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Information on EC 5.3.99.2 - Prostaglandin-D synthase and Organism(s) Homo sapiens and UniProt Accession P41222
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5.3.99.2 Prostaglandin-D synthaseIUBMB Comments
Brings about the opening of the epidioxy bridge. Some enzymes require glutathione.
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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: Homo sapiens
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
L-PGDS
-
lipocalin-type prostaglandin d 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
Isomerase, prostaglanin R2 D-
-
-
-
-
L-PGDS
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
-
-
-
-
Beta-trace protein
-
-
-
-
H-PGDS
-
-
-
-
Hematopoietic prostaglandin D synthase
-
-
-
-
PGD synthase
-
-
-
-
PGDS
-
-
-
-
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
9,11-epoxymethano-prostaglandin H2
9,11-epoxymethano-prostaglandin D2
substrate analogue U44069
product analogue 12415
-
?
(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 + glutathione
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + glutathione
-
-
?
(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
i.e. prostaglandin H2, PGH2
i.e. prostaglandin D2, PGD2
-
?
(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
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
-
-
-
-
?
additional information
?
-
prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology
-
-
?
additional information
?
-
lipocalin-type prostaglandin D synthase is a dual-functional protein, acting as a prostaglandin D2-producing enzyme and a lipid transporter, the enzyme can bind a wide variety of lipophilic molecules
-
-
?
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
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + glutathione
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + glutathione
-
-
?
(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
-
-
-
?
Prostaglandin H2
Prostaglandin D2
-
-
-
-
?
additional information
?
-
prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology
-
-
?
additional information
?
-
lipocalin-type prostaglandin D synthase is a dual-functional protein, acting as a prostaglandin D2-producing enzyme and a lipid transporter, the enzyme can bind a wide variety of lipophilic molecules
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
-
KM for glutathione is decreased from 0.0006 mM in presence of EDTA to 0.00014 mM in presence of Mg2+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
half maximal effective concentration at 0.4 mM, 1.5fold increase in activity
Mg2+
Mg2+
half maximal effective concentration at 0.05 mM, 1.5fold increase in activity, Mg2+ increases the affinity for glutathione
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-methoxy-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl][2,4'-bipyridine]-5-carboxamide
-
2'-oxo-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]-1',2'-dihydro[2,4'-bipyridine]-5-carboxamide
-
2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride
-
IC50: 0.0362 mM in presence of EDTA, 0.0981 in presence of Mg2+
3-(3-cyclopropyl-1H-pyrazol-4-yl)-N-ethyl-5,7-dihydro-6H-pyrrolo[3,4-b]pyridine-6-carboxamide
-
-
4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine
-
i.e. AT-56, inhibits the activity of lipocalin-type prostaglandin-D synthase in a concentration-dependent manner, but does not affect the activities of hematopoietic prostaglandin-D synthase, cyclooxygenase-1 and -2, and microsomal PGE synthase-1. AT-56 inhibits the lipocalin-type prostaglandin-D synthase activity in a competitive manner against the substrate prostaglandin H2 but does not inhibit the binding of 13-cis-retinoic acid. AT-56 occupies the catalytic pocket, but not the retinoid-binding pocket, of lipocalin-type prostaglandin-D synthase
6'-oxo-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]-1',6'-dihydro[2,2'-bipyridine]-5-carboxamide
-
6'-oxo-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]-1',6'-dihydro[2,3'-bipyridine]-5-carboxamide
-
6-(3-fluorophenyl)-N-[1-(1-methyl-1H-tetrazol-5-yl)piperidin-4-yl]pyridine-3-carboxamide
-
-
6-(3-methoxyphenyl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-(3-oxopiperazin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-(dimethylamino)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-(morpholin-4-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-(piperazin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-(piperidin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-(pyrrolidin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
6-phenoxy-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
AT-56
-
inhibition of prostaglandin-D synthase, resulting in suppression of prostaglandin D2 production under serum-starved conditions
erythrosine sodium
i.e. disodium 2-(2,4,5,7-tetraiodo-6-oxido-3-oxo-3H-xanthen-9-yl)benzoate
iopanic acid
linear competitive inhibitor, i.e. 2-[(3-amino-2,4,6-triiodophenyl)methyl]butanoic acid
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-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
N-(5-fluoro-3-methyl-1H-indol-1-yl)-2-(pyridin-2-yl)pyrimidine-5-carboxamide
-
-
N-([4-[5-(2-hydroxypropan-2-yl)-1,2,4-oxadiazol-3-yl]phenyl]methyl)-2-phenylpyrimidine-5-carboxamide
-
N-cyclopentyl-3-(3-cyclopropyl-1H-pyrazol-4-yl)-5,7-dihydro-6H-pyrrolo[3,4-b]pyridine-6-carboxamide
-
66% inhibition at 10 nM
N-[4-methyl-3-({3-[(4-methylpiperazin-1-yl)methyl]benzoyl}amino)phenyl]-3-phenyl-1,2-thiazole-5-carboxamide
-
-
N-[4-methyl-3-[([3-[(4-methylpiperazin-1-yl)methyl]phenyl]carbonyl)amino]phenyl]-3-phenylisothiazole-5-carboxamide
-
N-[5-(1H-indol-4-yl)pyridin-3-yl]-2-(1-methyl-1H-imidazol-5-yl)acetamide
-
N-[5-(1H-indol-4-yl)pyridin-3-yl]-5-oxopyrrolidine-2-carboxamide (incorrect configuration definition!)
