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Information on EC 5.3.99.2 - Prostaglandin-D synthase and Organism(s) Mus musculus and UniProt Accession O09114

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EC Tree
     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.99 Other intramolecular oxidoreductases
                5.3.99.2 Prostaglandin-D synthase
IUBMB Comments
Brings about the opening of the epidioxy bridge. Some enzymes require glutathione.
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This record set is specific for:
Mus musculus
UNIPROT: O09114
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipocalin type prostaglandin D synthase
-
lipocalin-type PGD synthase
-
lipocalin-type prostaglandin d synthase
lipocalin-type prostaglandin D2 synthase
-
Prostaglandin-H2 D-isomerase
-
beta-Trace
-
-
-
-
Beta-trace protein
-
-
-
-
Glutathione-dependent PGD synthetase
-
-
-
-
Glutathione-independent PGD synthetase
-
-
-
-
H-PGDS
haematopoietic prostaglandin D synthase
-
Hematopoietic prostaglandin D synthase
hematopoietic prostaglandin D2 synthase
-
-
HPGDS
-
-
Isomerase, prostaglanin R2 D-
-
-
-
-
L-PGDS
L-prostaglandin D synthase
-
-
L-type prostaglandin synthase
-
-
lipocalin prostaglandin D synthase
-
-
lipocalin-prostaglandin D synthase
-
-
lipocalin-type prostaglandin d synthase
-
-
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
-
-
-
-
PTGDS
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
isomerization
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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 hide
52227-78-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
-
required
additional information
-
L-PGDS is glutathione-independent
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine
i.e. AT-56. Orally administered AT-56 below 30 mg/kg body weight decreases the prostaglandin D2 production to 40% in the brain of H-PGDS-deficient mice after a stab-wound injury in a dose-dependent manner without affecting the production of prostaglandin E2 and prostaglandin F2alpha, and also suppresses the accumulation of eosinophils and monocytes in the bronco-alveolar lavage fluid from the antigen-induced lung inflammation model of human L-PGDS-transgenic mice
retinoic acid
non-competitive
2-phenyl-5-(1H-pyrazol-3-yl)thiazole
-
-
4-benzhydryloxy-1-[3-(1H-tetrazol-5-yl)-propyl]piperidine
-
HQL-79
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
-
-
5-(3-cyanophenyl)-N-(diphenylmethyl)thiophene-2-carboxamide
-
-
5-(3-hydroxyphenyl)thiophene-2-carboxylic acid
-
-
5-amino-4-[[(3'-hydroxybiphenyl-4-yl)carbonyl]amino]-5-oxopentanoic acid
-
-
HQL-79
N-(1,6-diamino-1-oxohexan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-2,3'-dihydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3'-hydroxybiphenyl-3-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3,3'-dihydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-4-(1H-indol-4-yl)benzamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-4-(thiophen-2-yl)benzamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-6-(thiophen-2-yl)nicotinamide
-
selective H-PGDS inhibitor with low micromolar potency in the inhibition of the purified enzyme
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
-
N-(1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
-
N-(1-amino-3-cyclohexyl-1-oxopropan-2-yl)-5-(1H-indol-4-yl)thiophene-2-carboxamide
-
-
N-(1-amino-3-methyl-1-oxobutan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-4-methyl-1-oxopentan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
N-(2-amino-2-oxoethyl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
-
N-(diphenylmethyl)-2-(3-hydroxyphenyl)-1,3-thiazole-4-carboxamide
-
-
N-(diphenylmethyl)-2-phenyl-1,3-thiazole-4-carboxamide
-
-
N-(diphenylmethyl)-5-(1H-indol-4-yl)thiophene-2-carboxamide
-
-
N-(diphenylmethyl)-5-phenylthiophene-2-carboxamide
-
-
N-(diphenylmethyl)-5-[3-(hydroxymethyl)phenyl]thiophene-2-carboxamide
-
-
