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Results 1 - 10 of 193 > >>
EC Number Inhibitors Commentary Structure
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.11,10-phenanthroline weak Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.11-Mercapto-9,11,15-trihydroxyprosta-5,13-diene inhibition of prostaglandin G1 synthesis Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.11-Mercapto-9-oxo-11,15-dihydroxyprosta-5,13-dione inhibition of prostaglandin G1 synthesis Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.112-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 Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.114-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 Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.115-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 Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.12,2'-bipyridyl weak Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.12,3-Dimercaptopropanol inhibition of prostaglandin G1 synthesis Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.12-hydroxybutyric acid weak Go to the Ligand Summary Page
Show all pathways known for 1.14.99.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.13,6-bis(3-[[(furan-2-yl)methyl]amino]propyl)-9H-xanthen-9-one - Go to the Ligand Summary Page
Results 1 - 10 of 193 > >>