Information on EC 5.3.99.2 - Prostaglandin-D synthase

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The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY
5.3.99.2
-
RECOMMENDED NAME
GeneOntology No.
Prostaglandin-D synthase
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
isomerization
-
-
isomerization
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arachidonic acid metabolism
-
-
arachidonic acid metabolism
-
-
C20 prostanoid biosynthesis
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase
Brings about the opening of the epidioxy bridge. Some enzymes require glutathione.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
beta-Trace
-
-
-
-
Beta-trace protein
-
-
-
-
Beta-trace protein
P41222
-
glutathione dependent prostaglandine D2 synthase
O73888
i.e. PGDS
Glutathione-dependent PGD synthetase
-
-
-
-
glutathione-dependent prostaglandin D2 synthase
-
-
Glutathione-independent PGD synthetase
-
-
-
-
H-PGDS
-
-
-
-
H-PGDS
-
-
H-PGDS
O60760
-
H-PGDS
-
-
haematopoietic PGD synthase
-
-
haematopoietic prostaglandin D synthase
-
-
Hematopoietic prostaglandin D synthase
-
-
-
-
Hematopoietic prostaglandin D synthase
-
-
Hematopoietic prostaglandin D synthase
-
-
Hematopoietic prostaglandin D synthase
-
i.e. H-PGDS
Hematopoietic prostaglandin D synthase
-
-
Hematopoietic prostaglandin D synthase
-
-
Hematopoietic prostaglandin D synthase
-
i.e. PGDS
hematopoietic prostaglandin D2 synthase
-
-
hematopoietic prostaglandin D2 synthase
O60760
-
hematopoietic prostaglandin D2 synthase
-
-
HPGDS
-
-
Isomerase, prostaglanin R2 D-
-
-
-
-
L-PGDS
-
also called beta-trace
L-PGDS
-
also called beta-trace
L-PGDS
O09114
-
L-PGDS
Mus musculus C57BL/6
-
-
-
L-prostaglandin D synthase
-
-
L-prostaglandin D synthase
P41222
-
L-prostaglandin D synthase
-
-
L-type prostaglandin synthase
-
-
lipocalin prostaglandin D synthase
P41222
-
lipocalin prostaglandin D synthase
-
-
lipocalin prostaglandin D synthase
Mus musculus C57BL/6
-
-
-
lipocalin type prostaglandin D synthase
-
-
lipocalin-prostaglandin D synthase
-
-
lipocalin-type PG D synthase
P41222
-
lipocalin-type PGD synthase
P41222
-
lipocalin-type PGD synthase
O09114
-
lipocalin-type Pgds
-
-
lipocalin-type prostaglandin d synthase
-
-
lipocalin-type prostaglandin d synthase
-
i.e. L-PGDS
lipocalin-type prostaglandin d synthase
P41222
-
lipocalin-type prostaglandin d synthase
-
-
lipocalin-type prostaglandin d synthase
O09114
-
lipocalin-type prostaglandin d synthase
O09114
; i.e. L-PGDS
lipocalin-type prostaglandin d synthase
-
-
lipocalin-type prostaglandin D2 synthase
-
-
lipocalin-type prostaglandin D2 synthase
-
-
lipocaline-type prostaglandin D synthase
-
-
PGD synthase
-
-
-
-
PGD2 synthase
-
-
-
-
PGD2 synthetase
-
-
PGDS
-
-
-
-
PGDS
-
-
PGDS
-
-
PGDS2
-
-
-
-
PGH-PGD isomerase
-
-
-
-
PGH2 D-isomerase
-
-
Prostaglandin D synthase
-
-
-
-
Prostaglandin D synthase
-
-
Prostaglandin D synthase
P41222
-
Prostaglandin D2 synthase
-
-
-
-
Prostaglandin D2 synthase
-
-
prostaglandin D2 synthetase
-
-
prostaglandin synthase
-
-
Prostaglandin-D synthase
-
-
-
-
Prostaglandin-D synthase
-
-
Prostaglandin-H2 D-isomerase
-
-
-
-
Prostaglandin-H2 D-isomerase
P41222
-
Prostaglandin-H2 D-isomerase
P41222
UniProt name
Prostaglandin-H2 D-isomerase
O09114
-
Prostaglandin-R-prostaglandin D isomerase
-
-
-
-
PTGDS
P41222
-
CAS REGISTRY NUMBER
COMMENTARY
52227-78-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bull
-
-
Manually annotated by BRENDA team
homologue of lipocalin-type prostaglandin synthase, no enzymic activity
SwissProt
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
homologue of lipocalin-type prostaglandin synthase, weak enzymic activity
SwissProt
Manually annotated by BRENDA team
isoform liocalin-type prostaglandin D-synthase
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
lipocalin-type prostaglandin-D synthase
-
-
Manually annotated by BRENDA team
patients with acute inflammatory demyelinating polyneuropathy
-
-
Manually annotated by BRENDA team
patients with HIV infection
-
-
Manually annotated by BRENDA team
