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Protein

Prostaglandin G/H synthase 2

Gene

Ptgs2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis.5 Publications

Catalytic activityi

Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O.4 Publications

Cofactori

heme b3 PublicationsNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.3 Publications

Enzyme regulationi

Inhibited by the nonsteroidal anti-inflammatory drugs aspirin, naproxen, diclofenac, meclofenamic acid, indomethacin and their analogs.2 Publications

Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei106Substrate1
Active sitei193Proton acceptorPROSITE-ProRule annotation1 Publication1
Binding sitei341Substrate1
Active sitei371For cyclooxygenase activity1 Publication1
Binding sitei371Substrate1
Metal bindingi374Iron (heme axial ligand)1
Sitei516Aspirin-acetylated serine1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.1. 3474.
ReactomeiR-MMU-197264. Nicotinamide salvaging.
R-MMU-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
UniPathwayiUPA00662.

Protein family/group databases

PeroxiBasei3360. MmPGHS02.

Chemistry databases

SwissLipidsiSLP:000001129.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin G/H synthase 2 (EC:1.14.99.1)
Alternative name(s):
Cyclooxygenase-2
Short name:
COX-2
Glucocorticoid-regulated inflammatory cyclooxygenase
Gripghs
Macrophage activation-associated marker protein P71/73
PES-2
PHS II
Prostaglandin H2 synthase 2
Short name:
PGH synthase 2
Short name:
PGHS-2
Prostaglandin-endoperoxide synthase 2
TIS10 protein
Gene namesi
Name:Ptgs2
Synonyms:Cox-2, Cox2, Pghs-b, Tis10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97798. Ptgs2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: Ensembl
  • cytoplasm Source: MGI
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • neuron projection Source: MGI
  • organelle membrane Source: UniProtKB-SubCell
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Disruption phenotypei

Mutant mice exhibit defects in colonic mucosal wound repair.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi517L → A, F, P or T: Slightly reduced activity. 1 Publication1
Mutagenesisi580N → A: Loss of glycosylation site. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Add BLAST17
ChainiPRO_000002387618 – 604Prostaglandin G/H synthase 2Add BLAST587

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi21 ↔ 32
Disulfide bondi22 ↔ 145
Disulfide bondi26 ↔ 42
Disulfide bondi44 ↔ 54
GlycosylationiCAR_00022253N-linked (GlcNAc...)7 Publications1
GlycosylationiCAR_000223130N-linked (GlcNAc...)7 Publications1
GlycosylationiCAR_000224396N-linked (GlcNAc...)7 Publications1
Disulfide bondi555 ↔ 561
GlycosylationiCAR_000225580N-linked (GlcNAc...)2 Publications1

Post-translational modificationi

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei592Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein, S-nitrosylation

Proteomic databases

PaxDbiQ05769.
PeptideAtlasiQ05769.
PRIDEiQ05769.

PTM databases

iPTMnetiQ05769.
PhosphoSitePlusiQ05769.
UniCarbKBiQ05769.

Expressioni

Tissue specificityi

Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level).1 Publication

Developmental stagei

During colonic wound repair, highly up-regulated (more than 1600-fold) in the mesenchyme of the wound bed 2 days after injury as compared to uninjured mucosa. Further increase in expression is observed at day 4 following injury (close to 2200-fold). Down-regulated at day 6 (only 93-fold increase as compared to uninjured mucosa).1 Publication

Inductioni

By cytokines and mitogens.

Gene expression databases

BgeeiENSMUSG00000032487.
CleanExiMM_PTGS2.
ExpressionAtlasiQ05769. baseline and differential.
GenevisibleiQ05769. MM.

Interactioni

Subunit structurei

Homodimer.5 Publications

GO - Molecular functioni

  • enzyme binding Source: MGI
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi202463. 5 interactors.
DIPiDIP-31082N.
IntActiQ05769. 1 interactor.
STRINGi10090.ENSMUSP00000035065.

Chemistry databases

BindingDBiQ05769.

