Detail Information for IndEnz0018001605
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;