Search results for PTGS1

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Protein (2 results from a total of 2)

Identifier: R-HSA-428931
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: PTGS1: P23219
Identifier: R-HSA-2314694
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: PTGS1: P23219

Complex (2 results from a total of 2)

Identifier: R-HSA-428986
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Identifier: R-HSA-2314695
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane

Reaction (5 results from a total of 5)

Identifier: R-HSA-140359
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen, endoplasmic reticulum membrane
Prostaglandin G/H synthase 1 (PTGS1) exhibits a dual catalytic activity, a cyclooxygenase and a peroxidase. The peroxidase function converts prostaglandin G2 (PGG2) to prostaglandin H2 (PGH2) via a two-electron reduction (Hamberg et al. 1973, Hla & Neilson 1992, Swinney et al. 1997, Barnett et al. 1994).
Identifier: R-HSA-2314678
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
Aspirin (acetylsalicylate) reacts spontaneously with one subunit of PTGS1 dimer to acetylate serine residue 516. The modified enzyme is no longer capable of catalyzing the conversion of arachidonic acid to PGH2. The identity of the acetylated residue is inferred from data for the humann PTGS2 enzyme (Lecomte et al. 1994) and the ovine PGHS1 enzyme (Loll et al. 1995).
Identifier: R-HSA-140355
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen, endoplasmic reticulum membrane
Prostaglandin G/H synthase PTGS1 exhibits a dual catalytic activity, a cyclooxygenase and a peroxidase. The cyclooxygenase function catalyzes the initial conversion of arachidonic acid to an intermediate, prostaglandin G2 (PGG2) (Hamberg et al. 1974, Nugteren 1973).
Identifier: R-HSA-2309779
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum membrane
While closely similar, PTGS1 and 2 differ sufficiently in the structures of their active sites so that the latter enzyme selectively binds and is inhibited by celecoxib (Luong et al. 1996; Smith et al. 2000; Dong et al. 2011).
Identifier: R-HSA-2161660
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
Prostaglandin E synthase (PTGES) requires glutathione (GSH) as an essential cofactor for its enzymatic activity, and together they isomerise prostaglandin H2 (PGH2) to prostaglandin E2 (PGE2) (Jegerschold et al. 2008). After PGH2 has been produced by the prostaglandin G/H synthases (PTGS1 and 2) on the lumenal side of the endoplasmic reticulum, it diffuses through the membrane to the active site of PTGES located on the cytoplasmic side.

Pathway (1 results from a total of 1)

Identifier: R-HSA-2162123
Species: Homo sapiens
The bioactive prostaglandin (PG) signalling molecules, including PGA2, PGE2, PGF2a, and PGI2 (prostacyclin) are synthesised from arachidonic acid and its products by various prostaglandin synthase type enzymes. Prostaglandin H2 (PGH2) is the starting point for the synthesis of Thromboxanes (TXs) (Buczynski et al. 2009, Vance & Vance 2008). PGs and TXs are collectively known as the prostanoids.
Two enzymes, PTGS1 and 2 (COX1 and 2) both catalyze the two-step conversion of arachidonic acid to PGH2. PTGS1 is constitutively expressed in many cell types while PTGS2 is induced in response to stress and mediates the syntheses of prostaglandins associated with pain, fever, and inflammation. Aspirin irreversibly inactivates both enzymes (though it acts more efficiently on PTGS1), explaining both its antiinflammatory effects and side effects like perturbed gastic acid secretion. Drugs like celecoxib, by specifically inhibiting PTGS2, have a strong anti-inflammatory effect with fewer side effects. These PTGS2-specific drugs, however, probably because of their effects on the balance of prostaglandin synthesis in platelets and endothelial cells, can also promote blood clot formation (Buczynski et al. 2009; Stables & Gilroy 2011).
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