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Human Metabolome Database Version 2.5

 

Showing metabocard for Prostaglandin H2 (HMDB01381)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:42
Accession Number HMDB01381
Secondary Accession Numbers Not Available
Common Name Prostaglandin H2
Description Prostaglandin H2 (PGH2) is the first intermediate in the biosynthesis of all prostaglandins. Prostaglandins are synthesized from arachidonic acid by the enzyme COX-1 and COX-2, which are also called PGH synthase 1 and 2. These enzymes generate a reactive intermediate PGH2 which has a reasonably long half-life (90-100 s) but is highly lipophilic. PGH2 is converted into the biologically active prostaglandins by prostaglandin isomerases, yielding PGE2, PGD2, and PGF2, or by thromboxane synthase to make TxA2 or by prostacyclin synthase to make PGI2. Most nonsteroidal anti-inflammatory drugs such as aspirin and indomethacin inhibit both PGH synthase 1 and 2. A key feature for eicosanoid transcellular biosynthesis is the export of PGH2 or LTA4 from the donor cell as well as the uptake of these reactive intermediates by the acceptor cell. Very little is known about either process despite the demonstrated importance of both events. In cells, PGH2 rearranges nonenzymatically to LGs even in the presence of enzymes that use PGH2 as a substrate. When platelets form Thromboxane A2 (TXA2) from endogenous arachidonic acid (AA), PGH2 reaches concentrations very similar to those of TXA2 and high enough to produce strong platelet activation. Therefore, platelet activation by TXA2 appears to go along with an activation by PGH2. The agonism of PGH2 is limited by the formation of inhibitory prostaglandins, especially PGD2 at higher concentrations. That is why thromboxane synthase inhibitors in PRP and at a physiological HSA concentration do not augment platelet activation. (PMID: 2798452, 15650407, 16968946) Prostaglandins are eicosanoids. The eicosanoids consist of the prostaglandins (PGs), thromboxanes (TXs), leukotrienes (LTs) and lipoxins (LXs). The PGs and TXs are collectively identified as prostanoids. Prostaglandins were originally shown to be synthesized in the prostate gland, thromboxanes from platelets (thrombocytes) and leukotrienes from leukocytes, hence the derivation of their names. All mammalian cells except erythrocytes synthesize eicosanoids. These molecules are extremely potent, able to cause profound physiological effects at very dilute concentrations. All eicosanoids function locally at the site of synthesis, through receptor-mediated G-protein linked signaling pathways.
Synonyms
  1. Prostaglandin-H2
  2. Prostaglandin R2
  3. PGH2
  4. Endoperoxide H2
  5. 9S,11R-epidioxy-15S-hydroxy-5Z,13E-prostadienoic acid
  6. 9S,11R-epidioxy-15S-hydroxy-5Z,13E-prostadienoate
  7. 9,11-Epoxymethano-pgh2
  8. 15-Hydroxy-9alpha,11alpha-peroxidoprosta-5,13-dienoic acid
  9. 15-Hydroxy-9alpha,11alpha-peroxidoprosta-5,13-dienoate
  10. (5Z,9alpha,11alpha,13E,15S)-9,11-epidioxy-15-hydroxy-Prosta-5,13-dien-1-oic acid
  11. (5Z,9alpha,11alpha,13E,15S)-9,11-epidioxy-15-hydroxy-Prosta-5,13-dien-1-oate
  12. (5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate
  13. (5Z,13E)-(15S)-9,11-epidioxy-15-hydroxyprosta-5,13-dienoate
  14. (15S)Hydroxy-9alpha,11alpha-(epoxymethano)prosta-5,13-dienoic acid
  15. (15S)Hydroxy-9alpha,11alpha-(epoxymethano)prosta-5,13-dienoate
  16. (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
  17. (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoic acid
  18. (5Z)-7-{(1R,4S,5R,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2,3-dioxabicyclo[2.2.1]hept-5-yl}hept-5-enoic acid
  19. (5Z)-7-{(1R,4S,5R,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2,3-dioxabicyclo[2.2.1]hept-5-yl}hept-5-enoate
  20. (5Z,13E,15S)-9a,11a-epidioxy-15-hydroxyprosta-5,13-dienoic acid
  21. (5Z,13E,15S)-9a,11a-epidioxy-15-hydroxyprosta-5,13-dienoate
  22. (5Z,9a,11a,13E,15S)-9,11-epidioxy-15-hydroxyprosta-5,13-dien-1-oic acid
  23. (5Z,9a,11a,13E,15S)-9,11-epidioxy-15-hydroxyprosta-5,13-dien-1-oate
  24. (5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
  25. (5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoic acid
  26. (5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoic acid
  27. (5Z,13E)-(15S)-9,11-epidioxy-15-hydroxyprosta-5,13-dienoic acid
Chemical IUPAC Name 7-[5-(3-hydroxyoct-1-enyl)-2,3-dioxabicyclo[2.2.1]hept-6-yl]hept-5-enoic acid
Chemical Formula C20H32O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Prostanoids
Sub Class
  • Prostaglandins
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • peroxide
  • carboxylic acid
  • alkene
  • heterocyclic compound
Biofunction
  • Component of Prostaglandin and leukotriene metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 352.465
Monoisotopic Molecular Weight 352.224976
Isomeric SMILES CCCCC[C@H](O)C=C[C@H]1[C@H]2C[C@H](OO2)[C@@H]1CC=C/CCCC(O)=O
Canonical SMILES CCCCCC(O)C=CC1C2CC(OO2)C1CC=CCCCC(O)=O
KEGG Compound ID C00427 Link Image
BioCyc ID PROSTAGLANDIN-H2 Link Image
BiGG ID 34952 Link Image
Wikipedia Link Prostaglandin H2 Link Image
NuGOwiki Link HMDB01381 Link Image
Metagene Link HMDB01381 Link Image
METLIN ID 3495 Link Image
PubChem Compound 445049 Link Image
PubChem Substance 4265958 Link Image
ChEBI ID 15554 Link Image
