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Enzyme Nomenclature
Information on EC 5.3.99.2 - Prostaglandin-D synthase
for references in articles please use BRENDA:EC5.3.99.2
Word Map on EC 5.3.99.2
- 5.3.99.2
-
cerebrospinal
- inflammatory
-
arachidonic
- inflammation
- renal
-
cyclooxygenase
-
prostanoids
- indomethacin
-
lipocalins
-
mast
-
cystatin
- creatinine
- sleep
-
seminal
-
glomerular
-
lipophilic
-
eicosanoids
- aspirin
-
nsaid
- plexus
- leptomeninges
-
synthase-1
-
nonsteroidal
- medicine
-
leukotriene
-
thromboxane
-
endoperoxide
-
fistula
-
nephelometric
-
1.14.99.1
-
subarachnoidal
-
preoptic
- rhinorrhea
-
pgf2alpha
-
ventrolateral
-
arachnoid
- transthyretin
- cysc
-
beta2-microglobulin
-
sleep-wake
- pghs-1
-
hydroperoxidase
-
tuberomammillary
- synthesis
- analysis
- nutrition
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
5.3.99.2
-
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RECOMMENDED NAME
GeneOntology No.
Prostaglandin-D synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
isomerization
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
52227-78-8
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
homologue of lipocalin-type prostaglandin synthase, no enzymic activity
SwissProt
homologue of lipocalin-type prostaglandin synthase, weak enzymic activity
SwissProt
-
3102, 3103, 3105, 3106, 3110, 3111, 3115, 3119, 3121, 3123, 649547, 649720, 661507, 662057, 662954, 663278, 678359, 679017, 682618, 693254, 693896, 694489, 701618, 704365, 705307, 713649, 713720, 715626, 715845
-
-
lipocalin-type prostaglandin D synthase. Isoform is identical to beta-trace, a major protein in human cerebrospinal fluid, and acts as both a PGD2-producing enzyme and as an extracellular transporter for lipophilic ligands
-
-
patients with stable coronary artery disease who underwent diagnostic coronary angiography
-
-
-
3098, 3102, 679990, 681206, 682519, 692921, 694939, 702057, 705932, 705934, 713720, 714066, 715626, 715845
-
-
ApcMin/+ mice bearing a defect in the adenomatous polyposis coli gene which leads to development of many adenomas
-
-
mouse model of globoid cell leukodystrophy or Krabbe’s disease, of Tay-Sachs disease, Sandhoff disease, GM1 gangliosidosis and Niemann-Pick type C1 disease
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
malfunction
-
dextran sodium sulfate treatment to L-PGDS-deficientmice shows lower ulcerative colitis disease activity than control mice
malfunction
-
the stable transfection with antisense L-PGDS induces markedly the stimulation of fat storage in cultured adipocytes during the maturation phase
malfunction
-
co-localization of arrestin-3 with L-PGDS is drastically reduced in MG-63 cells when L-PGDS activity is inhibited
malfunction
-
double knockout mice, lacking lipocalin prostaglandin D synthase as well as PPARgamma2, have impaired carbohydrate and lipid metabolism with glucose tolerance compared to any other genotypes, their interscapular brown adipose tissue exhibits greater lipid content than that of wild-type mice, which is independent of PPARgamma2 dysfunction. In subcutaneous white adipose tissue, L-PGDS KO mice exhibit a 4fold increase in UCP1 expression and a reduction in adipogenic marker aP2 expression. Phenotypes, overview
malfunction
-
double knockout mice, lacking lipocalin prostaglandin D synthase as well as PPARgamma2, have impaired carbohydrate and lipid metabolism with glucose tolerance compared to any other genotypes, their interscapular brown adipose tissue exhibits greater lipid content than that of wild-type mice, which is independent of PPARgamma2 dysfunction. In subcutaneous white adipose tissue, L-PGDS KO mice exhibit a 4fold increase in UCP1 expression and a reduction in adipogenic marker aP2 expression. Phenotypes, overview
-
physiological function
-
L-PGDS may fine-tune the all-trans retinoic acid signaling in melanocytes
physiological function
-
lipocalin type prostaglandin D synthase is a multi-functional protein acting as a somnogen (PGD2)-producing enzyme, an extracellular transporter of various lipophilic ligands, and an amyloid-beta chaperone in human cerebrospinal fluid
physiological function
-
lipocalin-type prostaglandin D synthase acts as both a PGD2 synthase and an extracellular transporter for small lipophilic molecules
physiological function
-
H-PGDS plays a critical role in the development of allergic rhinitis, especially in the induction of late phase nasal obstruction
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
-
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
-
lipocalin prostaglandin D synthase regulates synthesis of an important inflammatory and signaling mediator, prostaglandin D2
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
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
-
additional information
-
structure homology modelling using the solution structure of the C65A mouse L-PGDS, PDB code 2RQ0, as template, 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
-
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E,15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
4-hydroxynon-2-enal + glutathione
?