-
tranilast
i.e. 2-{[(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoyl]amino}benzoic acid
2-phenyl-5-(1H-pyrazol-3-yl)-1,3-thiazole
inhibitor generated by fragment-based drug design, crystallographic data
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
-
-
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
-
6-(3-fluorophenyl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
-
6-(3-fluorophenyl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
-
Ethacrynic acid
i.e. [2,3-dichloro-4-(2-methylidenebutanoyl)phenoxy]acetic acid
HQL-79
-
i.e. 4-benzhydryloxy-1-[3-(1H-tetrazol-5-yl)-propyl]-piperidine, H-PGDS-specific inhibitor
N-benzhydryl-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
low micromolar potency in the inhibition of the purified enzyme
additional information
the lipid transporter activity of the enzyme is competitively inhibited by pamitate, stearate and arachnoate
-
additional information
-
the lipid transporter activity of the enzyme is competitively inhibited by pamitate, stearate and arachnoate
-
additional information
-
not inhibited by oleamide, palmitoylethanolamide, oleoylethanolamide, prostamide F2alpha, N-arachidonoylethanolamine/anandamide, and 2-arachidonoylglycerol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arrestin-3
-
arrestin-3 promotes prostaglandin D2 production by L-PGDS in vitro. Incubation of L-PGDS with arrestin-3 amino acids 56-100 enhances prostaglandin D2 production by 145%
-
guanidinium hydrochloride
-
activation between 100-1000 mM, 3fold activation at 500 mM guanidinium hydrochloride, inhibition above 500 mM, less than 5% activity at 3 M
Urea
-
activation between 250-2000 mM, 1.7fold activation at 1 M urea, inhibition above 500 mM, less than 5% activity at 4 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0102
prostaglandin H2
mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0123
prostaglandin H2
mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0127
prostaglandin H2
mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0138
prostaglandin H2
wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0154
prostaglandin H2
mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0161
prostaglandin H2
mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0202
prostaglandin H2
mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0204
prostaglandin H2
mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0245
prostaglandin H2
mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0252
prostaglandin H2
mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0325
prostaglandin H2
mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.0328
prostaglandin H2
mutant enzyme L79A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.014
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
pH 8.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
prostaglandin H2
mutant enzyme L79A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.63
prostaglandin H2
mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.81
prostaglandin H2
mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
0.87
prostaglandin H2
mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
2.23
prostaglandin H2
mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
2.24
prostaglandin H2
mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
2.4
prostaglandin H2
mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
2.64
prostaglandin H2
wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
2.91
prostaglandin H2
mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
3.67
prostaglandin H2
mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
5.73
prostaglandin H2
mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
5.84
prostaglandin H2
mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110
prostaglandin H2
mutant enzyme L79A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
1170
prostaglandin H2
mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
1890
prostaglandin H2
mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
2120
prostaglandin H2
mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
6570
prostaglandin H2
mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
6660
prostaglandin H2
mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
8940
prostaglandin H2
mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
9420
prostaglandin H2
mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
11490
prostaglandin H2
wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
14290
prostaglandin H2
mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
24840
prostaglandin H2
mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
27050
prostaglandin H2
mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.075
4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine
-
pH 8.0
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7
2'-oxo-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]-1',2'-dihydro[2,4'-bipyridine]-5-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.0362
2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride
Homo sapiens
-
IC50: 0.0362 mM in presence of EDTA, 0.0981 in presence of Mg2+
0.0007
2-phenyl-5-(1H-pyrazol-3-yl)thiazole
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.00004
3-(3-cyclopropyl-1H-pyrazol-4-yl)-N-ethyl-5,7-dihydro-6H-pyrrolo[3,4-b]pyridine-6-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.017
3-(3-cyclopropyl-1H-pyrazol-4-yl)pyridine
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-acetamido-N-[5-(1H-indol-4-yl)pyridin-3-yl]propanamide
Homo sapiens
at 37°C, pH not specified in the publication
0.00018
4-(dimethylamino)-N-[5-(1H-indol-4-yl)pyridin-3-yl]butanamide
Homo sapiens
at 37°C, pH not specified in the publication
0.003
4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine
Homo sapiens
-
inhibition of enzyme in lipocalin-type prostaglandin-D synthase-expressing TE-671 cells after stimulation with Ca2+-ionophore A23187
0.000138 - 0.0014
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
0.0019
5-(3-aminophenyl)-N-benzhydrylthiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.023
5-amino-4-[[(3'-hydroxybiphenyl-4-yl)carbonyl]amino]-5-oxopentanoic acid
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.000071
6'-oxo-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]-1',6'-dihydro[2,2'-bipyridine]-5-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.00006
6-(3-methoxyphenyl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.00059
6-(3-oxopiperazin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.00032
6-(morpholin-4-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.000048
6-(piperidin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.00023
6-(pyrrolidin-1-yl)-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.000031
6-phenoxy-N-[1-(2,2,2-trifluoroethyl)piperidin-4-yl]pyridine-3-carboxamide
Homo sapiens
at 37°C, pH not specified in the publication
0.0046
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0248
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3,3'-dihydroxybiphenyl-4-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0037
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0012
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-6-(thiophen-2-yl)nicotinamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.001
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0021
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0013
N-(1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0071
N-(1-amino-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.008
N-(2-amino-2-oxoethyl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0108
N-(diphenylmethyl)-2-(3-hydroxyphenyl)-1,3-thiazole-4-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0007
N-benzhydryl-5-(3-hydroxyphenyl)thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
0.0085
N-cyclopentyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
N-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000075
N-[4-methyl-3-[([3-[(4-methylpiperazin-1-yl)methyl]phenyl]carbonyl)amino]phenyl]-3-phenylisothiazole-5-carboxamide
Homo sapiens
37°C
0.0012
N-[5-(1H-indol-4-yl)pyridin-3-yl]-2-(1-methyl-1H-imidazol-5-yl)acetamide
Homo sapiens
at 37°C, pH not specified in the publication
0.000043
N-[5-(1H-indol-4-yl)pyridin-3-yl]-2-(1H-tetrazol-1-yl)acetamide
Homo sapiens
at 37°C, pH not specified in the publication
0.00013
N-[5-(1H-indol-4-yl)pyridin-3-yl]-3-(piperidin-1-yl)propanamide
Homo sapiens
at 37°C, pH not specified in the publication
0.000026
N-[5-(1H-indol-4-yl)pyridin-3-yl]-3-(pyridin-3-yl)propanamide
Homo sapiens
at 37°C, pH not specified in the publication
0.000035
N-[5-(1H-indol-4-yl)pyridin-3-yl]-5-oxopyrrolidine-2-carboxamide (incorrect configuration definition!)
