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Information on EC 5.3.99.2 - Prostaglandin-D synthase and Organism(s) Rattus norvegicus and UniProt Accession P22057
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5.3.99.2 Prostaglandin-D synthaseIUBMB Comments
Brings about the opening of the epidioxy bridge. Some enzymes require glutathione.
Specify your search results
Word Map
- 5.3.99.2
-
cerebrospinal
-
arachidonic
- cox-2
- csf
-
cyclooxygenase
-
prostanoids
-
lipocalins
- indomethacin
- creatinine
- cystatin
-
mast
- sleep
-
glomerular
-
seminal
-
allergic
- leptomeninges
- aspirin
-
eicosanoids
-
thromboxane
-
leukotriene
-
nonsteroidal
- plexus
-
nsaid
- medicine
- synthase-1
-
subarachnoidal
-
1.14.99.1
-
ventrolateral
-
pgf2alpha
- transthyretin
-
preoptic
- rhinorrhea
-
endoperoxide
-
fistula
-
sleep-promoting
-
nephelometric
- beta2-microglobulin
- pghs-1
-
arachnoid
-
hydroperoxidase
-
sleep-wake
- analysis
- synthesis
- nutrition
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
l-pgds, prostaglandin synthase, beta-trace protein, ptgds, h-pgds, pgd synthase, prostaglandin d synthase, hpgds, lipocalin-type prostaglandin d synthase, prostaglandin d2 synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-Trace
-
-
-
-
Beta-trace protein
-
-
-
-
Glutathione-dependent PGD synthetase
-
-
-
-
Glutathione-independent PGD synthetase
-
-
-
-
H-PGDS
Hematopoietic prostaglandin D synthase
Isomerase, prostaglanin R2 D-
-
-
-
-
PGD synthase
-
-
-
-
PGD2 synthase
-
-
-
-
PGDS
-
-
-
-
PGDS2
-
-
-
-
PGH-PGD isomerase
-
-
-
-
Prostaglandin D synthase
-
-
-
-
Prostaglandin D2 synthase
Prostaglandin-D synthase
-
-
-
-
Prostaglandin-H2 D-isomerase
-
-
-
-
Prostaglandin-R-prostaglandin D isomerase
-
-
-
-
H-PGDS
-
-
-
-
Hematopoietic prostaglandin D synthase
-
-
-
-
Prostaglandin D2 synthase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase
Brings about the opening of the epidioxy bridge. Some enzymes require glutathione.
CAS REGISTRY NUMBER
COMMENTARY
52227-78-8
-
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
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + 2 GSH
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + GSSG + 2 H+
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + glutathione
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + glutathione
-
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
-
-
?
additional information
?
-
-
the enzyme binds all-trans-retinoic acid or 9-cis-retinoic acid and all-trans-retinal or 13-cis-retinal,but not all-trans-retinol
-
-
?
additional information
?
-
-
the enzyme belongs to the lipocalin family, a group of secretory proteins involved in the transport of small lipophilic ligands
-
-
?
additional information
?
-
-
the enzyme belongs to the lipocalin family, a group of secretory proteins involved in the transport of small lipophilic ligands
-
-
?
additional information
?
-
-
the hematopoietic prostaglandin D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells
-
-
?
additional information
?
-
-
the lipocalin-type prostaglandin D synthetase is responsible for the biosynthesis of prostaglandin D2 in the central nervous system and the genital organs and is secreted into the cerebrospinal fluid and the seminal plasma as beta-trace that has retinoid binding activity. It is likely that the enzyme is a bifunctional protein that acts as both retinoid transporter and prostaglandin D2-producing enzyme
-
-
?
additional information
?
-
-
glutathione-dependent enzyme is predicted to function somehow in immune and allergic responses
-
-
?
additional information
?
-
-
may be involved in both the maintenance and maturation of the CNS
-
-
?
additional information
?
-
-
the enzyme activity in rat brain exhibits a circadian fluctuation in parallel with the sleep/wake cycle
-
-
?
additional information
?
-
-
increased secretion of prostaglandin D synthase by interleukin-1beta is completely inhibited by prostaglandin E2
-
-
?
additional information
?