Structurei

Secondary structure

1604
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 23Combined sources4
Helixi27 – 29Combined sources3
Beta strandi31 – 36Combined sources6
Beta strandi39 – 43Combined sources5
Beta strandi47 – 50Combined sources4
Turni51 – 54Combined sources4
Helixi59 – 67Combined sources9
Helixi71 – 78Combined sources8
Helixi82 – 89Combined sources8
Helixi92 – 107Combined sources16
Beta strandi116 – 119Combined sources4
Beta strandi120 – 122Combined sources3
Helixi125 – 129Combined sources5
Beta strandi131 – 133Combined sources3
Beta strandi135 – 138Combined sources4
Beta strandi145 – 147Combined sources3
Beta strandi150 – 153Combined sources4
Helixi160 – 167Combined sources8
Helixi182 – 192Combined sources11
Turni193 – 195Combined sources3
Turni200 – 202Combined sources3
Beta strandi206 – 208Combined sources3
Beta strandi213 – 215Combined sources3
Helixi217 – 220Combined sources4
Helixi224 – 230Combined sources7
Beta strandi241 – 243Combined sources3
Beta strandi246 – 248Combined sources3
Helixi252 – 255Combined sources4
Beta strandi263 – 265Combined sources3
Helixi267 – 269Combined sources3
Turni276 – 279Combined sources4
Helixi282 – 305Combined sources24
Helixi311 – 332Combined sources22
Helixi334 – 339Combined sources6
Helixi349 – 352Combined sources4
Helixi365 – 370Combined sources6
Helixi374 – 376Combined sources3
Beta strandi379 – 383Combined sources5
Beta strandi386 – 388Combined sources3
Helixi390 – 393Combined sources4
Helixi398 – 414Combined sources17
Beta strandi420 – 424Combined sources5
Helixi428 – 430Combined sources3
Helixi431 – 443Combined sources13
Helixi449 – 455Combined sources7
Helixi464 – 468Combined sources5
Beta strandi469 – 471Combined sources3
Helixi472 – 481Combined sources10
Helixi484 – 486Combined sources3
Helixi489 – 495Combined sources7
Beta strandi503 – 505Combined sources3
Helixi506 – 521Combined sources16
Helixi524 – 526Combined sources3
Turni528 – 530Combined sources3
Helixi533 – 536Combined sources4
Helixi539 – 546Combined sources8
Helixi550 – 557Combined sources8
Beta strandi558 – 560Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CVUX-ray2.40A/B18-569[»]
1CX2X-ray3.00A/B/C/D18-604[»]
1DCXmodel-A/B18-569[»]
1DD0model-A/B18-569[»]
1DDXX-ray3.00A/B/C/D18-569[»]
1PXXX-ray2.90A/B/C/D1-604[»]
3HS5X-ray2.10A/B20-604[»]
3HS6X-ray2.40A/B20-604[»]
3HS7X-ray2.65A/B20-604[»]
3KRKX-ray2.40A/B20-604[»]
3LN0X-ray2.20A/B/C/D18-604[»]
3LN1X-ray2.40A/B/C/D18-604[»]
3MDLX-ray2.20A/B20-599[»]
3MQEX-ray2.80A/B/C/D18-604[»]
3NT1X-ray1.73A/B18-604[»]
3NTBX-ray2.27A/B/C/D18-604[»]
3NTGX-ray2.19A/B/C/D18-569[»]
3OLTX-ray2.45A/B20-604[»]
3OLUX-ray2.35A/B20-604[»]
3PGHX-ray2.50A/B/C/D18-604[»]
3Q7DX-ray2.40A/B18-604[»]
3QH0X-ray2.10A/B1-604[»]
3QMOX-ray3.00A/B1-604[»]
3RR3X-ray2.84A/B/C/D18-577[»]
3TZIX-ray2.15A/B20-604[»]
4COXX-ray2.90A/B/C/D18-604[»]
4E1GX-ray2.10A/B1-604[»]
4FM5X-ray2.81A/B/C/D1-604[»]
4M10X-ray2.01A/B/C/D18-604[»]
4M11X-ray2.45A/B/C/D18-569[»]
4OTJX-ray2.11A/B/C/D18-604[»]
4OTYX-ray2.35A/B18-604[»]
4PH9X-ray1.81A/B20-568[»]
4RRWX-ray2.57A/B/C/D18-604[»]
4RRXX-ray2.78A/B18-604[»]
4RRYX-ray2.43A/B/C/D18-604[»]
4RRZX-ray2.57A/B/C/D18-604[»]
4RS0X-ray2.81A18-604[»]
4RUTX-ray2.16A/B/C/D18-604[»]
4Z0LX-ray2.29A/B/C/D18-604[»]
5COXX-ray3.00A/B/C/D18-604[»]
5FDQX-ray1.90A/B20-604[»]
6COXX-ray2.80A/B18-604[»]
ProteinModelPortaliQ05769.
SMRiQ05769.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 55EGF-likePROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the prostaglandin G/H synthase family.Curated
Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00390000010743.
HOGENOMiHOG000013149.
HOVERGENiHBG000366.
InParanoidiQ05769.
KOiK11987.
OMAiCNNVKGC.
OrthoDBiEOG091G03CD.
PhylomeDBiQ05769.
TreeFamiTF329675.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029576. COX-2.
IPR000742. EGF-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF8. PTHR11903:SF8. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF00008. EGF. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY
60 70 80 90 100
GENCTTPEFL TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK
110 120 130 140 150
YVLTSRSYLI DSPPTYNVHY GYKSWEAFSN LSYYTRALPP VADDCPTPMG
160 170 180 190 200
VKGNKELPDS KEVLEKVLLR REFIPDPQGS NMMFAFFAQH FTHQFFKTDH
210 220 230 240 250
KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY QVIGGEVYPP
260 270 280 290 300
TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD
310 320 330 340 350
ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE
360 370 380 390 400
LLFNQQFQYQ NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL
410 420 430 440 450
LEHGLTQFVE SFTRQIAGRV AGGRNVPIAV QAVAKASIDQ SREMKYQSLN
460 470 480 490 500
EYRKRFSLKP YTSFEELTGE KEMAAELKAL YSDIDVMELY PALLVEKPRP
510 520 530 540 550
DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV GFKIINTASI
560 570 580 590 600
QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR

