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cyclooxygenase-1 (COX1, PGH synthase-1, prostaglandin endoperoxide synthase-1, PTGS1)

Function: - role in regulating or promoting cell proliferation in some normal & neoplastically transformed cells - fatty acids biosynthesis; prostaglandin biosynthesis - acts both as a dioxygenase & as a peroxidase - production of prostaglandins for protection of gastric mucosal barrier & prostaglandins regulating renal blood flow - in platelets, COX1 produces thromboxane A [3] Cofactor: - binds 1 heme B (iron-protoporphyrin IX) group per subunit (putative) Structure: - homodimer - belongs to the prostaglandin G/H synthase family - contains 1 EGF-like domain Compartment: microsome membrane, peripheral membrane Alternative splicing: named isoforms=2 Expression: - constitutionally expressed in most tissues producing prostaglandin precursors for housekeeping functions Pharmacology: - target of nonsteroidal anti-inflammatory drugs (NSAIDs) - toxic effects of NSAIDs are largely due to inhibition of COX1

Related

non-steroidal anti-inflammatory agent (NSAID)

General

cyclooxygenase (prostaglandin endoperoxide synthase, COX) glycoprotein

Properties

SIZE: entity length = 599 aa MW = 69 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-23} EGF domain {31-69} MOTIF: cysteine residue {C35} MODIFICATION: cysteine residue {C46} cysteine residue {C36} MODIFICATION: cysteine residue {C158} cysteine residue {C40} MODIFICATION: cysteine residue {C56} cysteine residue {C46} MODIFICATION: cysteine residue {C35} cysteine residue {C56} MODIFICATION: cysteine residue {C40} cysteine residue {C58} MODIFICATION: cysteine residue {C68} N-glycosylation site {N67} cysteine residue {C68} MODIFICATION: cysteine residue {C58} N-glycosylation site {N103} N-glycosylation site {N143} cysteine residue {C158} MODIFICATION: cysteine residue {C36} histidine residue {H206} tyrosine residue {Y384} Iron [Fe]-binding site SITE: 387-387 serine residue {529-529} cysteine residue {C568} MODIFICATION: cysteine residue {C574} cysteine residue {C574} MODIFICATION: cysteine residue {C568}

Database Correlations

OMIM 176805 UniProt P23219 PFAM correlations ENZYME 1.14.99.1

References

  1. UniProt :accession P23219
  2. Mayo Internal Medicine Board Review, 1998-99, Prakash UBS (ed) Lippincott-Raven, Philadelphia, 1998, pg 14, 851-53
  3. Journal Watch 22(10):78, 2002 Cheng Y et al, Science 296:539, 2002 Vane JR, Science 296:474, 2002