CAS Registry Number 42935-17-1
InChI Identifier InChI=1/C20H32O5/c1-2-3-6-9-15(21)12-13-17-16(18-14-19(17)25-24-18)10-7-4-5-8-11-20(22)23/h4,7,12-13,15-19,21H,2-3,5-6,8-11,14H2,1H3,(H,22,23)/b7-4-,13-12+/t15-,16+,17+,18-,19+/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0337 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.27 [Predicted by ALOGPS]; 4.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location Not Available
Tissue Location
Tissue References
Platelet —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Onguru O, Casey MB, Kajita S, Nakamura N, Lloyd RV: Cyclooxygenase-2 and thromboxane synthase in non-endocrine and endocrine tumors: a review. Endocr Pathol. 2005 Winter;16(4):253-77. [PubMed Link Image]
  2. Rybicki JP, Le Breton GC: Prostaglandin H2 directly lowers human platelet cAMP levels. Thromb Res. 1983 Jun 1;30(5):407-14. [PubMed Link Image]
  3. Ulrich CM, Carlson CS, Sibert J, Poole EM, Yu JH, Wang LH, Sparks R, Potter JD, Bigler J: Thromboxane synthase (TBXAS1) polymorphisms in African-American and Caucasian populations: evidence for selective pressure. Hum Mutat. 2005 Oct;26(4):394-5. [PubMed Link Image]
  4. Hornberger W, Patscheke H: Transient concentrations and agonist potency of PGH2 in platelet activation by endogenous arachidonate. Eicosanoids. 1989;2(4):241-8. [PubMed Link Image]
  5. Johnson GJ, Dunlop PC, Leis LA, From AH: Dihydropyridine agonist Bay K 8644 inhibits platelet activation by competitive antagonism of thromboxane A2-prostaglandin H2 receptor. Circ Res. 1988 Mar;62(3):494-505. [PubMed Link Image]
  6. Maclouf J, Kindahl H, Granstrom E, Samuelsson B: Interactions of prostaglandin H2 and thromboxane A2 with human serum albumin. Eur J Biochem. 1980 Aug;109(2):561-6. [PubMed Link Image]
  7. Gerrard JM, White JG, Rao GH, Townsend D: Localization of platelet prostaglandin production in the platelet dense tubular system. Am J Pathol. 1976 May;83(2):283-98. [PubMed Link Image]
  8. Patscheke H, Hornberger W, Zehender H: Pathophysiological role of thromboxane A2 and pharmacological approaches to its inhibition. Z Kardiol. 1990;79 Suppl 3:151-4. [PubMed Link Image]
  9. Goerig M, Habenicht AJ, Zeh W, Salbach P, Kommerell B, Rothe DE, Nastainczyk W, Glomset JA: Evidence for coordinate, selective regulation of eicosanoid synthesis in platelet-derived growth factor-stimulated 3T3 fibroblasts and in HL-60 cells induced to differentiate into macrophages or neutrophils. J Biol Chem. 1988 Dec 25;263(36):19384-91. [PubMed Link Image]
  10. Beitz J, Forster W: Influence of human low density and high density lipoprotein cholesterol on the in vitro prostaglandin I2 synthetase activity. Biochim Biophys Acta. 1980 Dec 5;620(3):352-5. [PubMed Link Image]
  11. Mevkh AT, Basevich VV, Varfolomeev SD: [Synthesis of thromboxane A2: limiting stages of primary thrombocyte aggregation in humans initiated by arachidonic acid and its metabolic products] Biokhimiia. 1984 Dec;49(12):2035-40. [PubMed Link Image]
  12. Basevich VV, Mevkh AT, Varfolomeev SD: [Kinetic mechanisms of enzyme activity of the thromboxane synthetase system. Thromboxane synthetase of human platelets] Biokhimiia. 1984 Sep;49(9):1538-45. [PubMed Link Image]
  13. Gresele P, Deckmyn H, Nenci GG, Vermylen J: Thromboxane synthase inhibitors, thromboxane receptor antagonists and dual blockers in thrombotic disorders. Trends Pharmacol Sci. 1991 Apr;12(4):158-63. [PubMed Link Image]
  14. Borg C, Lam SC, Dieter JP, Lim CT, Komiotis D, Venton DL, Le Breton GC: Anti-peptide antibodies against the human blood platelet thromboxane A2/prostaglandin H2 receptor. Production, purification and characterization. Biochem Pharmacol. 1993 May 25;45(10):2071-8. [PubMed Link Image]
  15. Miller OV, Johnson RA, Gorman RR: Inhibition of PGE1-stimulated cAMP accumulation in human platelets by thromboxane a2. Prostaglandins. 1977 Apr;13(4):599-609. [PubMed Link Image]
  16. Kuzuya T, Hoshida S, Yamagishi M, Ohmori M, Inoue M, Kamada T, Tada M: Effect of OKY-046, a thromboxane A2 synthetase inhibitor, on arachidonate-induced platelet aggregation: possible role of "prostaglandin H2 steal" mechanism. Jpn Circ J. 1986 Nov;50(11):1071-8. [PubMed Link Image]
  17. Vezza R, Mezzasoma AM, Venditti G, Gresele P: Prostaglandin endoperoxides and thromboxane A2 activate the same receptor isoforms in human platelets. Thromb Haemost. 2002 Jan;87(1):114-21. [PubMed Link Image]
  18. Ushikubi F, Nakajima M, Hirata M, Okuma M, Fujiwara M, Narumiya S: Purification of the thromboxane A2/prostaglandin H2 receptor from human blood platelets. J Biol Chem. 1989 Oct 5;264(28):16496-501. [PubMed Link Image]
  19. Hornberger WB, Patscheke H: Prostaglandin H2 in human platelet activation: coactivator and substitute for thromboxane A2. Prog Clin Biol Res. 1989;301:315-9. [PubMed Link Image]
  20. Wikipedia Link Image
Metabolic Enzymes
  1. Prostaglandin E synthase
  2. Prostaglandin G/H synthase 1 precursor
  3. Prostacyclin synthase
  4. Glutathione-requiring prostaglandin D synthase
  5. Prostaglandin-H2 D-isomerase precursor
  6. Thromboxane-A synthase
  7. Prostaglandin E synthase 2
  8. Thromboxane A synthase 1
  9. cDNA FLJ75306, highly similar to Homo sapiens prostaglandin- endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase), mRNA (Prostaglandin-endoperoxide synthase 2) (Prostaglandin G/H synthase and cyclooxygenase)