conjugation of glutathione
-
?
4-nitrobenzyl chloride + glutathione
?
conjugation of glutathione
-
?
7-chloro-4-nitrobenz-2-oxa-1,3-diazole + glutathione
?
conjugation of glutathione
-
?
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
(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
-
-
-
?
(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
-
-
?
(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
-
-
-
?
(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 + 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
-
i.e. prostaglandin H2, PGH2
i.e. prostaglandin D2, PGD2
-
?
1-bromo-2,4-dinitrobenzene + glutathione
?
conjugation of glutathione
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
conjugation of glutathione
-
?
1-fluoro-2,4-dinitrobenzene + glutathione
?
conjugation of glutathione
-
?
1-iodo-2,4-dinitrobenzene + glutathione
?
conjugation of glutathione
-
?
allyl isothiocyanate + glutathione
?
conjugation of glutathione
-
?
benzyl isothiocyanate + glutathione
?
conjugation of glutathione
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
-
-
?
Prostaglandin H2
Prostaglandin D2
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
-
-
-
-
?
additional information
?
-
-
the enzyme may play an important role in both the development and the maturation of sperm
-
-
-
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
-
-
-
additional information
?
-
-
enzyme may play a role in scavenging harmful lipophilic substrates in lysosomal storage disorders
-
-
-
additional information
?
-
-
the lipocalin-type prostaglandin D synthase, prostaglandin D2, and prostaglandin D receptor system plays a pivotal role in the regulation of physiological sleep
-
-
-
additional information
?
-
-
the enzyme is bi-functional capable of synthesising D series prostaglandins and acting as a carrier of small lipophilic molecules
-
-
-
additional information
?
-
-
the enzyme is bi-functional capable of synthesising D series prostaglandins and acting as a carrier of small lipophilic molecules
-
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(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
O73888
-
-
?
(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
O09114
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
O35543
-
-
?
(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
O60760
-
-
?
(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
O35543
-
-
?
Prostaglandin H2
Prostaglandin D2
-
-
-
-
?
additional information
?
-
-
the enzyme may play an important role in both the development and the maturation of sperm
-
-
-
additional information
?
-
P41222
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
-
-
-
additional information
?
-
-
enzyme may play a role in scavenging harmful lipophilic substrates in lysosomal storage disorders
-
-
-
additional information
?
-
-
the lipocalin-type prostaglandin D synthase, prostaglandin D2, and prostaglandin D receptor system plays a pivotal role in the regulation of physiological sleep
-
-
-
additional information
?
-
-
the enzyme is bi-functional capable of synthesising D series prostaglandins and acting as a carrier of small lipophilic molecules
-
-
-
additional information
?