Homo sapiens
at 37°C, pH not specified in the publication
0.000032
N-[5-(1H-indol-4-yl)pyridin-3-yl]propanamide
Homo sapiens
at 37°C, pH not specified in the publication
0.000138
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
Homo sapiens
37°C
0.0014
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
isolation of several enzyme isoforms with pI values ranging from 4.0 to 7.2, with identical molecular masses around 28000 Da
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
lipocalin-type prostaglandin D synthase (beta-trace) is upregulated in the alphaB-crystallin-positive astrocytes in the chronic multiple sclerosis
-
L-PGDS is constitutively expressed in the epithelium of the glandular base
-
precursor cells of platelets, CMK cells, Dami cells. The activity is undetectable in platelets and appears during differentiation of megakaryoblasts to megakaryocytes
-
CMK86, CMK, CMK11-5 and Dami cells. Expression level is highest in CMK86 cells and is less in CMK cells, CMK11-5 cells and Dami cells in that order
-
in normal mucosa the enzyme is only detected in few resident mast cells. In the nasal mucosa of subjects suffering from polyposis the enzyme is detected in mast cells and other large infiltrating inflammatory cells
-
lipocalin-type prostaglandin D synthase (beta-trace) is upregulated in the alphaB-crystallin-positive oligodendrocytes in the chronic multiple sclerosis
-
human ovarian cancer cells. Prostaglandin synthase and testicular factor SOX9 are expressed at both RNA and protein levels in different types of ovarian tumors, while treatment of these cells with prostaglandin D2 can inhibit their growth and induce apoptosis
-
determination of the correlation between content of enzyme in seminal plasma and on the surface of sperm
-
under serum-starved conditions, prostaglandin D2 production is induced through transcriptional activation of cyclooxygenase COX-2 and lipocalin-type PGD synthase via upstream stimulatory factor USF1
synthesized mainly at the rough endoplasmic reticulum membrane of arachnoid cells, chorioid plexus cells and oligodendrocytes, and then is secreted into the cerebrospinal fluid as a second major protein
qualitative and quantitative fluctuations of prostaglandin D synthase isoforms from cerebrospinal fluid reflect both major and subtle brain pathophysiology
-
in normal mucosa the enzyme is only detected in few resident mast cells. In the nasal mucosa of subjects suffering from polyposis the enzyme is detected in mast cells and other large infiltrating inflammatory cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
perinuclear L-type prostaglandin synthase/arrestin-3 co-localization is observed in prostaglandin D2-producing MG-63 cells
the N-terminal 22-amino acid residues correspond to the putative secretion signal peptide of the enzyme
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
malfunction
-
co-localization of arrestin-3 with L-PGDS is drastically reduced in MG-63 cells when L-PGDS activity is inhibited
physiological function
additional information
physiological function
lipocalin prostaglandin D synthase regulates synthesis of an important inflammatory and signaling mediator, prostaglandin D2
physiological function
lipocalin-type prostaglandin D synthase is a multi-functional protein, acting as a prostaglandin D2-producing enzyme and a lipid-transporter. It is involved in the biosynthesis of prostaglandin D2, acting as an endogenous somnogen and allergy response. Binding mechanism of small lipophilic molecules by the enzyme functioning as lipid transporter, e.g. of biliverdin, all-trans-retinoic acid, L-thyroxine (T4), progesterone, and genistein, thermodynamic parameters, overview. The enzme shows broad ligand selectivity for small lipophilic molecules, it binds heme metabolites with significantly higher affinity than other small lipophilic ligands
physiological function
the enzyme shows a protective effect on H2O2-induced apoptosis in neuroblastoma cell line SH-SY5Y, the enzyme level is highly associated with H2O2-induced apoptosis. It protects against neuronal cell death by scavenging reactive oxygen species without losing its ligand-binding function. H2O2 reacts with the thiol of Cys65 of the enzyme
physiological function
the enzyme plays a role in lipopolysaccharide-induced preterm birth
physiological function
-
L-PGDS may fine-tune the all-trans retinoic acid signaling in melanocytes
physiological function
-
the enzyme has dual functional roles as a prostaglandin D2-synthesizing enzyme and as an extracellular transporter for diverse lipophilic compounds in the cerebrospinal fluid
additional information
analysis of enzyme structure in complex with substrate analogue U44069, 9,11-epoxymethano-PGH2, and in ligand-free form. The catalytic Cys 65 thiol group occurs in two different conformations, each making a distinct hydrogen bond network to neighboring residues, mechanism of the cysteine nucleophile activation, and modelling of dynamics of protein-substrate and protein-product interactions, overview
additional information
-
analysis of enzyme structure in complex with substrate analogue U44069, 9,11-epoxymethano-PGH2, and in ligand-free form. The catalytic Cys 65 thiol group occurs in two different conformations, each making a distinct hydrogen bond network to neighboring residues, mechanism of the cysteine nucleophile activation, and modelling of dynamics of protein-substrate and protein-product interactions, overview
additional information
