IED ID | IndEnz0018001605 |
Enzyme Type ID | peroxidase001605 |
Protein Name |
Prostaglandin E synthase mPGES-1 EC 5.3.99.3 Glutathione peroxidase PTGES EC 1.11.1.- Glutathione transferase PTGES EC 2.5.1.18 Microsomal prostaglandin E synthase 1 |
Gene Name | Ptges Pges |
Organism | Mus musculus (Mouse) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MPSPGLVMESGQVLPAFLLCSTLLVIKMYAVAVITGQMRLRKKAFANPEDALKRGGLQYYRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPLIAWIHFLVVLTGRVVHTVAYLGKLNPRLRSGAYVLAQFSCFSMALQILWEVAHHL |
Enzyme Length | 153 |
Uniprot Accession Number | Q9JM51 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Activity is increased markedly in macrophages and osteoblasts following pro-inflammatory stimuli. {ECO:0000269|PubMed:11795891}. |
Binding Site | BINDING 39; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:O14684; BINDING 114; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:O14684; BINDING 118; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:O14684 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; Evidence={ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:11795891};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin E2; Xref=Rhea:RHEA:53324, ChEBI:CHEBI:85166, ChEBI:CHEBI:137172; Evidence={ECO:0000250|UniProtKB:O14684};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53325; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=prostaglandin G2 = (15S)-15-hydroperoxy-prostaglandin E2; Xref=Rhea:RHEA:64364, ChEBI:CHEBI:82629, ChEBI:CHEBI:152564; Evidence={ECO:0000250|UniProtKB:O14684};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64365; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:O14684}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:O14684}; |
DNA Binding | |
EC Number | 5.3.99.3; 1.11.1.-; 2.5.1.18 |
Enzyme Function | FUNCTION: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway (PubMed:10869354, PubMed:11795891). Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:11795891, PubMed:10869354). Plays a key role in inflammation response, fever and pain (PubMed:12835414, PubMed:14566340). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity). {ECO:0000250|UniProtKB:O14684, ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:11795891, ECO:0000269|PubMed:12835414, ECO:0000269|PubMed:14566340}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:11795891}; |
Pathway | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000269|PubMed:10869354}. |
nucleotide Binding | |
Features | Binding site (3); Chain (1); Region (2); Site (2); Topological domain (4); Transmembrane (4) |
Keywords | Cytoplasm;Fatty acid biosynthesis;Fatty acid metabolism;Isomerase;Lipid biosynthesis;Lipid metabolism;Membrane;Oxidoreductase;Prostaglandin biosynthesis;Prostaglandin metabolism;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
Interact With | |
Induction | INDUCTION: Induced by pro-inflammatory stimuli and down-regulated by anti-inflammatory glucocorticoid. {ECO:0000269|PubMed:10869354, ECO:0000269|PubMed:11795891}. |
Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11795891}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10725249; 11217851; 11704570; 12021206; 12023384; 12034740; 12080039; 12466851; 12604621; 12835322; 12842849; 14610273; 14681479; 15014433; 15016822; 15086459; 15140897; 15194860; 15677520; 15722356; 16000148; 16113047; 16204198; 16614756; 16627484; 16849500; 16864802; 16872525; 16873378; 16973753; 17023389; 17095726; 17277110; 17442791; 17535900; 17604949; 17628861; 17641732; 17967902; 18285567; 18347209; 18451151; 18485889; 18498757; 18523303; 18602702; 18614967; 18632796; 18799693; 18824665; 19018769; 19193887; 19225050; 19415240; 19524423; 19559811; 19561612; 19692487; 19845504; 19995978; 20028661; 20065147; 20128796; 20335314; 20452172; 20587000; 20622882; 20813913; 20844471; 20871624; 20943996; 21040902; 21070778; 21075851; 21190819; 21193590; 21219953; 21247731; 21266581; 21267068; 21282500; 21324324; 21497116; 21737615; 21784115; 21835766; 21880721; 21986945; 22081067; 22106404; 22137787; 22227567; 22237797; 22268508; 22302024; 22412193; 22430074; 22589381; 22766501; 22802632; 22822059; 22872578; 22926547; 22970288; 23171554; 23204105; 23624019; 23624557; 23913961; 23916744; 23943621; 24055573; 24085850; 24116971; 24127557; 24131900; 24147040; 24291175; 24668417; 24726877; 24753592; 24756129; 24984018; 25054560; 25634334; 25799228; 26001880; 26134597; 26407316; 26459051; 26475855; 26543101; 26585956; 26611322; 26690700; 26828067; 27059285; 27102561; 27174800; 27416888; 27440004; 27482714; 27784694; 27827823; 27913583; 28052039; 28341741; 28628921; 28879567; 29038248; 29237778; 29257087; 29282304; 29470537; 29581541; 29599139; 29678951; 29891646; 30127026; 30333759; 30382148; 30463256; 30619314; 30992314; 31015404; 31638830; 31688905; 31715374; 32060421; 32408168; 33285161; 33383181; 33582554; 33941650; 34555210; |
Motif | |
Gene Encoded By | |
Mass | 17,286 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37 uM for prostaglandin H2 {ECO:0000269|PubMed:11795891}; KM=130 uM for glutathione {ECO:0000269|PubMed:11795891}; |
Metal Binding | |
Rhea ID | RHEA:12893; RHEA:12894; RHEA:53324; RHEA:53325; RHEA:64364; RHEA:64365; RHEA:51220; RHEA:48620 |
Cross Reference Brenda | 5.3.99.3; |