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Prostaglandin E synthase (EC 5.3.99.3) (Microsomal glutathione S-transferase 1-like 1) (MGST1-L1) (Microsomal prostaglandin E synthase 1) (MPGES-1) (p53-induced gene 12 protein)

 PTGES_HUMAN             Reviewed;         152 AA.
O14684; O14900; Q5SZC0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
22-NOV-2017, entry version 143.
RecName: Full=Prostaglandin E synthase;
EC=5.3.99.3;
AltName: Full=Microsomal glutathione S-transferase 1-like 1;
Short=MGST1-L1;
AltName: Full=Microsomal prostaglandin E synthase 1;
Short=MPGES-1;
AltName: Full=p53-induced gene 12 protein;
Name=PTGES; Synonyms=MGST1L1, MPGES1, PGES, PIG12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY TP53.
TISSUE=Colon cancer;
PubMed=9305847; DOI=10.1038/38525;
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
"A model for p53-induced apoptosis.";
Nature 389:300-306(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10377395; DOI=10.1073/pnas.96.13.7220;
Jakobsson P.-J., 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. 96:7220-7225(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10760517; DOI=10.1016/S0014-5793(00)01367-3;
Forsberg L., Leeb L., Thoren S., Morgenstern R., Jakobsson P.J.;
"Human glutathione dependent prostaglandin E synthase: gene structure
and regulation.";
FEBS Lett. 471:78-82(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
ENZYME KINETICS.
PubMed=12460774; DOI=10.1016/S1046-5928(02)00566-1;
Ouellet M., Falgueyret J.-P., Ear P.H., Pen A., Mancini J.A.,
Riendeau D., Percival M.D.;
"Purification and characterization of recombinant microsomal
prostaglandin E synthase-1.";
Protein Expr. Purif. 26:489-495(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
STRUCTURE BY ELECTRON CRYOMICROSCOPY.
PubMed=12672824; DOI=10.1074/jbc.M303227200;
Thoren S., Weinander R., Saha S., Jegerschold C., Pettersson P.L.,
Samuelsson B., Hebert H., Hamberg M., Morgenstern R., Jakobsson P.-J.;
"Human microsomal prostaglandin E synthase-1: purification, functional
characterization, and projection structure determination.";
J. Biol. Chem. 278:22199-22209(2003).
[11]
STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) IN COMPLEX WITH
GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR
LOCATION, TRANSMEMBRANE TOPOLOGY, AND MUTAGENESIS OF GLU-66; ARG-67;
ARG-70; HIS-72; ARG-110 AND TYR-117.
PubMed=18682561; DOI=10.1073/pnas.0802894105;
Jegerschold C., Pawelzik S.C., Purhonen P., Bhakat P., Gheorghe K.R.,
Gyobu N., Mitsuoka K., Morgenstern R., Jakobsson P.J., Hebert H.;
"Structural basis for induced formation of the inflammatory mediator
prostaglandin E2.";
Proc. Natl. Acad. Sci. U.S.A. 105:11110-11115(2008).
[12]
X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEXES WITH GLUTATIONE,
SUBUNIT, AND PROBABLE TOPOLOGY.
PubMed=23431194; DOI=10.1073/pnas.1218504110;
Sjogren T., Nord J., Ek M., Johansson P., Liu G., Geschwindner S.;
"Crystal structure of microsomal prostaglandin E2 synthase provides
insight into diversity in the MAPEG superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 110:3806-3811(2013).
-!- FUNCTION: Catalyzes the oxidoreduction of prostaglandin
endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2).
{ECO:0000269|PubMed:18682561}.
-!- CATALYTIC ACTIVITY: (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.
{ECO:0000269|PubMed:18682561}.
-!- COFACTOR:
Name=glutathione; Xref=ChEBI:CHEBI:57925;
Evidence={ECO:0000269|PubMed:18682561};
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:23431194}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18682561};
Multi-pass membrane protein {ECO:0000269|PubMed:18682561}.
-!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:9305847}.
-!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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EMBL; AF010316; AAC39534.1; -; mRNA.
EMBL; AF027740; AAB82299.1; -; mRNA.
EMBL; AJ271802; CAB72099.1; -; Genomic_DNA.
EMBL; AJ271803; CAB72099.1; JOINED; Genomic_DNA.
