5.3.99.4: prostaglandin-I synthase
This is an abbreviated version!
For detailed information about prostaglandin-I synthase, go to the full flat file.
Word Map on EC 5.3.99.4
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5.3.99.4
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thromboxane
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cyclooxygenase
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endothelial
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arachidonic
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artery
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platelet
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cox-2
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vasodilator
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hypertension
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prostanoids
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endoperoxide
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eicosanoids
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pulmonary
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vessel
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indomethacin
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aorta
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6-keto-pgf1
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tranylcypromine
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peroxynitrite
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vasoconstriction
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endothelium-dependent
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6-keto-prostaglandin
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6-keto-pgf1alpha
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phosphoglucose
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iloprost
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tx
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mpges-1
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medicine
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6-keto
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antithrombotic
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5-lipoxygenase
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dazoxiben
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heme-thiolate
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ptges
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f1alpha
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synthase-1
-
beraprost
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15-hpete
- 5.3.99.4
-
thromboxane
-
cyclooxygenase
- endothelial
-
arachidonic
- artery
- platelet
- cox-2
-
vasodilator
- hypertension
-
prostanoids
-
endoperoxide
-
eicosanoids
- pulmonary
- vessel
- indomethacin
- aorta
-
6-keto-pgf1
- tranylcypromine
- peroxynitrite
-
vasoconstriction
-
endothelium-dependent
-
6-keto-prostaglandin
-
6-keto-pgf1alpha
-
phosphoglucose
-
iloprost
- tx
- mpges-1
- medicine
-
6-keto
-
antithrombotic
-
5-lipoxygenase
- dazoxiben
-
heme-thiolate
- ptges
- f1alpha
- synthase-1
-
beraprost
- 15-hpete
Reaction
Synonyms
Aortic cytochrom P450, CYP8A1, PGI synthase, PGI2 synthase, PGI2 synthetase, PGI2-S, PGIS, prostacyclin synthase, Prostacyclin synthetase, prostacyclin-synthase, prostacyclin/PGI2 synthase, Prostacycline synthetase, prostaglandin I synthase, Prostaglandin I2 synthase, Prostaglandin I2 synthetase, Ptgis, Synthetase, prostacyclin
ECTree
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Cofactor
Cofactor on EC 5.3.99.4 - prostaglandin-I synthase
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heme
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heme conformation and heme protein matrix interactions for human and zebrafish enzymes in the presence and absence of ligands, overview. The heme group is in the ferric, six-coordinate, low-spin state for both resting and ligand-bound enzymes of boh species. Drastically different RR shifts with heme conformational changes in both hPGIS and zPGIS upon different ligand bindings, suggesting that PGIS exhibits a ligand-specific heme conformational change to accommodate the substrate binding
heme
-
heme conformation and heme protein matrix interactions for human and zebrafish enzymes in the presence and absence of ligands, overview. The heme group is in the ferric, six-coordinate, low-spin state for both resting and ligand-bound enzymes of boh species. Drastically different RR shifts with heme conformational changes in both hPGIS and zPGIS upon different ligand bindings, suggesting that PGIS exhibits a ligand-specific heme conformational change to accommodate the substrate binding