binding of various lipophilic ligands in the hydrophobic cavity of lipocalin-type prostaglandin D synthase, i.e. hemin, biliverdin, and bilirubin, retinoids (all-trans and 9-cis retinoic acids), thyroids, steroids (progesterone, testosterone, and corticosterone), flavonoids (genistein, naringenin, and daidzein), the substrate PGH2 analogue U46619, and the fluorescence probe TNS, buffer-independent thermodynamic parameters, overview. The broad binding capability of the enzyme for ligands is realized by hydrophilic interactions delicately tuned by enthalpy-entropy compensation using combined effects of hydrophilic and hydrophobic interactions
additional information
-
binding of various lipophilic ligands in the hydrophobic cavity of lipocalin-type prostaglandin D synthase, i.e. hemin, biliverdin, and bilirubin, retinoids (all-trans and 9-cis retinoic acids), thyroids, steroids (progesterone, testosterone, and corticosterone), flavonoids (genistein, naringenin, and daidzein), the substrate PGH2 analogue U46619, and the fluorescence probe TNS, buffer-independent thermodynamic parameters, overview. The broad binding capability of the enzyme for ligands is realized by hydrophilic interactions delicately tuned by enthalpy-entropy compensation using combined effects of hydrophilic and hydrophobic interactions
additional information
structure homology modelling using the solution structure of the C65A mouse L-PGDS, PDB code 2RQ0, as template, overview
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_HUMAN
190
0
21029
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
28000
-
x * 28000, SDS-PAGE, molecular mass is the same for several isoforms showing pI values from 4.2 to 7.0
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 28000, SDS-PAGE, molecular mass is the same for several isoforms showing pI values from 4.2 to 7.0
additional information
analysis of enzyme structure in complex with substrate analogue U44069, 9,11-epoxymethano-PGH2, and in ligand-free form, NMR analysis, overview. The enzyme overall structure shows the classical lipocalin fold comprising an eight-stranded beta-barrel with two alpha-helices. The ligand-bound and the ligand-free structures differ only in the Omega loop conformationss
additional information
-
analysis of enzyme structure in complex with substrate analogue U44069, 9,11-epoxymethano-PGH2, and in ligand-free form, NMR analysis, overview. The enzyme overall structure shows the classical lipocalin fold comprising an eight-stranded beta-barrel with two alpha-helices. The ligand-bound and the ligand-free structures differ only in the Omega loop conformationss
additional information
structure homology modelling using the solution structure of the C65A mouse L-PGDS, PDB code 2RQ0, as template, overview
additional information
three-dimensional structure of the enzyme and its hydrophobic cavaity, overview. The secondary structure elements of the enzyme comprise nine beta-strands and four alpha-helices
additional information
-
three-dimensional structure of the enzyme and its hydrophobic cavaity, overview. The secondary structure elements of the enzyme comprise nine beta-strands and four alpha-helices
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
the two N-glycosylation sites are almost quantitatively occupied by carbohydrate. Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures, partially sialylated with alpha2-3- and/or alpha2-6-linked N-acetylneuraminic acid, that are almost quantitatively alpha1-6 fucosylated at the proximal N-acetylglucosamine. About 70% of the molecules contain a bisecting N-acetylglucosamine. Agalacto-structures as well as those with a peripheral fucose are also present
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant C65A in complex with oleic acid and palmitoleic acid, hanging drop vapor diffusion method, using 0.1 M citric acid (pH 4.0) and 1.7 M ammonium sulfate
mutant enzymes C65A/K59A, C65A, C65A/W54F, C65A/W112F and C65A/W54F/W112F hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 30% (w/v) PEG 4000
purified His-tagged recombinant enzyme, in complex with 9,11-epoxymethano prostaglandin H2, hanging drop vapor diffusion method, condition A: 0.1 M potassium thiocyanate and 30% PEG-MME 2000 in 1:1 protein-reservoir ratio, 5 days, 4°C, condition B: 1.4 M tri-sodium citrate, pH 6.5, using a similar method except in 2:1 protein-reservoir ratio. Micro-crystals from condition A are used to seed crystallization of ligand-free L-PGDS in the same condition but in the absence of SA U44069. Cryoprotection of condition A crystals using reservoir with 25% glycerol added, while crystals from condition B are cryo-protected with 1.6 M tri-sodium citrate solution. X-ray diffraction structure analysis at 1.88-2.09 A resolution
crystals of H-PGDS are first grown by hanging-drop vapor diffusion method with PEG6000 as the precipitant at 20°C in the presence of 5 mM Mg2+ and the native crystals are then soaked in the precipitant solution with a saturating concentration of 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride for 2 weeks. Structure of the enzyme complexed with 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride at 1.9 A resolution in the presence of Mg2+. The styryl group of the inhibitor penetrates to the bottom of the active site cleft, and the tetrazole ring is stabilized by the stacking interaction with TRp104, inducing large movement around the alpha5-helix, which causes the space group of the complex crystal to change from P2(1) to P1 upon binding of 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride
-
H-PGDS is crystallized in a microgravity environment at 20°C, using 30% (w/v) PEG 6000, 10 mM dithiothreitol, 10 mM glutathione, 1% (v/v) dioxane and 1 mM magnesium chloride in 50 mM Tris-HCl pH 8.4
-
hanging drop vapor diffusion method, using 0.1 M MES/NaOH at pH 6.5, 0.005 M MgCl2 and 24% (w/v) PEG 3350
-
macro-seeding using a solution containing 14% polyethylene glycol 6000, 50 mM Tris-HCl, pH 8.4, 5 mM reduced glutathione, 5 mM dithiothreitol, 2.5 mM CaCl2 or MgCl2 and 1% dioxane, structure resolution at 1.8 A
