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COX

prostaglandin-endoperoxide synthase
Identifiers
EC number 1.14.99.1
CAS number 9055-65-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
cyclooxygenase 1
PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX.png
Crystallographic structure of prostaglandin H2 synthase-1 complex with flurbiprofen.
Identifiers
Symbol PTGS1
Alt. symbols COX-1
Entrez 5742
HUGO 9604
OMIM 176805
PDB 1CQE
RefSeq NM_080591
UniProt P23219
Other data
EC number 1.14.99.1
Locus Chr. 9 q32-q33.3
cyclooxygenase 2
Cyclooxygenase-2.png
Cyclooxygenase-2 (Prostaglandin Synthase-2) in complex with a COX-2 selective inhibitor.
Identifiers
Symbol PTGS2
Alt. symbols COX-2
Entrez 5743
HUGO 9605
OMIM 600262
PDB 6COX
RefSeq NM_000963
UniProt P35354
Other data
EC number 1.14.99.1
Locus Chr. 1 q25.2-25.3

Cyclooxygenase (COX), officially known as prostaglandin-endoperoxide synthase (PTGS), is an enzyme (specifically, a family of isozymes, EC 1.14.99.1) that is responsible for formation of prostanoids, including thromboxane and prostaglandins such as prostacyclin.

Pharmaceutical inhibition of COX can provide relief from the symptoms of inflammation and pain. Nonsteroidal anti-inflammatory drugs (NSAIDs), such as aspirin and ibuprofen, exert their effects through inhibition of COX. Those that are specific to the COX-2 isozyme are called COX-2 inhibitors.

In medicine, the root symbol "COX" is encountered more often than "PTGS". In genetics, "PTGS" is officially used for this family of genes and proteins, because the root symbol "COX" was already used for the family. Thus the two isozymes found in humans, PTGS1 and PTGS2, are frequently called COX-1 and COX-2 in the medical literature. The names "prostaglandin synthase (PHS)", "prostaglandin synthetase (PHS)", and "prostaglandin-endoperoxide synthetase (PES)" are older terms still sometimes used to refer to COX.

In terms of their molecular biology, COX-1 and COX-2 are of similar molecular weight, approximately 70 and 72 kDa, respectively, and having 65% amino acid sequence homology and near-identical catalytic sites. The most significant difference between the isoenzymes, which allows for selective inhibition, is the substitution of isoleucine at position 523 in COX-1 with valine in COX-2. The smaller Val523 residue in COX-2 allows access to a hydrophobic side-pocket in the enzyme (which Ile523 sterically hinders). Drug molecules, such as DuP-697 and the coxibs derived from it, bind to this alternative site and are considered to be selective inhibitors of COX-2.


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Wikipedia

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