-
-
the enzyme is bi-functional capable of synthesising D series prostaglandins and acting as a carrier of small lipophilic molecules
-
-
-
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
-
-
-
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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+
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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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride
-
IC50: 0.0362 mM in presence of EDTA, 0.0981 in presence of Mg2+
2-phenyl-5-(1H-pyrazol-3-yl)-1,3-thiazole
-
; inhibitor generated by fragment-based drug design, crystallographic data
AT-56
-
inhibition of prostaglandin-D synthase, resulting in suppression of prostaglandin D2 production under serum-starved conditions
N-(1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
N-benzhydryl-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
; low micromolar potency in the inhibition of the purified enzyme
N-methoxy-N-methyl-4-(5-benzoylbenzimidazole-2-yl)-3,5-dimethylpyrrole-2-carboxamide
-
TAS-204, specific H-PGDS inhibitor
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
-
-
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
additional information
-
the lipid transporter activity of the enzyme is competitively inhibited by pamitate, stearate and arachnoate
-
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
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
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
-
-
HQL-79
-
i.e. 4-benzhydryloxy-1-[3-(1H-tetrazol-5-yl)-propyl]-piperidine, H-PGDS-specific inhibitor
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
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-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)-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-(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-(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-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-(1-amino-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
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]benzoyl}amino)phenyl]-3-phenyl-1,2-thiazole-5-carboxamide
-
-
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
Se4+
-
SeCl4; systemic administration of the inhibitor has sleep-reducing potency
SeCl4
-
selective inhibition of enzyme. Intraperitoneal injection of SeCl4 decreases the prostaglandin D2 content in the brain without affecting the amounts of prostaglandins E2 and F2alpha. It inhibits sleep dose-dependently and immediately after the administration
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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%
-
glutathione
-
required for activity of spleen enzyme, not required for brain enzyme; the spleen-type PGD synthase is a kind of glutathione S-transferase and therefore requires glutathione for activity
glutathione
-
Km: 0.2 mM; required; required for activity of spleen enzyme, not required for brain enzyme; the spleen-type PGD synthase is a kind of glutathione S-transferase and therefore requires glutathione for activity
glutathione
-
required for activity of spleen enzyme, not required for brain enzyme
glutathione
-
glutathione-independent enzyme is detected in: brain, spinal cord, epididymis; glutathione-requiring enzyme is detected in: spleen, thymus, bone marrow, digestive tract, mast cells, histiocytes, dendritic cells, Kupffer cells, Langerhans cells; the glutathione-requiring enzyme is a member of the glutathione S-transferase family
glutathione
-
the hematopoietic prostaglandin D synthase is a glutathione S-transferase
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
guanidinium hydrochloride
-
2.5fold activation at 500 mM, inhibition above, less than 5% activity at 2 M guanidinium hydrochloride; activation up to 750 mM, 1.5fold activition at 500 mM, inhibition above 1 M, complete deactivation at 4 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
Urea
-
1.6fold activation at 1M, inhibition above, less than 5% activity at 4 M urea
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
in the presence of 1 M urea
0.0028
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
-
0.0083
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
in the presence of 500 mM guanidinium hydrochloride
0.014
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
pH 8.0
0.014
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
pH 8.0
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
0.0008
prostaglandin H2
-
mutant DELTA1-24_L-PGDS; mutant DELTA1-24_L-PGDS+W54A/H111A
0.0012
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+S45A/S81A; mutant DELTA1-24_L-PGDS+S45A/T67A/S81A
0.0014
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+H111A; mutant DELTA1-24_L-PGDS+H116A
0.0021
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+S45A/T67A; mutant DELTA1-24_L-PGDS+T67A/S81A
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
1-chloro-2,4-dinitrobenzene
-
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
0.5
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
in the presence of 1 M urea
0.95
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
in the presence of 500 mM guanidinium hydrochloride
21.7
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
-
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
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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
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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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.003
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
0.0046
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
0.000075
N-[4-methyl-3-[([3-[(4-methylpiperazin-1-yl)methyl]phenyl]carbonyl)amino]phenyl]-3-phenylisothiazole-5-carboxamide
Homo sapiens
-
37°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.9
14.9
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184
14.9
-
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
isolation of several enzyme isoforms with pI values ranging from 4.4 to 6.4
additional information
-
isolation of several enzyme isoforms with pI values ranging from 4.0 to 7.2, with identical molecular masses around 28000 Da
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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
-
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
-
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
-
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
-
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
-
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
-
enzyme mRNA is up-regulated in mouse model of globoid cell leukodystrophy or Krabbe’s disease, of Tay-Sachs disease, Sandhoff disease, GM1 gangliosidosis and Niemann-Pick type C1 disease,. Oligodendrocytes of all these mouse models show strong immunoreactivity for enzyme, but not astrocytes or microglia
-
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