the structure of H-PGDS in complex with GSH and nocodazole is solved to a resolution of 1.9 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C65A/C167A
W43F/C65A/C167A
site-directed mutagenesis, the W43F mutant cannot be purified owing to the inclusion body formation of protein
W54F/C65A/W112F/C167A
site-directed mutagenesis, the mutant still provides the disulfide bond between Cys89 and Cys186
D96N
very high basal activity, no activation in the presence of Ca2+ or Mg2+
additional information
C65A/C167A
site-directed mutagenesis, the mutant still provides the disulfide bond between Cys89 and Cys186
C65A/C167A
site-directed mutagenesis, the mutation limits incorrect intra- and intermolecular disulfide bonds and protein aggregation during recombinant enzyme expression and purification
additional information
knockdown of the enzyme expression by siRNA in SH-SY5Y cells, two different siRNAs
additional information
-
transgenic expression of hematopoitic prostaglandin synthase in ApcMin/+ mice have 80% fewer intestinal adenomas
additional information
-
apoptosis induced by chemotherapeutics paclitaxel, cisplatin and 5-fluorouracil is prevented by siRNA targeting lipocalin-type prostaglandin synthase-D
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
purified recombinant enzyme, sodium phosphate, pH 7.0, containing 5% v/v ethanol, stable up to
65 - 90
purified recombinant enzyme, thermal unfolding in the absence and presence of small lipophilic ligands, two-state unfolding transition, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose column chromatography and Superdex 75 gel filtration
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant GST-tagged truncated enzyme mutant C65A/C167A from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, and dialysis
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, gel filtration, and dialysis
by ammonium sulfate precipitation, and on a GSH Sepharose 4B and a Superdex 75 pg column
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta BL21(DE3)
expression of GST-tagged enzyme mutant C65A/C167A, with truncated N-terminal 22-amino acid residues corresponding to the putative secretion signal peptide, in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
into the vectors pUB6/V5-His and pIRESneo, cDNA of positions 76-648 is cloned into the vector pGEM-T Easy
-
the coding region of human L-PGDS is sub-cloned into pCR-Script Amp SK+ vector
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L-PGDS, but not H-PGDS, is induced on fibroblasts close to infiltrating cells in the Helicobacter pylori-infected gastric mucosa
-
the level of L-PGDS mRNA expression is increased 20fold in ulcerative colitis and increases with disease activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
elevated enzyme levels in the cervicovaginal secretions of women are a potential biomarker for preterm birth
analysis
-
PGD synthase is a useful marker for identifying the differentiation stage of human megakaryocytic cells
medicine
medicine
-
the enzyme may be a potential marker that may aid in the differential diagnosis of obstructive and non-obstructive azoospermia
medicine
-
hematopoitic prostaglandin synthase controls an inhibitory effect on intestinal tumours
medicine
-
lipocalin-type prostaglandin D synthase may have the ability to improve progressive motility of sperm and, in seminal plasma and on sperm surface, may impact male fertility in the female reproductive tract
medicine
-
prostaglandin synthase and testicular factor SOX9 are expressed at both RNA and protein levels in different types of ovarian tumors, while treatment of these cells with prostaglandin D2 can inhibit their growth and induce apoptosis
medicine
-
apoptosis induced by chemotherapeutics paclitaxel, cisplatin and 5-fluorouracil is prevented by siRNA targeting lipocalin-type prostaglandin synthase-D
medicine
-
both hematopoietic- and lipocalin-type prostaglandin-D synthase are present in cartilage from healthy donors as well as from patients with osteoarthritits. Level of lipocalin-type prostaglandin-D synthase is more than 20fold higher than hematopoietic-type enzyme. Levels of lipocalin-type prostaglandin-D synthase mRNA and protein are increased in cartilage from aptients with osteoarthritis. Treatment of chondrocytes with IL-1beta upregulates lipocalin-type prostaglandin-D synthase mRNA and protein expressions as well as prostaglandin D2 production in a dose- and time-dependent manner. The upregulation of lipocalin-type prostaglandin-D synthase by IL-1beta is blocked by the translational inhibitor cycloheximide. Specific inhibitors of the MAPK p38 and c-jun N-terminal kinase and of the NF-kappaB and Notch signalling pathways suppress IL-1beta-induced upregulation of lipocalin-type prostaglandin-D synthase expression. An inhibitor of the extracellular signal-regulated kinase ERK/MAPK demonstrates no significant influence. Prostaglandin D2 prevents IL-1beta-induced upregulation of lipocalin-type prostaglandin-D synthase expression
medicine
-
in patients receiving long-term intravenous administration of gentamicin for the treatment of infective endocarditis, systemic clearance of gentamicin is reduced by 10% from the early to late treatment phase, wherease urinary lipocalin-type prostaglandin synthase excretion shows a significant increase. No significant changes are observed for urinary beta2-microglobulin and N-acetyl-beta-D-glucosaminidase concentrations
medicine
-