  10. cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
  11. cDNA PSEC0009 fis, clone NT2RM1000731, highly similar to Prostaglandin-H2 D-isomerase (EC 5.3.99.2)
Enzyme 1 [top]
Enzyme 1 ID 5308
Enzyme 1 Name Prostaglandin E synthase
Enzyme 1 Synonyms
  1. Microsomal glutathione S- transferase 1-like 1
  2. MGST1-L1
  3. p53-induced apoptosis protein 12
Enzyme 1 Gene Name PTGES
Enzyme 1 Protein Sequence >Prostaglandin E synthase 
MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCR
SDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGK
LRAPIRSVTYTLAQLPCASMALQILWEAARHL
Enzyme 1 Number of Residues 152
Enzyme 1 Molecular Weight 17103
Enzyme 1 Theoretical pI 9.77
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15- hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15- dihydroxy-9-oxoprosta-5,13-dienoate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-31
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2415308 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14684 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PTGES_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >462 bp 
ATGCCTGCCCACAGCCTGGTGATGAGCAGCCCGGCCCTCCCGGCCTTCCTGCTCTGCAGC
ACGCTGCTGGTCATCAAGATGTACGTGGTGGCCATCATCACGGGCCAAGTGAGGCTGCGG
AAGAAGGCCTTTGCCAACCCCGAGGATGCCCTGAGACACGGAGGAGGCCCCCAGTATTGC
AGGAGCGACCCCGACGTGGAACGCTGCCTCAGGGCCCACCGGAACGACATGGAGACCATC
TACCCCTTCCTTTTCCTGGGCTTCGTCTACTCCTTTCTGGGTCCTAACCCTTTTGTCGCC
TGGATGCACTTCCTGGTCTTCCTCGTGGGCCGTGTGGCACACACCGTGGCCTACCTGGGG
AAGCTGCGGGCACCCATCCGCTCCGTGACCTACACCCTGGCCCAGCTCCCCTGCGCCTCC
ATGGCTCTGCAGATCCTCTGGGAAGCGGCCCGCCACCTGTGA
Enzyme 1 GenBank Gene ID AF010316 Link Image
Enzyme 1 GeneCard ID PTGES Link Image
Enzyme 1 GenAtlas ID PTGES Link Image
Enzyme 1 HGNC ID HGNC:9599 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9q34.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed Link Image]
  2. Jakobsson PJ, Thoren S, Morgenstern R, Samuelsson B: Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7220-5. [PubMed Link Image]
  3. Forsberg L, Leeb L, Thoren S, Morgenstern R, Jakobsson P: Human glutathione dependent prostaglandin E synthase: gene structure and regulation. FEBS Lett. 2000 Apr 7;471(1):78-82. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6264
Enzyme 2 Name Prostaglandin G/H synthase 1 precursor
Enzyme 2 Synonyms
  1. Cyclooxygenase- 1
  2. COX-1
  3. Prostaglandin-endoperoxide synthase 1
  4. Prostaglandin H2 synthase 1
  5. PGH synthase 1
  6. PGHS-1
  7. PHS 1
Enzyme 2 Gene Name PTGS1
Enzyme 2 Protein Sequence >Prostaglandin G/H synthase 1 precursor 
MSRSLLLRFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTR
TGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTVRS
NLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDAQLLARRF
LLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQ
YQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLY
ATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKF
DPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEA
LVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQEL
VGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICS
PEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL
Enzyme 2 Number of Residues 599
Enzyme 2 Molecular Weight 68657
Enzyme 2 Theoretical pI 7.39
Enzyme 2 GO Classification
Function
  • antioxidant activity
  • peroxidase activity
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells
Enzyme 2 Pathways
Enzyme 2 Reactions
  • arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-23
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 387018 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P23219 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PGH1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1800 bp 
ATGAGCCGGAGTCTCTTGCTCCGGTTCTTGCTGTTGCTGCTCCTGCTCCCGCCGCTCCCC
GTCCTGCTCGCGGACCCAGGGGCGCCCACGCCAGTGAATCCCTGTTGTTACTATCCATGC
CAGCACCAGGGCATCTGTGTCCGCTTCGGCCTTGACCGCTACCAGTGTGACTGCACCCGC
ACGGGCTATTCCGGCCCCAACTGCACCATCCCTGGCCTGTGGACCTGGCTCCGGAATTCA
CTGCGGCCCAGCCCCTCTTTCACCCACTTCCTGCTCACTCACGGGCGCTGGTTCTGGGAG
TTTGTCAATGCCACCTTCATCCGAGAGATGCTCATGCTCCTGGTACTCACAGTGCGCTCC
AACCTTATCCCCAGTCCCCCCACCTACAACTCTGCACATGACTACATCAGCTGGGAGTCT
TTCTCCAACGTGAGCTATTACACTCGTATTCTGCCCTCTGTGCCTAAAGATTGCCCCACA
CCCATGGGAACCAAAGGGAAGAAGCAGTTGCCAGATGCCCAGCTCCTGGCCCGCCGCTTC
CTGCTCAGGAGGAAGTTCATACCTGACCCCCAAGGCACCAACCTCATGTTTGCCTTCTTT
GCACAACACTTCACCCACCAGTTCTTCAAAACTTCTGGCAAGATGGGTCCTGGCTTCACC
AAGGCCTTGGGCCATGGGGTAGACCTCGGCCACATTTATGGAGACAATCTGGAGCGTCAG
TATCAACTGCGGCTCTTTAAGGATGGGAAACTCAAGTACCAGGTGCTGGATGGAGAAATG
TACCCGCCCTCGGTAGAAGAGGCGCCTGTGTTGATGCACTACCCCCGAGGCATCCCGCCC
CAGAGCCAGATGGCTGTGGGCCAGGAGGTGTTTGGGCTGCTTCCTGGGCTCATGCTGTAT
GCCACGCTCTGGCTACGTGAGCACAACCGTGTGTGTGACCTGCTGAAGGCTGAGCACCCC
ACCTGGGGCGATGAGCAGCTTTTCCAGACGACCCGCCTCATCCTCATAGGGGAGACCATC
AAGATTGTCATCGAGGAGTACGTGCAGCAGCTGAGTGGCTATTTCCTGCAGCTGAAATTT
GACCCAGAGCTGCTGTTCGGTGTCCAGTTCCAATACCGCAACCGCATTGCCACGGAGTTC
AACCATCTCTACCACTGGCACCCCCTCATGCCTGACTCCTTCAAGGTGGGCTCCCAGGAG
TACAGCTACGAGCAGTTCTTGTTCAACACCTCCATGTTGGTGGACTATGGGGTTGAGGCC
CTGGTGGATGCCTTCTCTCGCCAGATTGCTGGCCGGATCGGTGGGGGCAGGAACATGGAC
CACCACATCCTGCATGTGGCTGTGGATGTCATCAGGGAGTCTCGGGAGATGCGGCTGCAG
CCCTTCAATGAGTACCGCAAGAGGTTTGGCATGAAACCCTACACCTCCTTCCAGGAGCTC
GTAGGAGAGAAGGAGATGGCAGCAGAGTTGGAGGAATTGTATGGAGACATTGATGCGTTG
GAGTTCTACCCTGGACTGCTTCTTGAAAAGTGCCATCCAAACTCTATCTTTGGGGAGAGT
