,13-dione |
inhibition of prostaglandin G1 synthesis |
|
1.14.99.1 | 12-nitroarachidonic acid |
nitro-fatty acid inhibition is due to a slow, tightly binding mechanism, it inhibits oxygenase and peroxidase activity PGHS-1, kinetics, overview. Inactivation of PGHS by nitroarachidonic acid involves two sequential steps: an initial reversible binding event, followed by a practically irreversible event leading to an inactivated enzyme. Inactivation is associated with irreversible disruption of heme binding to the protein, the inhibitor induces heme release from Fe2+-protoporphyrin-PGHS-1. In activated human platelets, nitroarachidonic acid significantly decreases PGHS-1-dependent thromboxane B2 formation in parallel with a decrease in platelet aggregation |
|
1.14.99.1 | 14-nitroarachidonic acid |
nitro-fatty acid inhibition is due to a slow, tightly binding mechanism, it inhibits oxygenase and peroxidase activity PGHS-1, kinetics, overview. Inactivation of PGHS by nitroarachidonic acid involves two sequential steps: an initial reversible binding event, followed by a practically irreversible event leading to an inactivated enzyme. Inactivation is associated with irreversible disruption of heme binding to the protein, the inhibitor induces heme release from Fe2+-protoporphyrin-PGHS-1. In activated human platelets, nitroarachidonic acid significantly decreases PGHS-1-dependent thromboxane B2 formation in parallel with a decrease in platelet aggregation |
|
1.14.99.1 | 15-nitroarachidonic acid |
nitro-fatty acid inhibition is due to a slow, tightly binding mechanism, it inhibits oxygenase and peroxidase activity PGHS-1, kinetics, overview. Inactivation of PGHS by nitroarachidonic acid involves two sequential steps: an initial reversible binding event, followed by a practically irreversible event leading to an inactivated enzyme. Inactivation is associated with irreversible disruption of heme binding to the protein, the inhibitor induces heme release from Fe2+-protoporphyrin-PGHS-1. In activated human platelets, nitroarachidonic acid significantly decreases PGHS-1-dependent thromboxane B2 formation in parallel with a decrease in platelet aggregation |
|
1.14.99.1 | 2,2'-bipyridyl |
weak |
|
1.14.99.1 | 2,3-Dimercaptopropanol |
inhibition of prostaglandin G1 synthesis |
|
1.14.99.1 | 2-hydroxybutyric acid |
weak |
|
1.14.99.1 | 3,6-bis(3-[[(furan-2-yl)methyl]amino]propyl)-9H-xanthen-9-one |
- |
|