EMBL; AJ271804; CAB72099.1; JOINED; Genomic_DNA.
EMBL; AK311947; BAG34888.1; -; mRNA.
EMBL; EF543149; ABQ01233.1; -; Genomic_DNA.
EMBL; AL590369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL592219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008280; AAH08280.1; -; mRNA.
CCDS; CCDS6927.1; -.
RefSeq; NP_004869.1; NM_004878.4.
UniGene; Hs.146688; -.
PDB; 3DWW; EM; 3.50 A; A/B/C=1-152.
PDB; 4AL0; X-ray; 1.16 A; A=1-152.
PDB; 4AL1; X-ray; 1.95 A; A=1-152.
PDB; 4BPM; X-ray; 2.08 A; A=10-152.
PDB; 4WAB; X-ray; 2.70 A; A=10-151.
PDB; 4YK5; X-ray; 1.42 A; A=2-152.
PDB; 4YL0; X-ray; 1.52 A; A=5-152.
PDB; 4YL1; X-ray; 1.41 A; A=5-152.
PDB; 4YL3; X-ray; 1.41 A; A=5-152.
PDB; 5BQG; X-ray; 1.44 A; A=2-152.
PDB; 5BQH; X-ray; 1.60 A; A=2-152.
PDB; 5BQI; X-ray; 1.88 A; A=2-152.
PDB; 5K0I; X-ray; 1.30 A; A=2-152.
PDB; 5T36; X-ray; 1.40 A; A=2-152.
PDB; 5T37; X-ray; 1.76 A; A=2-152.
PDB; 5TL9; X-ray; 1.20 A; A=2-152.
PDBsum; 3DWW; -.
PDBsum; 4AL0; -.
PDBsum; 4AL1; -.
PDBsum; 4BPM; -.
PDBsum; 4WAB; -.
PDBsum; 4YK5; -.
PDBsum; 4YL0; -.
PDBsum; 4YL1; -.
PDBsum; 4YL3; -.
PDBsum; 5BQG; -.
PDBsum; 5BQH; -.
PDBsum; 5BQI; -.
PDBsum; 5K0I; -.
PDBsum; 5T36; -.
PDBsum; 5T37; -.
PDBsum; 5TL9; -.
ProteinModelPortal; O14684; -.
SMR; O14684; -.
BioGrid; 114912; 2.
IntAct; O14684; 1.
STRING; 9606.ENSP00000342385; -.
BindingDB; O14684; -.
ChEMBL; CHEMBL5658; -.
GuidetoPHARMACOLOGY; 1377; -.
SwissLipids; SLP:000001631; -.
PhosphoSitePlus; O14684; -.
SwissPalm; O14684; -.
BioMuta; PTGES; -.
EPD; O14684; -.
MaxQB; O14684; -.
PaxDb; O14684; -.
PeptideAtlas; O14684; -.
PRIDE; O14684; -.
TopDownProteomics; O14684; -.
Ensembl; ENST00000340607; ENSP00000342385; ENSG00000148344.
GeneID; 9536; -.
KEGG; hsa:9536; -.
UCSC; uc004byi.4; human.
CTD; 9536; -.
DisGeNET; 9536; -.
EuPathDB; HostDB:ENSG00000148344.10; -.
GeneCards; PTGES; -.
HGNC; HGNC:9599; PTGES.
HPA; HPA045064; -.
MIM; 605172; gene.
neXtProt; NX_O14684; -.
OpenTargets; ENSG00000148344; -.
PharmGKB; PA33948; -.
eggNOG; ENOG410IY81; Eukaryota.
eggNOG; ENOG4111VJG; LUCA.
GeneTree; ENSGT00390000011980; -.
HOGENOM; HOG000231759; -.
HOVERGEN; HBG052470; -.
InParanoid; O14684; -.
KO; K15729; -.
OMA; CFSMALQ; -.
OrthoDB; EOG091G14I4; -.
PhylomeDB; O14684; -.
TreeFam; TF105327; -.
BioCyc; MetaCyc:HS07518-MONOMER; -.
BRENDA; 5.3.99.3; 2681.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RK; O14684; -.
SIGNOR; O14684; -.
ChiTaRS; PTGES; human.
EvolutionaryTrace; O14684; -.
GeneWiki; PTGES; -.