patients with osteoarthritis
-
-
Manually annotated by BRENDA team
patients with stable coronary artery disease who underwent diagnostic coronary angiography
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
ApcMin/+ mice bearing a defect in the adenomatous polyposis coli gene which leads to development of many adenomas
-
-
Manually annotated by BRENDA team
hematopoietic prostaglandin D2 synthase
-
-
Manually annotated by BRENDA team
isoform lipocalin-type prostaglandin-D synthase
-
-
Manually annotated by BRENDA team
Kunming White, outbred
-
-
Manually annotated by BRENDA team
male
-
-
Manually annotated by BRENDA team
mouse model of globoid cell leukodystrophy or Krabbes disease, of Tay-Sachs disease, Sandhoff disease, GM1 gangliosidosis and Niemann-Pick type C1 disease
-
-
Manually annotated by BRENDA team
recombinant protein
SwissProt
Manually annotated by BRENDA team
Mus musculus C57BL/6
male
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
diabetic Goto-Kakizaki
-
-
Manually annotated by BRENDA team
isoform lipocalin-type prostaglandin D synthase
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the lipocalin superfamily
evolution
-
the enzyme is a member of the lipocalin superfamily
malfunction
-
co-localization of arrestin-3 with L-PGDS is drastically reduced in MG-63 cells when L-PGDS activity is inhibited
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
-
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
-
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
-
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
-
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
Mus musculus C57BL/6
-
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
-
malfunction
Mus musculus C57BL/6
-
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
-
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
-
structure homology modelling using the solution structure of the C65A mouse L-PGDS, PDB code 2RQ0, as template, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
O35543
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
O09114
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
O73888
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
Q8QFM7
-
-
-
?
(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+
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + glutathione
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + glutathione
show the reaction diagram
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
show the reaction diagram
-
-
-
?
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E,15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
-
?
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E,15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
i.e. prostaglandin H2, PGH2
i.e. prostaglandin D2, PGD2
-
?
1-bromo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-bromo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-bromo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
4-hydroxynon-2-enal + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
4-nitrobenzyl chloride + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
7-chloro-4-nitrobenz-2-oxa-1,3-diazole + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
9,11-epoxymethano-prostaglandin H2
9,11-epoxymethano-prostaglandin D2
show the reaction diagram
-
substrate analogue U44069
product analogue 12415
-
?
allyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
allyl isothiocyanate + glutathione
?
show the reaction diagram
O35543
-
-
?
allyl isothiocyanate + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
benzyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
benzyl isothiocyanate + glutathione
?
show the reaction diagram
O35543
-
-
?
benzyl isothiocyanate + glutathione
?
show the reaction diagram
O73888
conjugation of glutathione
-
?
cumene hydroperoxide
cumene hydroxide
show the reaction diagram
O73888
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
show the reaction diagram
-
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
show the reaction diagram
O35543
-
-
?