ATGATAGAGATTGGGGCTCCCTTTTCCCTCAAGGGTCTCCTAGGGAATCCCATCTGTTCT
CCGGAGTACTGGAAGCCGAGCACATTTGGCGGCGAGGTGGGCTTTAACATTGTCAAGACG
GCCACACTGAAGAAGCTGGTCTGCCTCAACACCAAGACCTGTCCCTACGTTTCCTTCCGT
GTGCCGGATGCCAGTCAGGATGATGGGCCTGCTGTGGAGCGACCATCCACAGAGCTCTGA
Enzyme 2 GenBank Gene ID M31822 Link Image
Enzyme 2 GeneCard ID PTGS1 Link Image
Enzyme 2 GenAtlas ID PTGS1 Link Image
Enzyme 2 HGNC ID HGNC:9604 Link Image
Enzyme 2 Chromosome Location 9
Enzyme 2 Locus 9q32-q33.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Yokoyama C, Tanabe T: Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme. Biochem Biophys Res Commun. 1989 Dec 15;165(2):888-94. [PubMed Link Image]
  2. Funk CD, Funk LB, Kennedy ME, Pong AS, Fitzgerald GA: Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment. FASEB J. 1991 Jun;5(9):2304-12. [PubMed Link Image]
  3. Takahashi Y, Ueda N, Yoshimoto T, Yamamoto S, Yokoyama C, Miyata A, Tanabe T, Fuse I, Hattori A, Shibata A: Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase). Biochem Biophys Res Commun. 1992 Jan 31;182(2):433-8. [PubMed Link Image]
  4. Diaz A, Reginato AM, Jimenez SA: Alternative splicing of human prostaglandin G/H synthase mRNA and evidence of differential regulation of the resulting transcripts by transforming growth factor beta 1, interleukin 1 beta, and tumor necrosis factor alpha. J Biol Chem. 1992 May 25;267(15):10816-22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6425
Enzyme 3 Name Prostacyclin synthase
Enzyme 3 Synonyms
  1. Prostaglandin I2 synthase
Enzyme 3 Gene Name PTGIS
Enzyme 3 Protein Sequence >Prostacyclin synthase 
MAWAALLGLLAALLLLLLLSRRRTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEK
HGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDE
KARMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTL
YGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSLSVGDKDHMCSVKSRLWKL
LSPARLARRAHRSKWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLL
KNPEALAAVRGELESILWQAEQPVSQTTTLPQKVLDSTPVLDSVLSESLRLTAAPFITRE
VVVDLAMPMADGREFNLRRGDRLLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDF
YKDGKRLKNYNMPWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSR
YGFGLMQPEHDVPVRYRIRP
Enzyme 3 Number of Residues 500
Enzyme 3 Molecular Weight 57105
Enzyme 3 Theoretical pI 7.33
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 3 Specific Function Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-24
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 537949 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q16647 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PTGIS_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1503 bp 
ATGGCTTGGGCCGCGCTCCTCGGCCTCCTGGCCGCACTGTTGCTGCTGCTGCTACTGAGC
CGCCGCCGCACGCGGCGACCTGGTGAGCCTCCCCTGGACCTGGGCAGCATCCCCTGGTTG
GGGTATGCCTTGGACTTTGGAAAAGATGCTGCCAGCTTCCTCACGAGGATGAAGGAGAAG
CACGGTGACATCTTTACTATACTGGTTGGGGGCAGGTATGTCACCGTTCTCCTGGACCCA
CACTCCTACGACGCGGTGGTGTGGGAGCCTCGCACCAGGCTCGACTTCCATGCCTATGCC
ATCTTCCTCATGGAGAGGATTTTTGATGTGCAGCTTCCACATTACAGCCCCAGTGATGAA
AAGGCCAGGATGAAACTGACTCTTCTCCACAGAGAGCTCCAGGCACTCACAGAAGCCATG
TATACCAACCTCCATGCAGTGCTGTTGGGCGATGCTACAGAAGCAGGCAGTGGCTGGCAC
GAGATGGGTCTCCTCGACTTCTCCTACAGCTTCCTGCTCAGAGCCGGCTACCTGACTCTT
TACGGAATTGAGGCGCTGCCACGCACCCATGAAAGCCAGGCCCAGGACCGCGTCCACTCA
GCTGATGTCTTCCACACCTTTCGCCAGCTCGACCGGCTGCTCCCCAAACTGGCCCGTGGC
TCCCTGTCAGTGGGGGACAAGGACCACATGTGCAGTGTCAAAAGTCGCCTGTGGAAGCTG
CTATCCCCAGCCAGGCTGGCCAGGCGGGCCCACCGGAGCAAATGGCTGGAGAGTTACCTG
CTGCACCTGGAGGAGATGGGTGTGTCAGAGGAGATGCAGGCACGGGCCCTGGTGCTGCAG
CTGTGGGCCACACAGGGGAATATGGGTCCCGCTGCCTTCTGGCTCCTGCTCTTCCTTCTC
AAGAATCCTGAAGCCCTGGCTGCTGTCCGCGGAGAGCTCGAGAGTATCCTTTGGCAAGCG
GAGCAGCCTGTCTCGCAGACGACCACTCTCCCACAGAAGGTTCTAGACAGCACACCTGTG
CTTGATAGCGTGCTGAGTGAGAGCCTCAGGCTTACAGCTGCCCCCTTCATCACCCGCGAG
GTTGTGGTGGACCTGGCCATGCCCATGGCAGACGGGAGAGAATTCAACCTGCGACGTGGT
GACCGCCTCCTCCTCTTCCCCTTCCTGAGCCCCCAGAGAGACCCAGAAATCTACACAGAC
CCAGAGGTATTTAAATACAACCGATTCCTGAACCCTGACGGATCAGAGAAGAAAGACTTT
TACAAGGATGGGAAACGGCTGAAGAATTACAACATGCCCTGGGGGGCGGGGCACAATCAC
TGCCTGGGGAGGAGTTATGCGGTCAACAGCATCAAACAATTTGTGTTCCTTGTGCTGGTG
CACTTGGACTTGGAGCTGATCAACGCAGATGTGGAGATCCCTGAGTTTGACCTCAGCAGG
TACGGCTTCGGTCTGATGCAGCCGGAACACGACGTGCCCGTCCGCTACCGCATCCGCCCA
TGA
Enzyme 3 GenBank Gene ID D38145 Link Image
Enzyme 3 GeneCard ID PTGIS Link Image
Enzyme 3 GenAtlas ID PTGIS Link Image
Enzyme 3 HGNC ID HGNC:9603 Link Image
Enzyme 3 Chromosome Location 20
Enzyme 3 Locus 20q13.13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Miyata A, Hara S, Yokoyama C, Inoue H, Ullrich V, Tanabe T: Molecular cloning and expression of human prostacyclin synthase. Biochem Biophys Res Commun. 1994 May 16;200(3):1728-34. [PubMed Link Image]
  2. Chevalier D, Cauffiez C, Bernard C, Lo-Guidice JM, Allorge D, Fazio F, Ferrari N, Libersa C, Lhermitte M, D'Halluin JC, Broly F: Characterization of new mutations in the coding sequence and 5'-untranslated region of the human prostacylcin synthase gene (CYP8A1). Hum Genet. 2001 Feb;108(2):148-55. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6871
Enzyme 4 Name Glutathione-requiring prostaglandin D synthase
Enzyme 4 Synonyms
  1. Glutathione-dependent PGD synthetase
  2. Prostaglandin-H2 D-isomerase
  3. Hematopoietic prostaglandin D synthase
  4. H-PGDS
Enzyme 4 Gene Name PTGDS2
Enzyme 4 Protein Sequence >Glutathione-requiring prostaglandin D synthase 
MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLT
LHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELL
TYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKK
VQAIPAVANWIKRRPQTKL
Enzyme 4 Number of Residues 199
Enzyme 4 Molecular Weight 23344
Enzyme 4 Theoretical pI 5.64
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 3046817 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O60760 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PTGD2_HUMAN Link Image
Enzyme 4 PDB ID 1IYI Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >600 bp 
ATGCCAAACTACAAACTCACTTATTTTAATATGAGGGGGAGAGCAGAAATTATTCGTTAC
ATATTTGCTTATTTGGACATACAGTATGAAGACCACAGAATAGAACAAGCTGACTGGCCT
GAAATCAAATCAACTCTCCCATTTGGAAAAATCCCCATTTTGGAAGTTGATGGACTTACT
CTTCACCAGAGCCTAGCAATAGCAAGATATTTGACCAAAAACACAGATTTGGCTGGAAAC
ACAGAAATGGAACAATGTCATGTTGATGCTATTGTGGACACTCTGGATGATTTCATGTCA
TGTTTTCCTTGGGCAGAGAAAAAGCAAGATGTGAAAGAGCAGATGTTCAATGAGCTGCTC
ACGTATAATGCGCCTCATCTTATGCAAGACTTGGACACATATTTAGGGGGGAGAGAATGG
CTTATTGGTAACTCTGTAACTTGGGCAGACTTCTACTGGGAGATTTGCAGTACCACACTT
TTGGTCTTTAAGCCTGACCTGTTAGACAACCATCCAAGGCTGGTGACTTTACGGAAGAAA
GTCCAAGCCATTCCTGCCGTCGCTAACTGGATAAAACGAAGGCCCCAAACCAAACTCTAG
Enzyme 4 GenBank Gene ID D82073 Link Image
Enzyme 4 GeneCard ID Not Available
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Kanaoka Y, Fujimori K, Kikuno R, Sakaguchi Y, Urade Y, Hayaishi O: Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Conservation of the ancestral genomic structure of sigma-class glutathione S-transferase. Eur J Biochem. 2000 Jun;267(11):3315-22. [PubMed Link Image]
  2. Suzuki T, Watanabe K, Kanaoka Y, Sato T, Hayaishi O: Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester. Biochem Biophys Res Commun. 1997 Dec 18;241(2):288-93. [PubMed Link Image]
  3. Mahmud I, Ueda N, Yamaguchi H, Yamashita R, Yamamoto S, Kanaoka Y, Urade Y, Hayaishi O: Prostaglandin D synthase in human megakaryoblastic cells. J Biol Chem. 1997 Nov 7;272(45):28263-6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6872
Enzyme 5 Name Prostaglandin-H2 D-isomerase precursor
Enzyme 5 Synonyms
  1. Lipocalin-type prostaglandin-D synthase
  2. Glutathione-independent PGD synthetase
  3. Prostaglandin-D2 synthase
  4. PGD2 synthase
  5. PGDS2
  6. PGDS
  7. Beta-trace protein
  8. Cerebrin-28
Enzyme 5 Gene Name PTGDS
Enzyme 5 Protein Sequence >Prostaglandin-H2 D-isomerase precursor 
MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKA
ALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSV
VETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFL
PQTDKCMTEQ
Enzyme 5 Number of Residues 190
Enzyme 5 Molecular Weight 21029
Enzyme 5 Theoretical pI 7.94
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • intramolecular oxidoreductase activity
  • isomerase activity
  • prostaglandin-D synthase activity
  • transporter activity
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • cellular physiological process
  • fatty acid metabolism
  • icosanoid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
  • prostaglandin metabolism
  • prostanoid metabolism
  • transport
Component
—
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system
Enzyme 5 Pathways
Enzyme 5 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-22
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 111080340 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P41222 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PTGDS_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >573 bp 
ATGGCTACTCATCACACGCTGTGGATGGGACTGGCCCTGCTGGGGGTGCTGGGCGACCTG
CAGGCAGCACCGGAGGCCCAGGTCTCCGTGCAGCCCAACTTCCAGCAGGACAAGTTCCTG
GGGCGCTGGTTCAGCGCGGGCCTCGCCTCCAACTCGAGCTGGCTCCGGGAGAAGAAGGCG
GCGTTGTCCATGTGCAAGTCTGTGGTGGCCCCTGCCACGGATGGTGGCCTCAACCTGACC
TCCACCTTCCTCAGGAAAAACCAGTGTGAGACCCGAACCATGCTGCTGCAGCCCGCGGGG
TCCCTCGGCTCCTACAGCTACCGGAGTCCCCACTGGGGCAGCACCTACTCCGTGTCAGTG
GTGGAGACCGACTACGACCAGTACGCGCTGCTGTACAGCCAGGGCAGCAAGGGCCCTGGC
GAGGACTTCCGCATGGCCACCCTCTACAGCCGAACCCAGACCCCCAGGGCTGAGTTAAAG
GAGAAATTCACCGCCTTCTGCAAGGCCCAGGGCTTCACAGAGGATACCATTGTCTTCCTG
CCCCAAACCGATAAGTGCATGACGGAACAATAG
Enzyme 5 GenBank Gene ID M61900 Link Image
Enzyme 5 GeneCard ID PTGDS Link Image
Enzyme 5 GenAtlas ID PTGDS Link Image
Enzyme 5 HGNC ID HGNC:9592 Link Image
Enzyme 5 Chromosome Location 9
Enzyme 5 Locus 9q34.2-q34.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Nagata A, Suzuki Y, Igarashi M, Eguchi N, Toh H, Urade Y, Hayaishi O: Human brain prostaglandin D synthase has been evolutionarily differentiated from lipophilic-ligand carrier proteins. Proc Natl Acad Sci U S A. 1991 May 1;88(9):4020-4. [PubMed Link Image]
  2. White DM, Mikol DD, Espinosa R, Weimer B, Le Beau MM, Stefansson K: Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase. J Biol Chem. 1992 Nov 15;267(32):23202-8. [PubMed Link Image]
  3. Hoffmann A, Conradt HS, Gross G, Nimtz M, Lottspeich F, Wurster U: Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase. J Neurochem. 1993 Aug;61(2):451-6. [PubMed Link Image]
  4. Harrington MG, Aebersold R, Martin BM, Merril CR, Hood L: Identification of a brain-specific human cerebrospinal fluid glycoprotein, beta-trace protein. Appl Theor Electrophor. 1993;3(5):229-34. [PubMed Link Image]
  5. Zahn M, Mader M, Schmidt B, Bollensen E, Felgenhauer K: Purification and N-terminal sequence of beta-trace, a protein abundant in human cerebrospinal fluid. Neurosci Lett. 1993 May 14;154(1-2):93-5. [PubMed Link Image]