GenomeRNAi; 9536; -.
PRO; PR:O14684; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148344; -.
CleanEx; HS_PTGES; -.
Genevisible; O14684; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
GO; GO:0050220; F:prostaglandin-E synthase activity; IDA:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; TAS:ProtInc.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
Gene3D; 1.20.120.550; -; 1.
InterPro; IPR023352; MAPEG-like_dom_sf.
InterPro; IPR001129; Membr-assoc_MAPEG.
Pfam; PF01124; MAPEG; 1.
SUPFAM; SSF161084; SSF161084; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Isomerase; Lipid biosynthesis;
Lipid metabolism; Membrane; Prostaglandin biosynthesis;
Prostaglandin metabolism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 152 Prostaglandin E synthase.
/FTId=PRO_0000217745.
TOPO_DOM 1 12 Lumenal.
TRANSMEM 13 41 Helical.
TOPO_DOM 42 60 Cytoplasmic.
TRANSMEM 61 90 Helical.
TOPO_DOM 91 95 Lumenal.
TRANSMEM 96 119 Helical.
TOPO_DOM 120 123 Cytoplasmic.
TRANSMEM 124 152 Helical.
REGION 28 38 Glutathione binding.
REGION 70 77 Glutathione binding.
REGION 110 113 Glutathione binding.
BINDING 117 117 Glutathione.
BINDING 126 126 Glutathione.
BINDING 130 130 Glutathione.
BINDING 134 134 Glutathione.
MUTAGEN 66 66 E->A: Reduces enzyme activity by 50%.
{ECO:0000269|PubMed:18682561}.
MUTAGEN 67 67 R->A: Loss of enzyme activity.
{ECO:0000269|PubMed:18682561}.
MUTAGEN 70 70 R->A: Slightly reduced enzyme activity.
{ECO:0000269|PubMed:18682561}.
MUTAGEN 72 72 H->A: Reduces enzyme activity by 70%.
{ECO:0000269|PubMed:18682561}.
MUTAGEN 110 110 R->A,S: Loss of enzyme activity.
{ECO:0000269|PubMed:18682561}.
MUTAGEN 117 117 Y->A: Loss of enzyme activity.
{ECO:0000269|PubMed:18682561}.
MUTAGEN 117 117 Y->F: No effect on enzyme activity.
{ECO:0000269|PubMed:18682561}.
CONFLICT 55 55 G -> GG (in Ref. 1; AAC39534).
{ECO:0000305}.
HELIX 6 9 {ECO:0000244|PDB:5TL9}.
HELIX 13 41 {ECO:0000244|PDB:4AL0}.
STRAND 44 46 {ECO:0000244|PDB:4AL0}.
HELIX 47 52 {ECO:0000244|PDB:4AL0}.
HELIX 56 58 {ECO:0000244|PDB:4AL0}.
HELIX 63 90 {ECO:0000244|PDB:4AL0}.
HELIX 96 118 {ECO:0000244|PDB:4AL0}.
HELIX 125 150 {ECO:0000244|PDB:4AL0}.
SEQUENCE 152 AA; 17102 MW; BF9B9ED81CA67A3D CRC64;
MPAHSLVMSS PALPAFLLCS TLLVIKMYVV AIITGQVRLR KKAFANPEDA LRHGGPQYCR
SDPDVERCLR AHRNDMETIY PFLFLGFVYS FLGPNPFVAW MHFLVFLVGR VAHTVAYLGK
LRAPIRSVTY TLAQLPCASM ALQILWEAAR HL


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E0167p ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
U0167p CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
E0167p ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
10-288-22051F Prostaglandin-H2 D-isomerase - EC 5.3.99.2; Lipocalin-type prostaglandin-D synthase; Glutathione-independent PGD synthetase; Prostaglandin-D2 synthase; PGD2 synthase; PGDS2; PGDS; Beta-trace protein; 0.1 mg
10-288-22051F Prostaglandin-H2 D-isomerase - EC 5.3.99.2; Lipocalin-type prostaglandin-D synthase; Glutathione-independent PGD synthetase; Prostaglandin-D2 synthase; PGD2 synthase; PGDS2; PGDS; Beta-trace protein; 0.05 mg
E0167h ELISA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandi 96T
E0167h ELISA kit Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostag 96T


 

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