N-(diphenylmethyl)biphenyl-4-carboxamide
-
-
N-[4-methyl-3-({3-[(4-methylpiperazin-1-yl)methyl]benzoyl}amino)phenyl]-3-phenyl-1,2-thiazole-5-carboxamide
-
-
phenyl(thiophen-2-yl)methanone
-
-
SeCl4
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
guanidinium hydrochloride
Urea
1.6fold activation at 1M, inhibition above, less than 5% activity at 4 M urea
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.014
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
0.0005 - 0.0028
prostaglandin H2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37 - 0.95
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14.9
-
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184
434
-
wild-type, pH 8.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
of gut mucosa
Manually annotated by BRENDA team
-
auricle, ventricle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the incidence of preterm birth is significantly reduced to 40% in enzyme-deficient knockout mice
physiological function
malfunction
physiological function
-
requirement of the enzyme for maintenance of subcutaneous white adipose tissue function. The enzyme and peroxisome proliferator-activated receptor gamma2 coordinate to regulate carbohydrate and lipid metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTGDS_MOUSE
189
0
21066
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
L-PGDS
21000
L-PGDS bound to biliverdin
25000
-
SDS-PAGE
26000
-
determined by SDS-PAGE and Western Blot analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant DELTA1-24_C65A L-PGDS is crystallized in two different crystal forms representing the conformational change between the open and closed states of the cavity of the beta-barrel, the structures are determined to resolutions of 2.1 and 2.0 A
NMR solution structure, enzyme consists of an eight-stranded, antiparallel beta-barrel and a long alpha-helix associated with the outer surface of the barrel. The interior of the barrel forms a hydrophobic cavity containing two pockets. Prostaglandin H2 almost fully occupies hydrophilic pocket 1, in which C65 is located, and all-trans retinoic acid occupies hydrophilic pocket 2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C89A/C186A
mutant retains wild-type like activity and is stable
DELTA1-24_C65A
mutant
DELTA1-24_C65A L-PGDS
mutant, preserves a disulfide bond between Cys89 and Cys186
DELTA1-24_C65A+H111A
mutant
DELTA1-24_C65A+P110A
mutant
DELTA1-24_C65A+W54A
mutant
DELTA1-24_L-PGDS
mutant
DELTA1-24_L-PGDS+H111A
mutant
DELTA1-24_L-PGDS+H116A
mutant
DELTA1-24_L-PGDS+P110A
mutant
DELTA1-24_L-PGDS+S45A
mutant
DELTA1-24_L-PGDS+S45A/S81A
mutant
DELTA1-24_L-PGDS+S45A/T67A
mutant
DELTA1-24_L-PGDS+S45A/T67A/S81A
mutant
DELTA1-24_L-PGDS+S81A
mutant
DELTA1-24_L-PGDS+T67A
mutant
DELTA1-24_L-PGDS+T67A/S81A
mutant
DELTA1-24_L-PGDS+W45A
mutant
DELTA1-24_L-PGDS+W54A/H111A
mutant
W54A
mutant retains wild-type like activity and is stable
C65A
-
mutant binds all-trans-retinoic acid, bilirubin and biliverdin with high affinity. Radius of gyration is 19.4 A for the free enzyme, and it become compact after binding of these ligands
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
thermal unfolding is completely reversible at pH 4.0, with the presence of an intermediate state I between the native state N and the unfolded state U. Transition temperatures of the N-I and I-U transitions are 48.2 and 60.3°C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the DELTA1-24_C65A L-PGDS mutant is purified on a glutathione-Sepharose 4B column and incubated with thrombin to release the L-PGDS, the protein is further purified by gel filtration
GST-Prep column chromatography
-
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of cDNA in Escherichia coli
for expression in Escherichia coli BL21DE3 cells
for expression in Escherichia coli cells
expressed in 3T3-L1 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli C41(DE3) cells
-