in patients with acute inflammatory demyelinating polyneuropathy, concentration of prostaglandin-D synthase is significantly increased in cerebrospinal fluid, due to a blood-cerebrospinal fluid barrier dysfunction. The intrathecal synthesis of prostaglandin-D synthase is significantly decreased in these patients. Changes of the ratio of cerebrospinal fluid prostaglandin-D synthase to albumin are only observed in patients with acute inflammatory demyelinating polyneuropathy, but not in Miller Fisher Syndrome, chronic inflammatory demyelinating polyradiculoneuropathy, or multiple sclerosis patients
medicine
-
in patients with HIV infection who have progressive neurocognitive decline over the next 6 months and in patients with a history of intravenal drug use, 3-nitrotyrosine modified proteins are significantly elevated. Among the 13 different proteins with 3-nitrotyrosine modification identified, lipocalin-type prostaglandin-D synthase is the most abundant, and the modification results in loss of enzymatic activity
medicine
-
in patients with stabel coronary artery disease who underwent diagnostic coronary angiography, the most powerful independent predictor of the coronary severity score is the level of lipocalin-type prostaglandin-D synthase
medicine
-
level of seminal plasma lipocalin-type prostaglandin-D synthase is significantly lower in groups with obstruction of the male seminal tract. Men with nonobstructive azoospermia have less homogenity of lipocalin-type prostaglandin-D synthase levels. Lipocalin-type prostaglandin-D synthase can be a potential biomarker for assessing patency in the seminal tract in men with azoospermia. In men with azoospermia and high seminal lipocalin-type prostaglandin-D synthase levels, the diagnosis of nonobstructive azoospermia can be potentially made without biopsy
medicine
-
study on the pharmacokinetics of recombinant human lipocalin-type prostaglandin-D synthase in canines. After an intravenous bolus injection, the serum concentration decreases biexponentially with a half-life of the terminal line phase of 0.77 h. L-PGDS is distributed mainly in the blood. Only 10.3% of the administered enzyme is excreted to the urine, suggesting that L-PGDS is actively degraded within the body
medicine
-
based on the observations it is speculated that PGD2 acts as one of the immuno-modulating molecules in gastric mucosa infected with Helicobacter pylori, PGD2 might be involved in the pathophysiology of other gastric diseases, such as gastric ulcers or erosion
medicine
-
dendritic cells in the epidermis and dermis are capable of functioning as an important source of PGD2 in the skin, thereby contributing to or regulating innate and/or acquired immune responses of the skin
medicine
prostaglandin D2 synthesized by the hematopoietic prostaglandin D2 synthase has a pro-inflammatory effect in allergic asthma, regulating many hallmark characteristics of the disease
medicine
-
the enzyme is a biomarker for the assessment of cerebrospinal fluid leaks
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
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.
58
600-607
1998
Homo sapiens
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
-
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.
241
288-293
1997
Homo sapiens
Watanabe, K.; Urade, Y.; Mder, M.; Murphy, C.; Hayaishi, O.
Identification of beta-trace as prostaglandin D synthase
Biochem. Biophys. Res. Commun.
203
1110-1116
1994
Homo sapiens
Hoffmann, A.; Conradt, H.S.; 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.
61
451-456
1993
Homo sapiens
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.
272
28263-28266
1997
Homo sapiens
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
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. USA
88
4020-4024
1991
Homo sapiens
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
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)
Inoue, T.; Irikura, D.; Okazaki, N.; Kinugasa, S.; Matsumura, H.; Uodome, N.; Yamamoto, M.; Kumasaka, T.; Miyano, M.; Kai, Y.; Urade, Y.
Mechanism of metal activation of human hematopoietic prostaglandin D synthase
Nat. Struct. Biol.
10
291-296
2003
Homo sapiens (O60760), Homo sapiens
Chen, D.Y.; Wang, J.J.; Huang, Y.F.; Zhou, K.Y.
Relationship between lipocalin-type prostaglandin D synthase and alpha-glucosidase in azoospermia seminal plasma
Clin. Chim. Acta
354
69-76
2005
Homo sapiens
Harrington, M.G.; Fonteh, A.N.; Biringer, R.G.; AF, R.H.; Cowan, R.P.
Prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology
Dis. Markers
22
281-289
2006
Homo sapiens (P41222)
-
Inoue, T.; Okano, Y.; Kado, Y.; Aritake, K.; Irikura, D.; Uodome, N.; Okazaki, N.; Kinugasa, S.; Shishitani, H.; Matsumura, H.; Kai, Y.; Urade, Y.
First determination of the inhibitor complex structure of human hematopoietic prostaglandin D synthase
J. Biochem.
135
279-283
2004
Homo sapiens
Kagitani-Shimono, K.; Mohri, I.; Oda, H.; Ozono, K.; Suzuki, K.; Urade, Y.; Taniike, M.
Lipocalin-type prostaglandin D synthase (beta-trace) is upregulated in the alphaB-crystallin-positive oligodendrocytes and astrocytes in the chronic multiple sclerosis
Neuropathol. Appl. Neurobiol.
32
64-73
2006
Homo sapiens
Nantel, F.; Fong, C.; Lamontagne, S.; Wright, D.H.; Giaid, A.; Desrosiers, M.; Metters, K.M.; O'Neill, G.P.; Gervais, F.G.
Expression of prostaglandin D synthase and the prostaglandin D2 receptors DP and CRTH2 in human nasal mucosa
Prostaglandins Other Lipid Mediat.
73
87-101
2004
Homo sapiens
Chen, D.Y.; Zhu, M.Y.; Cui, Y.D.; Huang, T.H.
Relationship between contents of lipocalin-type prostaglandin D synthase on the surface of infertility sperm and in seminal plasma
Biochemistry (Moscow)
72
215-218
2007
Homo sapiens
Malki, S.; Bibeau, F.; Notarnicola, C.; Roques, S.; Berta, P.; Poulat, F.; Boizet-Bonhoure, B.
Expression and biological role of the prostaglandin D synthase/SOX9 pathway in human ovarian cancer cells
Cancer Lett.