-
qualitative and quantitative fluctuations of prostaglandin D synthase isoforms from cerebrospinal fluid reflect both major and subtle brain pathophysiology
-
L-PGDS expression in mouse epididymis gradually declines in parallel to the declining concentration of endogenous androgen after castration and increases with the treatment of exogenous testosterone
-
bone-marrow derived macrophage, lung and alveolar macrophage. Treatment with Escherichia coli lipopolysaccharide or Pseudomonas induce enzyme expression. Induction is regulated positively by AP-1 and negatively by p53
-
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
-
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
-
pigment epithelium; 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
interphotoreceptor matrix; pigment epithelium; the enzyme is predominantly expressed in retinal pigment epithelium and actively accumulates in interphotoreceptor matrix
-
both L-PGDS mRNA and protein are highly expressed in the interstitial tissue of adult testis. L-PGDS mRNA is first detected on day 30 after birth and exhibits an abundant signal in adult caput and cauda epididymis
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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
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
25000
26000
28000
-
x * 28000, SDS-PAGE, molecular mass is the same for several isoforms showing pI values from 4.2 to 7.0
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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
-
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
-
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
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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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
-
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
-
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
-
the structure of H-PGDS in complex with GSH and nocodazole is solved to a resolution of 1.9 A
-
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precipitation, and on a GSH Sepharose 4B and a Superdex 75 pg column
-
GST-Prep column chromatography
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme
-
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
-
recombinant PGDS
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
-
two-step purification method using cerebrospinal fluid
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
-
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli C41(DE3) cells
expression in Escherichia coli
expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta BL21(DE3)
-
expression of cDNA in Escherichia coli
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
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the coding region of human L-PGDS is sub-cloned into pCR-Script Amp SK+ vector
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression levels of L-PGDS mRNA and protein are significantly increased after 14 days of hypoxia
-
L-PGDS, but not H-PGDS, is induced on fibroblasts close to infiltrating cells in the Helicobacter pylori-infected gastric mucosa
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mice lacking PPARgamma2 have elevated levels of lipocalin prostaglandin D synthase expression in brown adipose tissue and subcutaneous white adipose tissue
oral pretreatment with the inhibitor EDJ300520 prevents the lipopolysaccharide-induced PGD2 increase in plasma and lungs
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the level of L-PGDS mRNA expression is increased 20fold in ulcerative colitis and increases with disease activity
the synthesis of PGD2 is increased in plasma and lungs in response to systemic lipopolysaccharide injection
-
mice lacking PPARgamma2 have elevated levels of lipocalin prostaglandin D synthase expression in brown adipose tissue and subcutaneous white adipose tissue
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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
-
the level of L-PGDS mRNA expression is increased 20fold in ulcerative colitis and increases with disease activity
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G59C
C59 is an essential residue for enzyme activity in mammals. Mutant G59C does not show enzymic activity
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
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
DELTA1-24_C65A L-PGDS
-
mutant, preserves a disulfide bond between Cys89 and Cys186
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
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
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
additional information
-
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184, shows weak enzymic activity
additional information
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184, shows weak enzymic activity
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
additional information
-
knockdown of the enzyme expression by siRNA in SH-SY5Y cells, two different siRNAs
additional information
-
disruption of gene for hematopoietic prostaglandin synthase in ApcMin/+ mice bearing a defect in the adenomatous polyposis coli gene which leads to development of many adenomas leads to 50% more intestinal adenomas compared with controls. Tumour size is not affected
additional information
-
chimeric protein construct carrying the mouse amino-terminal portion from D25 to L84, and zebrafish carboxyl-terminal portion from K79 to A184, shows weak enzymic activity
additional information
-
transgenic mice overexpressing the enzyme improve clearance of Pseudomonas from the lung compared with nontransgenic mice, as does intratracheal instillation of prostaglandin D2. Enzyme knock-out mice show impaired ability to remove Pseudomonas from the lung
additional information
-
enzyme knockout animals and transgenic animals. Knockout mice display a more severe inflammatory response that fails to resolve, whereas transgenic mice have little detectable inflammation. Lymphocytes isolated from inguinal lymph nodes of knockout mice show hyperproliferation and increased IL-2 synthesis effects that are rescued by 15-deoxy-DELTA12,14-prostaglandin J2, but not prostaglandin D2
additional information
-
adipocytes from lipocalin-type prostaglandin synthase-D knockout mice are significantly less sensitive to insulin-stimulated glucose transport than wild-type
additional information
-
generation of double knock out mice lacking lipocalin prostaglandin D synthase and PPARgamma2
additional information
-
generation of double knock out mice lacking lipocalin prostaglandin D synthase and PPARgamma2
-
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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
synthesis
-
optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme
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
analysis
-
PGD synthase is a useful marker for identifying the differentiation stage of human megakaryocytic cells