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Information on EC 1.14.99.1 - prostaglandin-endoperoxide synthase and Organism(s) Bos taurus and UniProt Accession O62664
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1.14.99.1 prostaglandin-endoperoxide synthaseIUBMB Comments
This enzyme acts both as a dioxygenase and as a peroxidase.
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Word Map
- 1.14.99.1
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arachidonic
- indomethacin
- necrosis
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nsaid
- tnf
- lipopolysaccharide
- endothelial
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nonsteroidal
- celecoxib
- artery
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thromboxane
- aspirin
- lps
- lipoxygenase
- pain
- cardiovascular
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lps-induced
- platelet
-
prostanoids
- agonist
- gastrointestinal
- mapks
- phospholipase
- gastric
- carcinogenesis
-
eicosanoids
-
leukotriene
- ulcer
- arthritis
-
analgesic
- prostacyclin
- nf-kappab
-
lps-stimulated
- colorectal
- angiogenesis
- edema
- tnf-alpha
- ibuprofen
-
vasodilator
- il-1beta
- osteoarthritis
-
nonselective
- factor-alpha
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chemopreventive
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lipopolysaccharide-induced
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factor-kappa
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endothelium-dependent
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vasoconstriction
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l-name
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endothelium-derived
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cox-2, cyclooxygenase, cyclooxygenase-2, cox-1, cyclooxygenase 2, ptgs2, pghs-2, cyclooxygenase-1, prostaglandin synthetase, pghs-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(PG)H synthase
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cyclooxygenase
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-
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fatty acid cyclooxygenase
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-
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PG synthetase
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prostaglandin endoperoxide synthetase
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prostaglandin G/H synthase
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prostaglandin synthase
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prostaglandin synthase-2
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prostaglandin synthetase
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synthase, prostaglandin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen oxidoreductase
This enzyme acts both as a dioxygenase and as a peroxidase.
CAS REGISTRY NUMBER
COMMENTARY
39391-18-9
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9055-65-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
arachidonate + electron donor + O2
prostaglandin H2 + oxidized electron donor + H2O
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-
-
-
?
8,11,14-eicosatrienoic acid + O2
prostaglandin G1 + ?
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bis-dioxygenase activity, cyclooxygenase activity, presence of hematin
9alpha,11alpha-epidioxy-15(S)-hydroperoxy-13-trans-prostenoic acid
?
8,11,14-eicosatrienoic acid + O2
prostaglandin H1 + ?
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hydroperoxidase activity, presence of hematin and tryptophan
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
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either free or protein-bound heme is required for cyclooxygenase- and hydroperoxidase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Mercapto-9,11,15-trihydroxyprosta-5,13-diene
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inhibition of prostaglandin G1 synthesis
1-Mercapto-9-oxo-11,15-dihydroxyprosta-5,13-dione
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inhibition of prostaglandin G1 synthesis
6-[2,4-difluorophenoxy]-5-methyl-sulfonylamino-1-indanone
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CGP28238, an isozyme-2 specific inhibitor, 65% inhibition at 100 nM
9,11-Dihydroxy-15S-mercaptoprosta-5,13-dienoic acid
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or 15R-isomer, inhibition of prostaglandin G1 synthesis
ellagic acid
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at high concentration and in presence of cofactors inhibition, at low concentrations stimulation
Tannic acid
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at high concentration and in presence of cofactors inhibition, at low concentrations stimulation
additional information
-
effect of cofactor, enzyme and substrate concentration on inhibition by human serum, haptoglobin and albumin
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ellagic acid
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at high concentration and in presence of cofactors inhibition, at low concentrations stimulation
Tannic acid
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at high concentration and in presence of cofactors inhibition, at low concentrations stimulation
additional information
-
USF proteins are involved in the trans-activation of the PGH-2 promoter in granulosa cells
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additional information
the enzyme is induced by arachidonic acid up to 7.5-fold within 6 h, it is also induced by protein kinase C activators 4beta-PMA and PGF2alpha, all activation effects are blocked by PKC inhibitors, regulation, overview, protein kinase C induces PTGS2 independently of PPARs, i.e. peroxisome-proliferator-activated receptors
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additional information
-
the enzyme is induced by arachidonic acid up to 7.5-fold within 6 h, it is also induced by protein kinase C activators 4beta-PMA and PGF2alpha, all activation effects are blocked by PKC inhibitors, regulation, overview, protein kinase C induces PTGS2 independently of PPARs, i.e. peroxisome-proliferator-activated receptors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PTGS1 enzyme activity is higher in late corpora lutea and lower in regressive ones
PTGS2 increases from early to late corpora lutea and lowers in regressive ones
additional information
-
enzyme can be associated with endoplasmic reticulum, nuclear envelope and plasma membrane even within the same cell
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
enzyme can be associated with endoplasmic reticulum, nuclear envelope and plasma membrane even within the same cell
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
prostaglandin-endoperoxide synthases and nitric oxide synthases regulate the bovine corpea lutea life span mainly during the transition from the luteotrophic to the luteolytic phase
physiological function
prostaglandin-endoperoxide synthases and nitric oxide synthases regulate the bovine corpea lutea life span mainly during the transition from the luteotrophic to the luteolytic phase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PGH1_BOVIN
600
0
68805
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PGH-synthase immobilized on dry Opuntia imbricata trunk retains around 30-40% of initial activity, immobilized microsomes are able to catalyze several cycles of arachidonic acid transformation and are more stable than free enzyme solution upon storage at 4°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, Opuntia imbricata-immobilized enzyme, 2 days, 90-95% loss of initial activity
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4°C, Opuntia imbricata-immobilized enzyme, 24 h, 36-48% of initial activity is maintained after storage
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saeed, S.A.; Butt, N.M.; McDonald-Gibson, W.J.