expression as glutathione S-transferase fusion protein in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression levels of L-PGDS mRNA and protein are significantly increased after 14 days of hypoxia
-
L-PGDS knockout mice are generated
-
mice lacking PPARgamma2 have elevated levels of lipocalin prostaglandin D synthase expression in brown adipose tissue and subcutaneous white adipose tissue
-
the level of L-PGDS mRNA expression is increased 20fold in ulcerative colitis and increases with disease activity
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
complete recovery of activity after denaturation with 2 M guanidinium hydrochloride or 4 M urea
thermal unfolding is completely reversible at pH 4.0. Differential scanning calorimetry data show no concentration dependency. Presence of an intermediate state I between the native state N and the unfolded state U. Transition temperatures of the N-I and I-U transitions are 48.2 and 60.3°C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
orally administered AT-56, i.e. 4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine, below 30 mg/kg body weight decreases the prostaglandin D2 production to 40% in the brain of H-PGDS-deficient mice after a stab-wound injury in a dose-dependent manner without affecting the production of prostaglandin E2 and prostaglandin F2alpha, and also suppresses the accumulation of eosinophils and monocytes in the bronco-alveolar lavage fluid from the antigen-induced lung inflammation model of human L-PGDS-transgenic mice
medicine
nutrition
-
prostaglandin D2 stimulates food intake after intracerebroventricular administration in mice. Central administration of an antagonist or antisense oligodeoxynucleotide for the DP1 receptor remarkably decreases food intake, body weight and fat mass. Hypothalamic mRNA levels of lipocalin-type PGD synthase are up-regulated after fasting
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
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
Inui, T.; Ohkubo, T.; Urade, Y.; Hayaishi, O.
Enhancement of lipocalin-type prostaglandin D synthase enzyme activity by guanidine hydrochloride
Biochem. Biophys. Res. Commun.
266
641-646
1999
Homo sapiens, Mus musculus (O09114), Mus musculus
Manually annotated by BRENDA team
Zhu, H.; Ma, H.; Ni, H.; Ma, X.H.; Mills, N.; Yang, Z.M.
L-prostaglandin D synthase expression and regulation in mouse testis and epididymis during sexual maturation and testosterone treatment after castration
Endocrine
24
39-45
2004
Mus musculus
Manually annotated by BRENDA team
Park, J.M.; Kanaoka, Y.; Eguchi, N.; Aritake, K.; Grujic, S.; Materi, A.M.; Buslon, V.S.; Tippin, B.L.; Kwong, A.M.; Salido, E.; French, S.W.; Urade, Y.; Lin, H.J.
Hematopoietic prostaglandin D synthase suppresses intestinal adenomas in ApcMin/+ mice
Cancer Res.
67
881-889
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fujimori, K.; Inui, T.; Uodome, N.; Kadoyama, K.; Aritake, K.; Urade, Y.
Zebrafish and chicken lipocalin-type prostaglandin D synthase homologues: Conservation of mammalian gene structure and binding ability for lipophilic molecules, and difference in expression profile and enzyme activity
Gene
375
14-25
2006
Mus musculus, Gallus gallus (Q8QFM7), Gallus gallus, Danio rerio (Q8QGV4), Danio rerio
Manually annotated by BRENDA team
Shimamoto, S.; Yoshida, T.; Inui, T.; Gohda, K.; Kobayashi, Y.; Fujimori, K.; Tsurumura, T.; Aritake, K.; Urade, Y.; Ohkubo, T.
NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity
J. Biol. Chem.
282
31373-31379
2007
Mus musculus (O09114), Mus musculus
Manually annotated by BRENDA team
Joo, M.; Kwon, M.; Sadikot, R.T.; Kingsley, P.J.; Marnett, L.J.; Blackwell, T.S.; Peebles, R.S.; Urade, Y.; Christman, J.W.
Induction and function of lipocalin prostaglandin D synthase in host immunity
J. Immunol.
179
2565-2575
2007
Mus musculus
Manually annotated by BRENDA team
Mohri, I.; Taniike, M.; Okazaki, I.; Kagitani-Shimono, K.; Aritake, K.; Kanekiyo, T.; Yagi, T.; Takikita, S.; Kim, H.S.; Urade, Y.; Suzuki, K.