255
182-193
2007
Homo sapiens
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
Schlatterer, J.C.; Baeker, R.; Schlatterer, B.; Klose, J.; Kehler, W.; Schlatterer, K.
Purification of prostaglandin D synthase by ceramic- and size exclusion chromatography
Prostaglandins Other Lipid Mediat.
81
80-89
2006
Bos taurus, Homo sapiens
Zayed, N.; Li, X.; Chabane, N.; Benderdour, M.; Martel-Pelletier, J.; Pelletier, J.P.; Duval, N.; Fahmi, H.
Increased expression of lipocalin-type prostaglandin D2 synthase in osteoarthritic cartilage
Arthritis Res. Ther.
10
R146
2008
Homo sapiens
Inoue, T.; Eguchi, Y.; Matsumoto, T.; Kijima, Y.; Kato, Y.; Ozaki, Y.; Waseda, K.; Oda, H.; Seiki, K.; Node, K.; Urade, Y.
Lipocalin-type prostaglandin D synthase is a powerful biomarker for severity of stable coronary artery disease
Atherosclerosis
201
385-391
2008
Homo sapiens
Fujimori, K.; Aritake, K.; Urade, Y.
Enhancement of prostaglandin D(2) production through cyclooxygenase-2 and lipocalin-type prostaglandin D synthase by upstream stimulatory factor 1 in human brain-derived TE671 cells under serum starvation
Gene
426
72-80
2008
Homo sapiens
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
Hohwy, M.; Spadola, L.; Lundquist, B.; Hawtin, P.; Dahmen, J.; Groth-Clausen, I.; Nilsson, E.; Persdotter, S.; von Wachenfeldt, K.; Folmer, R.H.; Edman, K.
Novel prostaglandin D synthase inhibitors generated by fragment-based drug design
J. Med. Chem.
51
2178-2186
2008
Homo sapiens (O60760)
Huang, Y.C.; Lyu, R.K.; Tseng, M.Y.; Chang, H.S.; Hsu, W.C.; Kuo, H.C.; Chu, C.C.; Wu, Y.R.; Ro, L.S.; Huang, C.C.; Chen, C.M.
Decreased intrathecal synthesis of prostaglandin D(2) synthase in the cerebrospinal fluid of patients with acute inflammatory demyelinating polyneuropathy
J. Neuroimmunol.
206
100-105
2009
Homo sapiens
Heshmat, S.M.; Mullen, J.B.; Jarvi, K.A.; Soosaipillai, A.; Diamandis, E.P.; Hamilton, R.J.; Lo, K.C.
Seminal plasma lipocalin-type prostaglandin D synthase: a potential new marker for the diagnosis of obstructive azoospermia
J. Urol.
179
1077-1080
2008
Homo sapiens
Li, W.; Malpica-Llanos, T.M.; Gundry, R.; Cotter, R.J.; Sacktor, M.; Mc Arthur, J.; Nath, A.
Nitrosative stress with HIV dementia causes decreased L-prostaglandin D synthase activity
Neurology
70
1753-1762
2008
Homo sapiens
Li, W.; Mase, M.; Inui, T.; Shimoda, M.; Isomura, K.; Oda, H.; Yamada, K.; Urade, Y.
Pharmacokinetics of recombinant human lipocalin-type prostaglandin D synthase/beta-trace in canine
Neurosci. Res.
61
289-293
2008
Homo sapiens
Eichele, K.; Ramer, R.; Hinz, B.
Decisive role of cyclooxygenase-2 and lipocalin-type prostaglandin D synthase in chemotherapeutics-induced apoptosis of human cervical carcinoma cells
Oncogene
27
3032-3044
2008
Homo sapiens
Nakayama, H.; Echizen, H.; Gomi, T.; Shibuya, Y.; Nakamura, Y.; Nakano, K.; Arashi, H.; Itai, T.; Ohnishi, S.; Tanaka, M.; Orii, T.
Urinary lipocalin-type prostaglandin D synthase: a potential marker for early gentamicin-induced renal damage?
Ther. Drug Monit.
31
126-130
2009
Homo sapiens
Shimura, C.; Satoh, T.; Igawa, K.; Aritake, K.; Urade, Y.; Nakamura, M.; Yokozeki, H.
Dendritic cells express hematopoietic prostaglandin D synthase and function as a source of prostaglandin D2 in the skin
Am. J. Pathol.
176
227-237
2010
Homo sapiens
Weber, J.E.; Oakley, A.J.; Christ, A.N.; Clark, A.G.; Hayes, J.D.; Hall, R.; Hume, D.A.; Board, P.G.; Smythe, M.L.; Flanagan, J.U.
Identification and characterisation of new inhibitors for the human hematopoietic prostaglandin D2 synthase
Eur. J. Med. Chem.
45
447-454
2010
Homo sapiens (O60760), Homo sapiens
Takeda, K.; Takahashi, N.H.; Yoshizawa, M.; Shibahara, S.
Lipocalin-type prostaglandin D synthase as a regulator of the retinoic acid signaling in melanocytes
J. Biochem.
148
139-148
2010
Homo sapiens
Uchida, Y.; Urade, Y.; Mori, S.; Kohzuma, T.
UV resonance Raman studies on the activation mechanism of human hematopoietic prostaglandin D(2) synthase by a divalent cation, Mg(2+)
J. Inorg. Biochem.
104
331-340
2010
Homo sapiens (O60760), Homo sapiens
Hokari, R.; Nagata, N.; Kurihara, C.; Watanabe, C.; Komoto, S.; Okada, Y.; Kawaguchi, A.; Nagao, S.; Hibi, T.; Nagata, K.; Urade, Y.; Miura, S.