The effect of ellagic acid and tannic acid on prostaglandin synthase activity in bovine seminal-vesicle homogenates
Biochem. Soc. Trans.
8
443
1981
Bos taurus
-
Denning-Kendall, P.A.; Saeed, S.A.
Effect of cofactor, enzyme and substrate concentration on inhibition of prostaglandin synthase of bull seminal vesicles by human serum, haptoglobin and albumin
Biochem. Soc. Trans.
9
379-380
1981
Bos taurus
-
Miyamoto, T.; Ogino, N.; Yamamoto, S.; Hayaishi, O.
Purification of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes
J. Biol. Chem.
251
2629-2636
1976
Bos taurus
Mizuno, K.; Yamamoto, S.; Lands, W.E.M.
Effects of non-steroidal anti-inflammatory drugs on fatty acid cyclooxygenase and prostaglandin hydroperoxidase activities
Prostaglandins
23
743-757
1982
Bos taurus
Smith, W.L.
Prostaglandin biosynthesis and its compartmentation in vascular smooth muscle and endothelial cells
Annu. Rev. Physiol.
48
251-262
1986
Bos taurus, Homo sapiens, Sus scrofa
Ohki, S.; Ogino, N.; Yamamoto, S.; Hayaishi, O.; Yamamoto, H.; Miyake, H.; Hayashi, M.
Inhibition of prostaglandin endoperoxide synthetase by thiol analogues of prostaglandin
Proc. Natl. Acad. Sci. USA
74
144-148
1977
Bos taurus
Friedman, Y.; Lang, M.; Burke, G.
Further characterization of bovine thyroid prostaglandin synthase
Biochim. Biophys. Acta
397
331-341
1975
Bos taurus
Liu, J.; Antaya, M.; Goff, A.K.; Boerboom, D.; Silversides, D.W.; Lussier, J.G.; Sirois, J.
Molecular characterization of bovine prostaglandin G/H synthase-2 and regulation in uterine stromal cells
Biol. Reprod.
64
983-991
2001
Bos taurus (O62698), Bos taurus
Doualla-Bell, F.; Guay, J.M.; Bourgoin, S.; Fortier, M.A.
Prostaglandin G/H synthase (PGHS)-2 expression in bovine myometrium: influence of steroid hormones and PGHS inhibitors
Biol. Reprod.
59
1433-1438
1998
Bos taurus
Sayasith, K.; Bouchard, N.; Sawadogo, M.; Lussier, J.G.; Sirois, J.
Molecular characterization and role of bovine upstream stimulatory factor 1 and 2 in the regulation of the prostaglandin G/H synthase-2 promoter in granulosa cells
J. Biol. Chem.
279
6327-6336
2004
Bos taurus
Sheldrick, E.L.; Derecka, K.; Marshall, E.; Chin, E.C.; Hodges, L.; Wathes, D.C.; Abayasekara, D.R.; Flint, A.P.
Peroxisome-proliferator-activated receptors and the control of levels of prostaglandin-endoperoxide synthase 2 by arachidonic acid in the bovine uterus
Biochem. J.
406
175-183
2007
Bos taurus (O62698), Bos taurus
Ilyina, A.; Huerta-Guel, P.; Martinez-Hernandez, J.; Rodriguez-Martinez, J.; Gorokhovsky, A.
Stability and activity of bovine prostaglandin H synthase immobilized on Opuntia imbricata (coyonoxtle)
J. Mol. Catal. B
51
1-9
2008
Bos taurus
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