Prostaglandin G2
15-Hydroperoxyprostaglandin D2
show the reaction diagram
-
-
-
-
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
ir
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
-
-
-
?
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
?
-
-
key enzyme in sleep regulation
-
-
-
additional information
?
-
-
key enzyme in sleep regulation
-
-
-
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 may play an important role in both the development and the maturation of sperm
-
-
-
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
?
-
P41222
prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology
-
-
-
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
?
-
-
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
-
-
-
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
?
-
Mus musculus, Mus musculus C57BL/6
-
the enzyme is bi-functional capable of synthesising D series prostaglandins and acting as a carrier of small lipophilic molecules
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
O35543
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
O09114
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
O73888
-
-
?
(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+
show the reaction diagram
-
-
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate + glutathione
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + glutathione
show the reaction diagram
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
show the reaction diagram
-
-
-
?
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E,15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
-
-
-
-
?
1-bromo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-bromo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
-
-
-
?
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
O35543
-
-
?
allyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
allyl isothiocyanate + glutathione
?
show the reaction diagram
O35543
-
-
?
benzyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
benzyl isothiocyanate + glutathione
?
show the reaction diagram
O35543
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
show the reaction diagram
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
show the reaction diagram
O35543
-
-
?
additional information
?
-
-
the enzyme belongs to the lipocalin family, a group of secretory proteins involved in the transport of small lipophilic ligands
-
-
-
additional information
?
-
-
key enzyme in sleep regulation
-
-
-
additional information
?
-
-
key enzyme in sleep regulation
-
-
-
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 may play an important role in both the development and the maturation of sperm
-
-
-
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
?
-
P41222
prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology
-
-
-
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
?
-
-
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
-
-
-
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
?
-
Mus musculus, Mus musculus C57BL/6
-
the enzyme is bi-functional capable of synthesising D series prostaglandins and acting as a carrier of small lipophilic molecules
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
O73888
-
glutathione
O35543
-
glutathione
-
KM for glutathione is decreased from 0.0006 mM in presence of EDTA to 0.00014 mM in presence of Mg2+
glutathione
-
GSH
glutathione
-
required
additional information
-
glutathione-independent enzyme
-
additional information
-
L-PGDS is glutathione-independent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
increase in activity
Ca2+
-
half maximal effective concentration at 0.4 mM, 1.5fold increase in activity
Mg2+
-
half maximal effective concentration at 0.05 mM, 1.5fold increase in activity, Mg2+ increases the affinity for glutathione
Mg2+
-
-
Sr2+
-
increase in activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-benzoyl piperazine
-
-
1-benzoyl piperidine
-
-
1-benzoyl-4-(methylsulfonyl)piperazine
-
-
1-phenyl-1-(2-thienyl)methanamine
-
-
15-Hydroperoxyarachidonic acid
-
-