  6. Kuruvilla AP, Hochwald GM, Ghiso J, Castano EM, Pizzolato M, Frangione B: Isolation and amino terminal sequence of beta-trace, a novel protein from human cerebrospinal fluid. Brain Res. 1991 Nov 29;565(2):337-40. [PubMed Link Image]
  7. Tokugawa Y, Kunishige I, Kubota Y, Shimoya K, Nobunaga T, Kimura T, Saji F, Murata Y, Eguchi N, Oda H, Urade Y, Hayaishi O: Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma. Biol Reprod. 1998 Feb;58(2):600-7. [PubMed Link Image]
  8. Saso L, Leone MG, Sorrentino C, Giacomelli S, Silvestrini B, Grima J, Li JC, Samy E, Mruk D, Cheng CY: Quantification of prostaglandin D synthetase in cerebrospinal fluid: a potential marker for brain tumor. Biochem Mol Biol Int. 1998 Nov;46(4):643-56. [PubMed Link Image]
  9. Leone MG, Saso L, Del Vecchio A, Mo MY, Silvestrini B, Cheng CY: Micropurification of two human cerebrospinal fluid proteins by high performance electrophoresis chromatography. J Neurochem. 1993 Aug;61(2):533-40. [PubMed Link Image]
  10. Giacomelli S, Leone MG, Grima J, Silvestrini B, Cheng CY: Astrocytes synthesize and secrete prostaglandin D synthetase in vitro. Biochim Biophys Acta. 1996 Feb 29;1310(3):269-76. [PubMed Link Image]
  11. Yamashima T, Sakuda K, Tohma Y, Yamashita J, Oda H, Irikura D, Eguchi N, Beuckmann CT, Kanaoka Y, Urade Y, Hayaishi O: Prostaglandin D synthase (beta-trace) in human arachnoid and meningioma cells: roles as a cell marker or in cerebrospinal fluid absorption, tumorigenesis, and calcification process. J Neurosci. 1997 Apr 1;17(7):2376-82. [PubMed Link Image]
  12. Blodorn B, Mader M, Urade Y, Hayaishi O, Felgenhauer K, Bruck W: Choroid plexus: the major site of mRNA expression for the beta-trace protein (prostaglandin D synthase) in human brain. Neurosci Lett. 1996 May 10;209(2):117-20. [PubMed Link Image]
  13. Eguchi Y, Eguchi N, Oda H, Seiki K, Kijima Y, Matsu-ura Y, Urade Y, Hayaishi O: Expression of lipocalin-type prostaglandin D synthase (beta-trace) in human heart and its accumulation in the coronary circulation of angina patients. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14689-94. [PubMed Link Image]
  14. Blodorn B, Bruck W, Tumani H, Michel U, Rieckmann P, Althans N, Mader M: Expression of the beta-trace protein in human pachymeninx as revealed by in situ hybridization and immunocytochemistry. J Neurosci Res. 1999 Sep 1;57(5):730-4. [PubMed Link Image]
  15. Hirawa N, Uehara Y, Yamakado M, Toya Y, Gomi T, Ikeda T, Eguchi Y, Takagi M, Oda H, Seiki K, Urade Y, Umemura S: Lipocalin-type prostaglandin d synthase in essential hypertension. Hypertension. 2002 Feb;39(2 Pt 2):449-54. [PubMed Link Image]
  16. White DM, Takeda T, DeGroot LJ, Stefansson K, Arnason BG: Beta-trace gene expression is regulated by a core promoter and a distal thyroid hormone response element. J Biol Chem. 1997 May 30;272(22):14387-93. [PubMed Link Image]
  17. Hiraoka A, Seiki K, Oda H, Eguchi N, Urade Y, Tominaga I, Baba K: Charge microheterogeneity of the beta-trace proteins (lipocalin-type prostaglandin D synthase) in the cerebrospinal fluid of patients with neurological disorders analyzed by capillary isoelectrofocusing. Electrophoresis. 2001 Oct;22(16):3433-7. [PubMed Link Image]
  18. Hirawa N, Uehara Y, Ikeda T, Gomi T, Hamano K, Totsuka Y, Yamakado M, Takagi M, Eguchi N, Oda H, Seiki K, Nakajima H, Urade Y: Urinary prostaglandin D synthase (beta-trace) excretion increases in the early stage of diabetes mellitus. Nephron. 2001 Apr;87(4):321-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6879
Enzyme 6 Name Thromboxane-A synthase
Enzyme 6 Synonyms
  1. TXA synthase
  2. TXS
  3. Cytochrome P450 5A1
Enzyme 6 Gene Name TBXAS1
Enzyme 6 Protein Sequence >Thromboxane-A synthase 
MEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFR
QGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSV
ADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQR
CYCNYTTDVVASVPFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLA
RILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDIV
RDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATN
PDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEV
LGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCL
GVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR
Enzyme 6 Number of Residues 533
Enzyme 6 Molecular Weight 60545
Enzyme 6 Theoretical pI 7.68
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 6 Specific Function (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15- hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9-alpha,11-alpha- epoxy-15-hydroxythromboxa-5,13-dienoate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9alpha,11alpha-epoxy-15-hydroxythromboxa-5,13-dienoate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-34
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 338704 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P24557 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name THAS_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1605 bp 
ATGATGGAAGCCTTGGGGTTTCTAAAATTGGAAGTGAATGGCCCCATGGTGACGGTGGCC
CTGTCAGTGGCTCTCTTGGCCCTCCTGAAATGGTACTCCACATCAGCATTCTCAAGACTG
GAGAAGTTAGGCCTCAGACATCCCAAGCCTTCTCCTTTCATTGGAAACTTGACATTTTTC
CGCCAGGGTTTTTGGGAAAGCCAAATGGAGCTCAGAAAGCTGTATGGACCTCTGTGTGGG
TACTATCTTGGTCGTCGGATGTTTATTGTTATTTCTGAGCCAGACATGATCAAGCAGGTG