Lipocalin-type prostaglandin D synthase is up-regulated in oligodendrocytes in lysosomal storage diseases and binds gangliosides
J. Neurochem.
97
641-651
2006
Mus musculus
Manually annotated by BRENDA team
Qu, W.M.; Huang, Z.L.; Xu, X.H.; Aritake, K.; Eguchi, N.; Nambu, F.; Narumiya, S.; Urade, Y.; Hayaishi, O.
Lipocalin-type prostaglandin D synthase produces prostaglandin D2 involved in regulation of physiological sleep
Proc. Natl. Acad. Sci. USA
103
17949-17954
2006
Mus musculus
Manually annotated by BRENDA team
Trivedi, S.G.; Newson, J.; Rajakariar, R.; Jacques, T.S.; Hannon, R.; Kanaoka, Y.; Eguchi, N.; Colville-Nash, P.; Gilroy, D.W.
Essential role for hematopoietic prostaglandin D2 synthase in the control of delayed type hypersensitivity
Proc. Natl. Acad. Sci. USA
103
5179-5184
2006
Mus musculus
Manually annotated by BRENDA team
Iida, T.; Nishimura, S.; Mochizuki, M.; Uchiyama, S.; Ohkubo, T.; Urade, Y.; Tanaka, A.; Inui, T.
Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase
FEBS J.
275
233-241
2008
Mus musculus (O09114)
Manually annotated by BRENDA team
Ohinata, K.; Takagi, K.; Biyajima, K.; Fujiwara, Y.; Fukumoto, S.; Eguchi, N.; Urade, Y.; Asakawa, A.; Fujimiya, M.; Inui, A.; Yoshikawa, M.
Central prostaglandin D(2) stimulates food intake via the neuropeptide Y system in mice
FEBS Lett.
582
679-684
2008
Mus musculus
Manually annotated by BRENDA team
Inoue, K.; Yagi, N.; Urade, Y.; Inui, T.
Compact packing of lipocalin-type prostaglandin D synthase induced by binding of lipophilic ligands
J. Biochem.
145
169-175
2009
Mus musculus
Manually annotated by BRENDA team
Irikura, D.; Aritake, K.; Nagata, N.; Maruyama, T.; Shimamoto, S.; Urade, Y.
Biochemical, functional and pharmacological characterization of AT-56, an orally active and selective inhibitor of lipocalin-type prostaglandin d synthase
J. Biol. Chem.
284
7623-7630
2009
Homo sapiens, Mus musculus (O09114), Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Han, F.; Takeda, K.; Ishikawa, K.; Ono, M.; Date, F.; Yokoyama, S.; Furuyama, K.; Shinozawa, Y.; Urade, Y.; Shibahara, S.
Induction of lipocalin-type prostaglandin D synthase in mouse heart under hypoxemia
Biochem. Biophys. Res. Commun.
385
449-453
2009
Mus musculus
Manually annotated by BRENDA team
Kumasaka, T.; Aritake, K.; Ago, H.; Irikura, D.; Tsurumura, T.; Yamamoto, M.; Miyano, M.; Urade, Y.; Hayaishi, O.
Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase
J. Biol. Chem.
284
22344-22352
2009
Mus musculus (O09114), Mus musculus
Manually annotated by BRENDA team
Miyamoto, Y.; Nishimura, S.; Inoue, K.; Shimamoto, S.; Yoshida, T.; Fukuhara, A.; Yamada, M.; Urade, Y.; Yagi, N.; Ohkubo, T.; Inui, T.
Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR
J. Struct. Biol.
169
209-218
2010
Mus musculus (O09114)
Manually annotated by BRENDA team
Saleem, S.; Shah, Z.A.; Urade, Y.; Dore, S.
Lipocalin-prostaglandin D synthase is a critical beneficial factor in transient and permanent focal cerebral ischemia
Neuroscience
160
248-254
2009
Mus musculus
Manually annotated by BRENDA team
Liu, M.; Eguchi, N.; Yamasaki, Y.; Urade, Y.; Hattori, N.; Urabe, T.
