EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
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 | Homo sapiens | |
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 | Homo sapiens | |
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 | Homo sapiens | |
1.14.99.1 | 9-nitroarachidonic acid | nitro-fatty acid inhibition is due to a slow, tightly binding mechanism, it inhibits oxygenase activity and peroxidase activity of 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 | Homo sapiens | |
1.14.99.1 | additional information | no inhibition of PGHS-2 oxygenase activity by 9-nitro-, 12-nitro-, 14-nitro, and 15-nitroarachidonic acid and by nitrooleic acid and nitrolinoleic acid; other nitro fatty acids tested, such as nitrooleic acid and nitrolinoleic acid, are unable to inhibit the enzyme activity | Homo sapiens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.1 | Iron | each subunit contains a molecule of Fe3+-protoporphyrin IX noncovalently attached to the enzyme, the heme group is essential for both enzyme activities, the cofactor is released by induction of inhibitor nitroarachidonic acid | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.99.1 | arachidonate + AH2 + 2 O2 | Homo sapiens | - |
prostaglandin H2 + A + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.99.1 | Homo sapiens | P23219 | isozyme PGHS-1 | - |
1.14.99.1 | Homo sapiens | P35354 | isozyme PGHS-2 | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.99.1 | blood platelet | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.99.1 | arachidonate + AH2 + 2 O2 | - |
Homo sapiens | prostaglandin H2 + A + H2O | - |
? | |
1.14.99.1 | arachidonate + reduced N,N,N',N'-tetramethylphenylenediamine + 2 O2 | - |
Homo sapiens | prostaglandin H2 + oxidized N,N,N',N'-tetramethylphenylenediamine + H2O | - |
? | |
1.14.99.1 | additional information | PGHS-1 also exhibits peroxidase activity | Homo sapiens | ? | - |
? | |
1.14.99.1 | additional information | PGHS-2 also exhibits peroxidase activity | Homo sapiens | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.99.1 | homodimer | PGHS-1 is a homodimer of 70 kDa whose dimerization is required for structural integrity and catalytic activity | Homo sapiens |
1.14.99.1 | homodimer | PGHS-2 is a homodimer of 70 kDa whose dimerization is required for structural integrity and catalytic activity | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.99.1 | COX | - |
Homo sapiens |
1.14.99.1 | PGHS | - |
Homo sapiens |
1.14.99.1 | prostaglandin endoperoxide H synthase | - |
Homo sapiens |
1.14.99.1 | prostaglandin endoperoxide H synthase 1 | - |
Homo sapiens |
1.14.99.1 | prostaglandin endoperoxide H synthase 2 | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.99.1 | 37 | - |
prostaglandin endoperoxide H synthase assay at | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.99.1 | 7.4 | - |
prostaglandin endoperoxide H synthase assay at | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.1 | iron-protoporphyrin IX | each subunit contains a molecule of Fe3+-protoporphyrin IX noncovalently attached to the enzyme, the heme group is essential for both enzyme activities | Homo sapiens |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.99.1 | additional information | - |
additional information | inhibition kinetics of the isozymes' peroxidase activity, overview | Homo sapiens |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.99.1 | malfunction | PGHS-1 inhibition in activated human plateletts significantly decreases PGHS-1-dependent thromboxane B2 formation in parallel with a decrease in platelet aggregation | Homo sapiens |