| IED ID | IndEnz0018000741 |
| Enzyme Type ID | peroxidase000741 |
| Protein Name |
Hematopoietic prostaglandin D synthase H-PGDS EC 5.3.99.2 GST class-sigma Glutathione S-transferase EC 2.5.1.18 Glutathione-dependent PGD synthase Glutathione-requiring prostaglandin D synthase Prostaglandin-H2 D-isomerase |
| Gene Name | HPGDS GSTS PGDS PTGDS2 |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MPNYKLTYFNLRGRAEICRYLFAYAGIKYEDHRLEGADWPKIKPTIPFGKVPILEVDGVIIHQSLAIARYLARESGLAGQTPVEQALADAIVDTIDDFMMLFPWAEKNQDVKEKAFNDILTNKAPELLKDLDTFLGDKKWFVGKSVTWADFYWDVCSTTLLSYKADLADKYPRLLALRDRVEALPAIAAWIQKRPKTAI |
| Enzyme Length | 199 |
| Uniprot Accession Number | O73888 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 8; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:O60760; BINDING 14; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:O60760; BINDING 39; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:O60760 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:9657971};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:9657971}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin D2; Xref=Rhea:RHEA:51232, ChEBI:CHEBI:85166, ChEBI:CHEBI:133979; Evidence={ECO:0000250|UniProtKB:O60760};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233; Evidence={ECO:0000250|UniProtKB:O60760}; |
| DNA Binding | |
| EC Number | 5.3.99.2; 2.5.1.18 |
| Enzyme Function | FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides, organic isothiocyanates and alpha,beta-unsaturated carbonyls. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide and t-butyl hydroperoxide. {ECO:0000269|PubMed:9657971}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Domain (2); Initiator methionine (1); Region (2) |
| Keywords | Cytoplasm;Fatty acid biosynthesis;Fatty acid metabolism;Isomerase;Lipid biosynthesis;Lipid metabolism;Prostaglandin biosynthesis;Prostaglandin metabolism;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: Significantly increased expression by estrogen. Up-regulated after 1 hour of exposure to estrogen. Expression persists through 72 hours. {ECO:0000269|PubMed:11572089}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,730 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=128 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=97 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=410 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=116 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=67 umol/min/mg enzyme with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole as substrate {ECO:0000269|PubMed:9657971}; Vmax=1.4 umol/min/mg enzyme with 4-nitrobenzyl chloride as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.05 umol/min/mg enzyme with 1,2-dichloro-4-nitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.04 umol/min/mg enzyme with ethacrynic acid as substrate {ECO:0000269|PubMed:9657971}; Vmax=2.8 umol/min/mg enzyme with 4-hydroxynon-2-enal as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.06 umol/min/mg enzyme with trans,trans-deca-2,4-dienal as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.02 umol/min/mg enzyme with trans-non-2-enal as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.5 umol/min/mg enzyme with cumene hydroperoxide as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.06 umol/min/mg enzyme with t-butyl hydroperoxide as substrate {ECO:0000269|PubMed:9657971}; Vmax=12.6 umol/min/mg enzyme with allyl isothiocyanate as substrate {ECO:0000269|PubMed:9657971}; Vmax=17.6 umol/min/mg enzyme with benzyl isothiocyanate as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.02 umol/min/mg enzyme with Delta5-androstene-3,17-dione as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.11 umol/min/mg enzyme with 4-nitrophenyl acetate as substrate {ECO:0000269|PubMed:9657971}; |
| Metal Binding | |
| Rhea ID | RHEA:10600; RHEA:10601; RHEA:16437; RHEA:51232; RHEA:51233 |
| Cross Reference Brenda | 5.3.99.2; |