-
-
it is proposed that in wild-type vascular smooth muscle cells the enzyme retards cell cycle progression and migration, precluding hyperplasia of the tunica media, and that diabetic cells appear resistant to inhibitory effects of L-PGDS, which may help explain the increased atherosclerosis observed in diabetes
-
-
?
additional information
?
-
-
lipocalin-type prostaglandin synthase-D can stimulate glucose transport approximately 2fold as well as enhance insulin-stimulated glucose transport due to stimulation of insulin-responsive glucose transporter GLUT4 translocation to the plasma membrane. In response to lipocalin-type prostaglandin synthase-D, there is an increase in GLUT1 expression and an increase in hexokinase III expression
-
-
?
NATURAL SUBSTRATE
NATURAL 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
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + 2 GSH
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + GSSG + 2 H+
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + glutathione
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + glutathione
-
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
-
-
?
additional information
?
-
-
the enzyme belongs to the lipocalin family, a group of secretory proteins involved in the transport of small lipophilic ligands
-
-
?
additional information
?
-
-
the enzyme belongs to the lipocalin family, a group of secretory proteins involved in the transport of small lipophilic ligands
-
-
?
additional information
?
-
-
the hematopoietic prostaglandin D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells
-
-
?
additional information
?
-
-
the lipocalin-type prostaglandin D synthetase is responsible for the biosynthesis of prostaglandin D2 in the central nervous system and the genital organs and is secreted into the cerebrospinal fluid and the seminal plasma as beta-trace that has retinoid binding activity. It is likely that the enzyme is a bifunctional protein that acts as both retinoid transporter and prostaglandin D2-producing enzyme
-
-
?
additional information
?
-
-
glutathione-dependent enzyme is predicted to function somehow in immune and allergic responses
-
-
?
additional information
?
-
-
may be involved in both the maintenance and maturation of the CNS
-
-
?
additional information
?
-
-
the enzyme activity in rat brain exhibits a circadian fluctuation in parallel with the sleep/wake cycle
-
-
?
additional information
?
-
-
increased secretion of prostaglandin D synthase by interleukin-1beta is completely inhibited by prostaglandin E2
-
-
?
additional information
?
-
-
it is proposed that in wild-type vascular smooth muscle cells the enzyme retards cell cycle progression and migration, precluding hyperplasia of the tunica media, and that diabetic cells appear resistant to inhibitory effects of L-PGDS, which may help explain the increased atherosclerosis observed in diabetes
-
-
?
additional information
?
-
-
lipocalin-type prostaglandin synthase-D can stimulate glucose transport approximately 2fold as well as enhance insulin-stimulated glucose transport due to stimulation of insulin-responsive glucose transporter GLUT4 translocation to the plasma membrane. In response to lipocalin-type prostaglandin synthase-D, there is an increase in GLUT1 expression and an increase in hexokinase III expression
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Na2SeO3
-
systemic administration of the inhibitor has sleep-reducing potency
Se2+
-
organic selenocompounds have no effect, hexavalent selenium compound is ineffective. The inhibition requires the preincubation of the metal with sulfhydryl compounds such as dithiothreitol, reversal of inhibition by excess amount of dithiothreitol. The rat spleen enzyme is much less inhibited than the rat brain enzyme
Se4+
-
systemic administration of the inhibitor has sleep-reducing potency
Se4+
-
organic selenocompounds have no effect, hexavalent selenium compound is ineffective. The inhibition requires the preincubation of the metal with sulfhydryl compounds such as dithiothreitol, reversal of inhibition by excess amount of dithiothreitol. The rat spleen enzyme is much less inhibited than the rat brain enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
-
the hematopoietic prostaglandin D synthase is a glutathione S-transferase
glutathione
-
the glutathione-requiring enzyme is a member of the glutathione S-transferase family
glutathione
-
the spleen-type PGD synthase is a kind of glutathione S-transferase and therefore requires glutathione for activity
glutathione
-
glutathione-independent enzyme is detected in: brain, spinal cord, epididymis
glutathione
-
glutathione-requiring enzyme is detected in: spleen, thymus, bone marrow, digestive tract, mast cells, histiocytes, dendritic cells, Kupffer cells, Langerhans cells
glutathione
-
required for activity of spleen enzyme, not required for brain enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
0.5