TTGGTTGAGAACTTCAGTAACTTTACCAACAGAATGGCGTCGGGTTTGGAGTTCAAGTCG
GTAGCCGACAGCGTTCTGTTTTTACGTGACAAAAGATGGGAAGAGGTCAGAGGTGCCCTG
ATGTCTGCTTTCAGTCCTGAAAAGCTGAACGAGATGGTTCCCCTCATCAGCCAAGCCTGC
GACCTTCTCCTGGCTCATTTAAAACGCTATGCGGAATCTGGGGACGCATTTGACATCCAG
AGGTGCTACTGCAATTACACCACAGATGTGGTTGCCAGCGTCCCGTTTGGCACCCCGGTG
GACTCCTGGCAGGCCCCTGAGGATCCCTTTGTGAAACACTGCAAGCGTTTCTTCGAATTC
TGCATCCCCAGACCTATCCTGGTTTTACTCTTATCATTTCCATCCATAATGGTCCCACTG
GCCCGGATTTTGCCCAATAAGAACCGAGACGAACTGAATGGCTTTTTTAACAAACTCATT
AGGAATGTGATTGCCTTGCGGGACCAGCAAGCTGCCGAAGAGAGGCGGAGAGACTTCCTC
CAAATGGTCCTGGATGCCCGACATTCTGCAAGTCCCATGGGCGTGCAAGACTTTGACATC
GTCAGAGACGTTTTCTCCTCTACTGGGTGCAAGCCGAACCCTTCCCGGCAACACCAGCCC
AGCCCTATGGCCAGGCCTTTGACTGTGGATGAGATTGTGGGCCAGGCCTTCATCTTCCTC
ATCGCTGGCTATGAAATCATCACCAACACACTTTCTTTTGCCACCTACCTACTGGCCACC
AACCCTGACTGCCAAGAGAAGCTTCTGAGAGAGGTAGACGTTTTTAAGGAGAAACACATG
GCCCCTGAGTTCTGCAGCCTCGAGGAAGGCCTGCCCTATCTGGACATGGTGATTGCAGAG
ACGCTGAGGATGTACCCGCCAGCTTTCAGATTCACACGGGAGGCAGCTCAGGACTGCGAG
GTGCTGGGGCAGCGCATCCCCGCAGGCGCTGTGCTAGAGATGGCCGTGGGTGCCCTGCAC
CATGACCCTGAGCACTGGCCAAGCCCGGAGACCTTCAACCCTGAAAGGTTCACGGCTGAG
GCCCGGCAGCAGCACCGGCCCTTCACGTACCTGCCCTTCGGGGCCGGCCCACGGAGCTGC
CTCGGGGTGCGTCTAGGGCTGCTTGAGGTCAAGTTGACACTGCTCCACGTGCTGCACAAG
TTCCGGTTCCAAGCCTGCCCTGAGACCCAGGTACCGCTGCAGCTAGAATCCAAATCTGCC
CTAGGTCCAAAAAATGGTGTCTATATCAAGATCGTATCCCGCTGA
Enzyme 6 GenBank Gene ID M80647 Link Image
Enzyme 6 GeneCard ID TBXAS1 Link Image
Enzyme 6 GenAtlas ID TBXAS1 Link Image
Enzyme 6 HGNC ID HGNC:11609 Link Image
Enzyme 6 Chromosome Location 7
Enzyme 6 Locus 7q34-q35
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Yokoyama C, Miyata A, Ihara H, Ullrich V, Tanabe T: Molecular cloning of human platelet thromboxane A synthase. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1479-84. [PubMed Link Image]
  2. Ohashi K, Ruan KH, Kulmacz RJ, Wu KK, Wang LH: Primary structure of human thromboxane synthase determined from the cDNA sequence. J Biol Chem. 1992 Jan 15;267(2):789-93. [PubMed Link Image]
  3. Miyata A, Yokoyama C, Ihara H, Bandoh S, Takeda O, Takahashi E, Tanabe T: Characterization of the human gene (TBXAS1) encoding thromboxane synthase. Eur J Biochem. 1994 Sep 1;224(2):273-9. [PubMed Link Image]
  4. Chevalier D, Lo-Guidice JM, Sergent E, Allorge D, Debuysere H, Ferrari N, Libersa C, Lhermitte M, Broly F: Identification of genetic variants in the human thromboxane synthase gene (CYP5A1). Mutat Res. 2001 Jan;432(3-4):61-7. [PubMed Link Image]
  5. Wang LH, Ohashi K, Wu KK: Isolation of partial complementary DNA encoding human thromboxane synthase. Biochem Biophys Res Commun. 1991 May 31;177(1):286-91. [PubMed Link Image]
  6. Nusing R, Schneider-Voss S, Ullrich V: Immunoaffinity purification of human thromboxane synthase. Arch Biochem Biophys. 1990 Aug 1;280(2):325-30. [PubMed Link Image]
  7. Ruan KH, Wang LH, Wu KK, Kulmacz RJ: Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum. J Biol Chem. 1993 Sep 15;268(26):19483-90. [PubMed Link Image]
  8. Mestel F, Oetliker O, Beck E, Felix R, Imbach P, Wagner HP: Severe bleeding associated with defective thromboxane synthetase. Lancet. 1980 Jan 19;1(8160):157. [PubMed Link Image]
  9. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  10. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed Link Image]
  11. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 11165
Enzyme 7 Name Prostaglandin E synthase 2
Enzyme 7 Synonyms
  1. Microsomal prostaglandin E synthase 2
  2. mPGES-2[Contains: Prostaglandin E synthase 2 truncated form]
Enzyme 7 Gene Name PTGES2
Enzyme 7 Protein Sequence >Prostaglandin E synthase 2 
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
Enzyme 7 Number of Residues 377
Enzyme 7 Molecular Weight 41944
Enzyme 7 Theoretical pI Not Available
Enzyme 7 GO Classification
Function
  • electron transporter activity
  • transporter activity
Process
  • cell homeostasis
  • cell redox homeostasis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • homeostasis
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Isomerase that catalyzes the conversion of unstable intermediate of prostaglandin E2 H2 (PGH2) into the more stable prostaglandin E2 (PGE2) form. May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear
Enzyme 7 Pathways
Enzyme 7 Reactions
  • Prostaglandin H2 <==> Prostaglandin E2
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 58-74
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 10436397 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9H7Z7 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PGES2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK024100 Link Image
Enzyme 7 GeneCard ID Not Available
Enzyme 7 GenAtlas ID PTGES2 Link Image
Enzyme 7 HGNC ID HGNC:17822 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Tanikawa N, Ohmiya Y, Ohkubo H, Hashimoto K, Kangawa K, Kojima M, Ito S, Watanabe K: Identification and characterization of a novel type of membrane-associated prostaglandin E synthase. Biochem Biophys Res Commun. 2002 Mar 8;291(4):884-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 12988
Enzyme 8 Name Thromboxane A synthase 1
Enzyme 8 Synonyms
  1. Platelet, cytochrome P450, family 5, subfamily Aisoform TXS-I variant
  2. HCG14925, isoform CRA_a
Enzyme 8 Gene Name Not Available
Enzyme 8 Protein Sequence >Thromboxane A synthase 1 
MMEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFF
RQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKS
VADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQ
RCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPL
ARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDI
VRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLAT
NPDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCE
VLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSC
LGVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR
Enzyme 8 Number of Residues 534
Enzyme 8 Molecular Weight 60650
Enzyme 8 Theoretical pI 7.68
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 8 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 62898664 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q53F23 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q53F23_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK223466 Link Image
Enzyme 8 GeneCard ID Q53F23 Link Image
Enzyme 8 GenAtlas ID hCG_14925 Link Image
Enzyme 8 HGNC ID HGNC:11609 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs Not Available
Enzyme 8 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 15877
Enzyme 9 Name cDNA FLJ75306, highly similar to Homo sapiens prostaglandin- endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase), mRNA (Prostaglandin-endoperoxide synthase 2) (Prostaglandin G/H synthase and cyclooxygenase)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name PTGS2
Enzyme 9 Protein Sequence >cDNA FLJ75306, highly similar to Homo sapiens prostaglandin- endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase), mRNA (Prostaglandin-endoperoxide synthase 2) (Prostaglandin G/H synthase and cyclooxygenase) 
MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFL
TRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADY
GYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGS
NMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKY
QIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCD
VLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQ
NRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRV
AGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEAL
YGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEV
GFQIINTASIQSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKER
STEL
Enzyme 9 Number of Residues 604
Enzyme 9 Molecular Weight 68997
Enzyme 9 Theoretical pI 7.41
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID A8K802 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name A8K802_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK292167 Link Image
Enzyme 9 GeneCard ID A8K802 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16494
Enzyme 10 Name cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name Not Available
Enzyme 10 Protein Sequence >cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3) 
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRALL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLIFPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
Enzyme 10 Number of Residues 377
Enzyme 10 Molecular Weight 41970
Enzyme 10 Theoretical pI 9.50
Enzyme 10 GO Classification
Function
  • electron transporter activity
  • transporter activity
Process
  • cell homeostasis
  • cell redox homeostasis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • homeostasis
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate [RN:R02265] ALL_REAC R02265
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID B3KPZ2 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B3KPZ2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK057049 Link Image
Enzyme 10 GeneCard ID B3KPZ2 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs Not Available
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16761
Enzyme 11 Name cDNA PSEC0009 fis, clone NT2RM1000731, highly similar to Prostaglandin-H2 D-isomerase (EC 5.3.99.2)
Enzyme 11 Synonyms
  1. SubName: Prostaglandin D2 synthase 21kDa (Brain), isoform CRA_a
  2. SubName: cDNA, FLJ93254, Homo sapiens prostaglandin D2 synthase 21kDa (brain) (PTGDS), mRNA
Enzyme 11 Gene Name PTGDS
Enzyme 11 Protein Sequence >cDNA PSEC0009 fis, clone NT2RM1000731, highly similar to Prostaglandin-H2 D-isomerase (EC 5.3.99.2) 
MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKA
ALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSV
VETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFL
PQTDKCMTEQ
Enzyme 11 Number of Residues 190
Enzyme 11 Molecular Weight 21029
Enzyme 11 Theoretical pI 7.94
Enzyme 11 GO Classification
Function
  • binding
  • catalytic activity
  • intramolecular oxidoreductase activity
  • isomerase activity
  • prostaglandin-D synthase activity
  • transporter activity
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • cellular physiological process
  • fatty acid metabolism
  • icosanoid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
  • prostaglandin metabolism
  • prostanoid metabolism
  • transport
Component
—
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate [RN:R02266] ALL_REAC R02266
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B2R727 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B2R727_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK312817 Link Image
Enzyme 11 GeneCard ID B2R727 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available