STEL
Length:604
Mass (Da):69,013
Last modified:June 1, 1994 - v1
Checksum:iDFE1658295C92064
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti98I → T in AAA39924 (PubMed:1712772).Curated1
Sequence conflicti142A → R in AAA39918 (PubMed:1419907).Curated1
Sequence conflicti301I → L no nucleotide entry (PubMed:1744122).Curated1
Sequence conflicti585H → R in AAA39918 (PubMed:1419907).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64291 mRNA. Translation: AAA39924.1.
M94967 mRNA. Translation: AAA39918.1.
M82866
, M82862, M82863, M82864, M82865 Genomic DNA. Translation: AAA40448.1.
M88242 mRNA. Translation: AAA37740.1.
AK049923 mRNA. Translation: BAC33986.1.
AK144956 mRNA. Translation: BAE26154.1.
AK166221 mRNA. Translation: BAE38639.1.
AK172161 mRNA. Translation: BAE42855.1.
CH466520 Genomic DNA. Translation: EDL39487.1.
CCDSiCCDS15353.1.
PIRiA49010.
RefSeqiNP_035328.2. NM_011198.4.
UniGeneiMm.292547.

Genome annotation databases

EnsembliENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
GeneIDi19225.
KEGGimmu:19225.
UCSCiuc007cxv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64291 mRNA. Translation: AAA39924.1.
M94967 mRNA. Translation: AAA39918.1.
M82866
, M82862, M82863, M82864, M82865 Genomic DNA. Translation: AAA40448.1.
M88242 mRNA. Translation: AAA37740.1.
AK049923 mRNA. Translation: BAC33986.1.
AK144956 mRNA. Translation: BAE26154.1.
AK166221 mRNA. Translation: BAE38639.1.
AK172161 mRNA. Translation: BAE42855.1.
CH466520 Genomic DNA. Translation: EDL39487.1.
CCDSiCCDS15353.1.
PIRiA49010.
RefSeqiNP_035328.2. NM_011198.4.
UniGeneiMm.292547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CVUX-ray2.40A/B18-569[»]
1CX2X-ray3.00A/B/C/D18-604[»]
1DCXmodel-A/B18-569[»]
1DD0model-A/B18-569[»]
1DDXX-ray3.00A/B/C/D18-569[»]
1PXXX-ray2.90A/B/C/D1-604[»]
3HS5X-ray2.10A/B20-604[»]
3HS6X-ray2.40A/B20-604[»]
3HS7X-ray2.65A/B20-604[»]
3KRKX-ray2.40A/B20-604[»]
3LN0X-ray2.20A/B/C/D18-604[»]
3LN1X-ray2.40A/B/C/D18-604[»]
3MDLX-ray2.20A/B20-599[»]
3MQEX-ray2.80A/B/C/D18-604[»]
3NT1X-ray1.73A/B18-604[»]
3NTBX-ray2.27A/B/C/D18-604[»]
3NTGX-ray2.19A/B/C/D18-569[»]
3OLTX-ray2.45A/B20-604[»]
3OLUX-ray2.35A/B20-604[»]
3PGHX-ray2.50A/B/C/D18-604[»]
3Q7DX-ray2.40A/B18-604[»]
3QH0X-ray2.10A/B1-604[»]
3QMOX-ray3.00A/B1-604[»]
3RR3X-ray2.84A/B/C/D18-577[»]
3TZIX-ray2.15A/B20-604[»]
4COXX-ray2.90A/B/C/D18-604[»]
4E1GX-ray2.10A/B1-604[»]
4FM5X-ray2.81A/B/C/D1-604[»]
4M10X-ray2.01A/B/C/D18-604[»]
4M11X-ray2.45A/B/C/D18-569[»]
4OTJX-ray2.11A/B/C/D18-604[»]
4OTYX-ray2.35A/B18-604[»]
4PH9X-ray1.81A/B20-568[»]
4RRWX-ray2.57A/B/C/D18-604[»]
4RRXX-ray2.78A/B18-604[»]
4RRYX-ray2.43A/B/C/D18-604[»]
4RRZX-ray2.57A/B/C/D18-604[»]
4RS0X-ray2.81A18-604[»]
4RUTX-ray2.16A/B/C/D18-604[»]
4Z0LX-ray2.29A/B/C/D18-604[»]
5COXX-ray3.00A/B/C/D18-604[»]
5FDQX-ray1.90A/B20-604[»]
6COXX-ray2.80A/B18-604[»]
ProteinModelPortaliQ05769.
SMRiQ05769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202463. 5 interactors.
DIPiDIP-31082N.
IntActiQ05769. 1 interactor.
STRINGi10090.ENSMUSP00000035065.