Protective role of hematopoietic prostaglandin D synthase in transient focal cerebral ischemia in mice
Neuroscience
163
296-307
2009
Mus musculus
Manually annotated by BRENDA team
Hokari, R.; Kurihara, C.; Nagata, N.; Aritake, K.; Okada, Y.; Watanabe, C.; Komoto, S.; Nakamura, M.; Kawaguchi, A.; Nagao, S.; Urade, Y.; Miura, S.
Increased expression of lipocalin-type-prostaglandin D synthase in ulcerative colitis and exacerbating role in murine colitis
Am. J. Physiol. Gastrointest. Liver Physiol.
300
G401-G408
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chowdhury, A.A.; Hossain, M.S.; Rahman, M.S.; Nishimura, K.; Jisaka, M.; Nagaya, T.; Shono, F.; Yokota, K.
Sustained expression of lipocalin-type prostaglandin D synthase in the antisense direction positively regulates adipogenesis in cloned cultured preadipocytes
Biochem. Biophys. Res. Commun.
411
287-292
2011
Mus musculus
Manually annotated by BRENDA team
Mathurin, K.; Gallant, M.A.; Germain, P.; Allard-Chamard, H.; Brisson, J.; Iorio-Morin, C.; de Brum Fernandes, A.; Caron, M.G.; Laporte, S.A.; Parent, J.L.
An interaction between L-prostaglandin D synthase and arrestin increases PGD2 production
J. Biol. Chem.
286
2696-2706
2011
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Christ, A.N.; Labzin, L.; Bourne, G.T.; Fukunishi, H.; Weber, J.E.; Sweet, M.J.; Smythe, M.L.; Flanagan, J.U.
Development and characterization of new inhibitors of the human and mouse hematopoietic prostaglandin D2 synthases
J. Med. Chem.
53
5536-5548
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Virtue, S.; Masoodi, M.; Velagapudi, V.; Tan, C.Y.; Dale, M.; Suorti, T.; Slawik, M.; Blount, M.; Burling, K.; Campbell, M.; Eguchi, N.; Medina-Gomez, G.; Sethi, J.K.; Ore?i?, M.; Urade, Y.; Griffin, J.L.; Vidal-Puig, A.
Lipocalin prostaglandin D synthase and PPARgamma2 coordinate to regulate carbohydrate and lipid metabolism in vivo
PLoS ONE
7
e39512
2012
Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
Davani, D.; Kumar, S.; Palaia, T.; Hall, C.; Ragolia, L.
Lipocalin-type prostaglandin D2 synthase reduces glucagon secretion in alpha TC-1 clone 6 cells via the DP1 receptor
Biochem. Biophys. Rep.
4
224-227
2015
Mus musculus (O09114)
Manually annotated by BRENDA team
Virtue, S.; Masoodi, M.; de Weijer, B.A.; van Eijk, M.; Mok, C.Y.; Eiden, M.; Dale, M.; Pirraco, A.; Serlie, M.J.; Griffin, J.L.; Vidal-Puig, A.
Prostaglandin profiling reveals a role for haematopoietic prostaglandin D synthase in adipose tissue macrophage polarisation in mice and humans
Int. J. Obes.
39
1151-1160
2015
Homo sapiens (O60760), Homo sapiens, Mus musculus (Q9JHF7), Mus musculus
Manually annotated by BRENDA team
Omori, K.; Morikawa, T.; Kunita, A.; Nakamura, T.; Aritake, K.; Urade, Y.; Fukayama, M.; Murata, T.
Lipocalin-type prostaglandin D synthase-derived PGD2 attenuates malignant properties of tumor endothelial cells
J. Pathol.
244
84-96
2018
Mus musculus
Manually annotated by BRENDA team
Kumar, S.; Palaia, T.; Hall, C.; Ragolia, L.
Role of lipocalin-type prostaglandin D2 synthase (L-PGDS) and its metabolite, prostaglandin D2, in preterm birth
Prostaglandins Other Lipid Mediat.
118-119
28-33
2015
Mus musculus (O09114), Homo sapiens (P41222), Homo sapiens
Manually annotated by BRENDA team