Increased expression and cellular localization of lipocalin-type prostaglandin D synthase in Helicobacter pylori-induced gastritis
J. Pathol.
219
417-426
2009
Homo sapiens
Takahashi, S.; Tsurumura, T.; Aritake, K.; Furubayashi, N.; Sato, M.; Yamanaka, M.; Hirota, E.; Sano, S.; Kobayashi, T.; Tanaka, T.; Inaka, K.; Tanaka, H.; Urade, Y.
High-quality crystals of human haematopoietic prostaglandin D synthase with novel inhibitors
Acta Crystallogr. Sect. F
66
846-850
2010
Homo sapiens
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
Zhou, Y.; Shaw, N.; Li, Y.; Zhao, Y.; Zhang, R.; Liu, Z.J.
Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules
FASEB J.
24
4668-4677
2010
Homo sapiens (P41222), Homo sapiens
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
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
Fukuhara, A.; Yamada, M.; Fujimori, K.; Miyamoto, Y.; Kusumoto, T.; Nakajima, H.; Inui, T.
Lipocalin-type prostaglandin D synthase protects against oxidative stress-induced neuronal cell death
Biochem. J.
443
75-84
2012
Homo sapiens (P41222)
Kume, S.; Lee, Y.H.; Miyamoto, Y.; Fukada, H.; Goto, Y.; Inui, T.
Systematic interaction analysis of human lipocalin-type prostaglandin D synthase with small lipophilic ligands
Biochem. J.
446
279-289
2012
Homo sapiens (P41222), Homo sapiens
Kume, S.; Lee, Y.H.; Nakatsuji, M.; Teraoka, Y.; Yamaguchi, K.; Goto, Y.; Inui, T.
Fine-tuned broad binding capability of human lipocalin-type prostaglandin D synthase for various small lipophilic ligands
FEBS Lett.
588
962-969
2014
Homo sapiens (P41222), Homo sapiens
Lim, S.M.; Chen, D.; Teo, H.; Roos, A.; Jansson, A.E.; Nyman, T.; Tresaugues, L.; Pervushin, K.; Nordlund, P.
Structural and dynamic insights into substrate binding and catalysis of human lipocalin prostaglandin D synthase
J. Lipid Res.
54
1630-1643
2013
Homo sapiens (P41222), Homo sapiens
Perduca, M.; Bovi, M.; Bertinelli, M.; Bertini, E.; Destefanis, L.; Carrizo, M.E.; Capaldi, S.; Monaco, H.L.
High-resolution structures of mutants of residues that affect access to the ligand-binding cavity of human lipocalin-type prostaglandin D synthase
Acta Crystallogr. Sect. D
70
2125-2138
2014
Homo sapiens (P41222), Homo sapiens
Edfeldt, F.; Evenaes, J.; Lepistoe, M.; Ward, A.; Petersen, J.; Wissler, L.; Rohman, M.; Sivars, U.; Svensson, K.; Perry, M.; Feierberg, I.; Zhou, X.H.; Hansson, T.; Narjes, F.
Identification of indole inhibitors of human hematopoietic prostaglandin D2 synthase (hH-PGDS)
Bioorg. Med. Chem. Lett.
25
2496-2500
2015
Homo sapiens (O60760), Homo sapiens
Mazari, A.M.; Hegazy, U.M.; Mannervik, B.
Identification of new inhibitors for human hematopoietic prostaglandin D2 synthase among FDA-approved drugs and other compounds
Chem. Biol. Interact.
229
91-99
2015
Homo sapiens (O60760), Homo sapiens
Morell-Garcia, D.; Bauca, J.M.; Sastre, M.P.; Yanez, A.; Llompart, I.
Sample-dependent diagnostic accuracy of prostaglandin D synthase in cerebrospinal fluid leak
Clin. Biochem.
50
27-31
2017
Homo sapiens
Pires, A.; Santos, R.; Nogueira, A.; Abranches, R.
Production of human lipocalin-type prostaglandin D synthase in the model plant Medicago truncatula
In Vitro Cell. Dev. Biol. Plant
50
276-281
2014
Homo sapiens (P41222)
-
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
Mizoguchi, M.; Nakatsuji, M.; Takano, J.; Ishibashi, O.; Wada, K.; Inui, T.
Development of pH-independent drug release formulation using lipocalin-type prostaglandin D synthase
J. Pharm. Sci.
105
2735-2742
2016
Homo sapiens (P41222)
Elmes, M.W.; Volpe, A.D.; d'Oelsnitz, S.; Sweeney, J.M.; Kaczocha, M.
Lipocalin-type prostaglandin D synthase is a novel phytocannabinoid-binding protein
Lipids
53
353-360
2018
Homo sapiens
Saxty, G.; Norton, D.; Affleck, K.; Clapham, D.; Cleasby, A.; Coyle, J.; Day, P.; Frederickson, M.; Hancock, A.; Hobbs, H.; Hutchinson, J.; Le, J.; Leveridge, M.; McMenamin, R.; Mortenson, P.; Page, L.; Richardson, C.; Russell, L.; Sherriff, E.; Teague, S
Identification of orally bioavailable small-molecule inhibitors of hematopoietic prostaglandin D2 synthase using X-ray fragment based drug discovery
MedChemComm
5
134-141
2014
Homo sapiens
-
Teraoka, Y.; Kume, S.; Lin, Y.; Atsuji, S.; Inui, T.
Comprehensive evaluation of the binding of lipocalin-type prostaglandin D synthase to poorly water-soluble drugs
Mol. Pharm.
14
3558-3567
2017
Homo sapiens (P41222)
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