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
3
1-chloro-2,4-dinitrobenzene
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
0.5
glutathione
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.7
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
5
1-chloro-2,4-dinitrobenzene
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
2
glutathione
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme is found in luminal and glandular epithelial cells and in stroma during late pregnancy
-
enzyme is found in luminal and glandular epithelial cells and in stroma during late pregnancy
-
of cyclic, pregnant, and pseudopregnant rats. Expression of prostaglandin D synthase or prostacyclin synthase are not influenced by the estrous cycle. Prostaglandion D synthase expression is high during early and maximal at the end of pregnancy. During pseudopregnancy, enzyme is increased in time-dependent manner and maximal at day 5
the enzyme is predominantly expressed in retinal pigment epithelium and actively accumulates in interphotoreceptor matrix
-
cellular localization of the enzyme changes postnatally. The enzyme is distributed in most neurons of the brain of 1-2 week old rats, whereas it is localized in the oligodendrocytes of adult animals
-
prostaglandin-H2 D-isomerase is produced in the membrane system surrounding the brain and is secreted into the cerebrospinal fluid to become beta-trace
-
the enzyme is synthesized within the epithelial cells of the iris and the ciliary body and is then secreted into the aqueous and vitreous humors, where it accumulates as an active enzyme
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PTGDS_RAT
189
0
21301
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A106S
-
creation of a new protein kinase C phosphorylation site, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity
C156L
loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity
C156Y
loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity
C186A
C65A
C65A/C89A/C186A
-
mutant is properly folded with well-defined tertiary structures
C89A/C186A
D51A
-
creation of new glycosylation site 1, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity
D78A
-
creation of new glycosylation site 2, no significant changes in enzyme activity or ability to induce apoptosis
K112E
retention of prostaglandin D synthase and glutathione S-transferase activity
K198E
retention of prostaglandin D synthase and glutathione S-transferase activity
L199F
retention of prostaglandin D synthase and glutathione S-transferase activity
R14E
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
R14K
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
W104I
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
Y152F
retention of prostaglandin D synthase and glutathione S-transferase activity
Y8F
complete loss of prostaglandin D synthase activity and glutathione S-transferase activity
C186A
-
no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid and retinoic acid. Urea-induced unfolding at 2.875 mol/l compared with 5.75 mol/l for wild-type
C65A
-
mutation of active site, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity
C65A
-
no significant change in conformation. Urea-induced unfolding at 5.125 mol/l compared with 5.75 mol/l for wild-type
C89A/C186A
-
mutant is properly folded with well-defined tertiary structures
C89A/C186A
-
no significant change in conformation. Decrease in stability and in dissociation constants for 8-anilino-1-naphthalenesulfonic acid. Urea-induced unfolding at 2.625 mol/l compared with 5.75 mol/l for wild-type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
oral pretreatment with the inhibitor EDJ300520 prevents the lipopolysaccharide-induced PGD2 increase in plasma and lungs
-
the synthesis of PGD2 is increased in plasma and lungs in response to systemic lipopolysaccharide injection
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
particle concentration fluorescence immunoassay for prostaglandin D synthase is suitable for determining the content of prostaglandin D synthetase in various regions of the rat CNS. The method allows to assay a large number of samples with reasonable sensitivity
medicine
-
prostaglandin D2 produced by hematopoietic prostaglandin D synthase contributes to lipopolysaccharide-induced fever
synthesis
-
optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimizu, T.; Yamamoto, S.; Hayaishi, O.
Purification of PGH-PDG isomerase from rat brain
Methods Enzymol.
86
73-77
1982
Cavia porcellus, Oryctolagus cuniculus, Felis catus, Platyrrhini, Mus musculus, Rattus norvegicus
Christ-Hazelhof, E.; Nugteren, D.H.
Isolation of PGH-PGS isomerase from rat spleen
Methods Enzymol.
86
77-84
1982
Rattus norvegicus
Shimizu, T.; Yamamoto, S.; Hayaishi, O.
Purification and properties of prostaglandin D synthetase from rat brain
J. Biol. Chem.
254
5222-5228
1979
Rattus norvegicus
Toh, H.; Kubodera, H.; Nakajima, N.; Sekiya, T.; Eguchi, N.; Tanaka, T.; Urade, Y.; Hayaishi, O.
Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins
Protein Eng.
9
1067-1082
1996
Ursus sp., Felis catus, Homo sapiens, Mus musculus, Rattus norvegicus, Xenopus sp.
Hayaishi, O.; Matsumura, H.; Urade, Y.
Prostaglandin D synthase is the key enzyme in the promotion of physiological sleep
J. Lipid Mediat. Cell Signal.
6
429-431
1993
Homo sapiens, Rattus norvegicus
Hayaishi, O.
Prostaglandin D synthase, beta-trace and sleep
Recent Adv. Prostaglandin Thromboxane Leukotriene Res.
1998
347-350
1998
Homo sapiens, Rattus norvegicus
-
Ujihara, M.; Tsuchida, S.; Satoh, K.; Sato, K.; Urade, Y.
Biochemical and immunological demonstration of prostaglandin D2, E2, and F2alpha formation from prostaglandin H2 by various rat glutathione S-transferase isoenzymes
Arch. Biochem. Biophys.
264
428-437
1988
Rattus norvegicus
Islam, F.; Watanabe, Y.; Morii, H.; Hayaishi, O.
Inhibition of rat brain prostaglandin D synthase by inorganic selenocompounds
Arch. Biochem. Biophys.
289
161-166
1991
Rattus norvegicus
Islam, F.; Urade, Y.; Watanabe, Y.; Hayaishi, O.
A particle concentration fluorescence immunoassay for prostaglandin D synthase in the rat central nervous system
Arch. Biochem. Biophys.
277
290-295
1990
Rattus norvegicus
Takahata, R.; Matsumura, H.; Kantha, S.S.; Kubo, E.; Kawase, K.; Sakai, T.; Hayaishi, O.
Intravenous administration of inorganic selenium compounds, inhibitors of prostaglandin D synthase, inhibits sleep in freely moving rats
Brain Res.
623
65-71
1993
Rattus norvegicus
Gerashchenko, D.Y.; Beuckmann, C.T.; Marcheselli, V.L.; Gordon, W.C.; Kanaoka, Y.; Eguchi, N.; Urade, Y.; Hayaishi, O.; Bazan, N.G.
Localization of lipocalin-type prostaglandin D synthase (beta-trace) in iris ciliary body, and eye fluids
Invest. Ophthalmol. Vis. Sci.
39
198-203
1998
Rattus norvegicus
Beuckmann, C.T.; Gordon, W.C.; Kanaoka, Y.; Eguchi, N.; Marcheselli, V.L.; Gerashchenko, D.Y.; Urade, Y.; Hayaishi, O.; Bazan, N.G.
Lipocalin-type prostaglandin D synthase (beta-trace) is located in pigment epithelial cells of rat retina and accumulates within interophotoreceptor matrix
J. Neurosci.
16
6119-6124
1996
Rattus norvegicus (P22057)
Matsumura, H.; Takahata, R.; Hayaishi, O.
Inhibition of sleep in rats by inorganic selenium compounds, inhibitors of prostaglandin D synthase
Proc. Natl. Acad. Sci. USA
88
9046-9050
1991
Rattus norvegicus
Tanaka, T.; Urade, Y.; Kimura, H.; Eguchi, N.; Nishikawa, A.; Hayaishi, O.
Lipocalin-type prostaglandin D synthase (beta-trace) is a newly recognized type of retinoid transporter
J. Biol. Chem.
272
15789-15795
1997
Rattus norvegicus
Meyer, D.J.; Thomas, M.
Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase
Biochem. J.
311
739-742
1995
Rattus norvegicus
Urade, Y.; Watanabe, K.; Hayaishi, O.
Prostaglandin D, E, and F synthases
J. Lipid Mediat. Cell Signal.
12
257-273
1995
Gallus gallus, Homo sapiens, Rattus norvegicus
Kanaoka, Y.; Ago, H.; Inagaki, E.; Nanayama, T.; Miyano, M.; Kikuno, R.; Eguchi, N.; Toh, H.; Urade, Y.; Hayaishi, O.