Chemistry databases

BindingDBiQ05769.
ChEMBLiCHEMBL4321.
SwissLipidsiSLP:000001129.

Protein family/group databases

PeroxiBasei3360. MmPGHS02.

PTM databases

iPTMnetiQ05769.
PhosphoSitePlusiQ05769.
UniCarbKBiQ05769.

Proteomic databases

PaxDbiQ05769.
PeptideAtlasiQ05769.
PRIDEiQ05769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
GeneIDi19225.
KEGGimmu:19225.
UCSCiuc007cxv.1. mouse.

Organism-specific databases

CTDi5743.
MGIiMGI:97798. Ptgs2.

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00390000010743.
HOGENOMiHOG000013149.
HOVERGENiHBG000366.
InParanoidiQ05769.
KOiK11987.
OMAiCNNVKGC.
OrthoDBiEOG091G03CD.
PhylomeDBiQ05769.
TreeFamiTF329675.

Enzyme and pathway databases

UniPathwayiUPA00662.
BRENDAi1.14.99.1. 3474.
ReactomeiR-MMU-197264. Nicotinamide salvaging.
R-MMU-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

EvolutionaryTraceiQ05769.
PROiQ05769.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032487.
CleanExiMM_PTGS2.
ExpressionAtlasiQ05769. baseline and differential.
GenevisibleiQ05769. MM.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029576. COX-2.
IPR000742. EGF-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF8. PTHR11903:SF8. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF00008. EGF. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGH2_MOUSE
AccessioniPrimary (citable) accession number: Q05769
Secondary accession number(s): Q543K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The conversion of arachidonate to prostaglandin H2 is a 2 step reaction: a cyclooxygenase (COX) reaction which converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase reaction occurs in a hydrophobic channel in the core of the enzyme. The peroxidase reaction occurs at a heme-containing active site located near the protein surface. The nonsteroidal anti-inflammatory drugs (NSAIDs) binding site corresponds to the cyclooxygenase active site.
Conversion of arachidonate to prostaglandin H2 is mediated by 2 different isozymes: the constitutive PTGS1 and the inducible PTGS2. PGHS1 is expressed constitutively and generally produces prostanoids acutely in response to hormonal stimuli to fine-tune physiological processes requiring instantaneous, continuous regulation (e.g. hemostasis). PGHS2 is inducible and typically produces prostanoids that mediate responses to physiological stresses such as infection and inflammation.
PTGS1 and PTGS2 are the targets of nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is able to produce an irreversible inactivation of the enzyme through a serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces inflammation, pain, and fever, and long-term use of these drugs reduces fatal thrombotic events, as well as the development of colon cancer and Alzheimer's disease. PTGS2 is the principal isozyme responsible for production of inflammatory prostaglandins. New generation PTGSs inhibitors strive to be selective for PTGS2, to avoid side effects such as gastrointestinal complications and ulceration.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.