Cloning and crystal structure of hematopoietic prostaglandin D synthase
Cell
90
1085-1095
1997
Rattus norvegicus
Urade, Y.; Nagata, A.; Suzuki, Y.; Fujii, Y.; Hayaishi, O.
Primary structure of rat brain prostaglandin D synthetase deduced from cDNA sequence
J. Biol. Chem.
264
1041-1045
1989
Rattus norvegicus
Steinhoff, M.M.; Lee, L.H.; Jakschik, B.A.
Enzymatic formation of prostaglandin D2 by rat basophilic leukemia cells and normal rat mast cells
Biochim. Biophys. Acta
618
28-34
1980
Rattus norvegicus
Jowsey, I.R.; Thomson, A.M.; Flanagan, J.U.; Murdock, P.R.; Moore, G.B.T.; Meyer, D.J.; Murphy, G.J.; Smith, S.A.; Hayes, J.D.
Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases
Biochem. J.
359
507-516
2001
Homo sapiens, Rattus norvegicus (O35543)
Beuckmann, C.T.; Aoyagi, M.; Okazaki, I.; Hiroike, T.; Toh, H.; Hayaishi, O.; Urade, Y.
Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase
Biochemistry
38
8006-8013
1999
Rattus norvegicus
Samy, E.T.; Li, J.C.H.; Grima, J.; Lee, W.M.; Silvestrini, B.; Cheng, C.Y.
Sertoli cell prostaglandin D2 synthetase is a multifunctional molecule: its expression and regulation
Endocrinology
141
710-721
2000
Rattus norvegicus
Pinzar, E.; Miyano, M.; Kanaoka, Y.; Urade, Y.; Hayaishi, O.
Structural basis of hematopoietic prostaglandin D synthase activity elucidated by site-directed mutagenesis
J. Biol. Chem.
275
31239-31244
2000
Rattus norvegicus (O35543)
Ragolia, L.; Palaia, T.; Koutrouby, T.B.; Maesaka, J.K.
Inhibition of cell cycle progression and migration of vascular smooth muscle cells by prostaglandin D2 synthase: resistance in diabetic Goto-Kakizaki rats
Am. J. Physiol.
287
C1273-1281
2004
Rattus norvegicus
Nagasaka, T.; Hiraide, M.; Sugimoto, T.; Shindo, K.; Shiozawa, Z.; Yokota, S.
Localization of lipocaline-type prostaglandin D synthase in rat brain: immunoelectron microscopic study
Histochem. Cell Biol.
121
483-491
2004
Rattus norvegicus
Muraki, T.; Fujimori, K.; Ishizaka, M.; Ohe, Y.; Urade, Y.; Okajima, F.; Ishikawa, K.
Effects of interleukin-1beta and prostaglandin E2 on prostaglandin D synthase production in cultivated rat leptomeningeal cells
J. Cereb. Blood Flow Metab.
24
409-418
2004
Rattus norvegicus
Kengni, J.H.; St-Louis, I.; Parent, S.; Leblanc, V.; Shooner, C.; Asselin, E.
Regulation of prostaglandin D synthase and prostacyclin synthase in the endometrium of cyclic, pregnant, and pseudopregnant rats and their regulation by sex steroids
J. Endocrinol.
195
301-311
2007
Rattus norvegicus
Ragolia, L.; Hall, C.E.; Palaia, T.
Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis
Prostaglandins Other Lipid Mediat.
83
25-32
2007
Rattus norvegicus
Liu, J.; Lin, K.; Guo, C.; Gao, H.; Yao, Y.; Lin, D.
Expression and purification of cysteine mutation isoforms of rat lipocalin-type prostaglandin D synthase for nuclear magnetic resonance study
Acta Biochim. Biophys. Sin.
40
489-496
2008
Rattus norvegicus
Liu, J.; Guo, C.; Yao, Y.; Lin, D.
Effects of removing a conserved disulfide bond on the biological characteristics of rat lipocalin-type prostaglandin D synthase
Biochimie
90
1637-1646
2008
Rattus norvegicus
Ragolia, L.; Hall, C.E.; Palaia, T.
Lipocalin-type prostaglandin D(2) synthase stimulates glucose transport via enhanced GLUT4 translocation
Prostaglandins Other Lipid Mediat.
87
34-41
2008
Mus musculus, Rattus norvegicus
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