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
2-phenyl-5-(1H-pyrazol-3-yl)thiazole
-
-
3,3',5'-triiodo-L-thyronine
-
0.0093 mM, 50% inhibition
3,3',5-triiodo-L-thyronine
-
0.011 mM, 50% inhibition
3-benzoylpyrrole
-
-
3-phenyl-5-(1H-pyrazol-3-yl)-1,2-oxazole
-
-
4-benzhydryloxy-1-[3-(1H-tetrazol-5-yl)-propyl]piperidine
-
HQL-79
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
-
-
5-(3-aminophenyl)-N-benzhydrylthiophene-2-carboxamide
-
-
5-(3-cyanophenyl)-N-(diphenylmethyl)thiophene-2-carboxamide
-
-
5-(3-hydroxyphenyl)thiophene-2-carboxylic acid
-
-
5-amino-4-[[(3'-hydroxybiphenyl-4-yl)carbonyl]amino]-5-oxopentanoic acid
-
-
AB179670
-
-
all-trans-retinoic acid
-
-
AT-56
-
inhibition of prostaglandin-D synthase, resulting in suppression of prostaglandin D2 production under serum-starved conditions
benzophenone
-
-
bilirubin
-
0.0068 mM, 50% inhibition
Biliverdin
-
0.0053 mM, 50% inhibition
Cibacron blue
O73888
0.00003 mM, 50% inhibition
Cibacron blue 3GA
-
-
CMB5190724
-
-
CMB5256165
-
-
cyclohexyl-phenylketone
-
-
cyclopentyl-phenylketone
-
-
EDJ300520
-
-
-
Ethacrynic acid
-
-
haematin
O73888
0.00008 mM, 50% inhibition
HQL-79
-
i.e. 4-benzhydryloxy-1-[3-(1H-tetrazol-5-yl)-propyl]-piperidine, H-PGDS-specific inhibitor
HQL-79
-
-
iodoacetamide
-
-
N-(1,6-diamino-1-oxohexan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-2,3'-dihydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3'-hydroxybiphenyl-3-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3,3'-dihydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-4-(1H-indol-4-yl)benzamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-4-(thiophen-2-yl)benzamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-6-(thiophen-2-yl)nicotinamide
-
selective H-PGDS inhibitor with low micromolar potency in the inhibition of the purified enzyme
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
-
N-(1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
-
N-(1-amino-3-cyclohexyl-1-oxopropan-2-yl)-5-(1H-indol-4-yl)thiophene-2-carboxamide
-
-
N-(1-amino-3-methyl-1-oxobutan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-4-methyl-1-oxopentan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
-
N-(1-amino-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
-
N-(2-amino-2-oxoethyl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
-
N-(diphenylmethyl)-2-(3-hydroxyphenyl)-1,3-thiazole-4-carboxamide
-
-
N-(diphenylmethyl)-2-phenyl-1,3-thiazole-4-carboxamide
-
-
N-(diphenylmethyl)-5-(1H-indol-4-yl)thiophene-2-carboxamide
-
-
N-(diphenylmethyl)-5-phenylthiophene-2-carboxamide
-
-
N-(diphenylmethyl)-5-[3-(hydroxymethyl)phenyl]thiophene-2-carboxamide
-
-
N-(diphenylmethyl)biphenyl-4-carboxamide
-
-
N-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-phenyl-2-thiophene-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]phenyl]carbonyl)amino]phenyl]-3-phenylisothiazole-5-carboxamide
-
-
Na2SeO3
-
systemic administration of the inhibitor has sleep-reducing potency
nocodazole
-
-
NSC151248
-
-
NSC4502
-
-
oxfendazole
-
-
p-hydroxymercuribenzoate
-
-
PCMB
-
reversible
phenyl(thiophen-2-yl)methanone
-
-
phenyl-(2-thienyl)-methanol
-
-
phenyl-(3-thienyl)-methanone
-
-
retinoic acid
O09114
non-competitive
RNAi
-
-
-
Se2+
-
organic selenocompounds have no effect, hexavalent selenium compound is ineffective. The inhibition requires the preincubation of the metal with sulfhydryl compounds such as dithiothreitol, reversal of inhibition by excess amount of dithiothreitol. The rat spleen enzyme is much less inhibited than the rat brain enzyme
Se4+
-
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
Sulfobromophthalein
-
-
Tributyltin acetate
O73888
0.00009 mM, 50% inhibition
tributyltin bromide
O73888
0.00003 mM, 50% inhibition
Tributyltin chloride
O73888
0.00001 mM, 50% inhibition
U-46619
-
-
L-thyroxine
-
0.0039 mM, 50% inhibition, noncompetitve inhibition
additional information
-
the lipid transporter activity of the enzyme is competitively inhibited by pamitate, stearate and arachnoate
-
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
-
optimal concentration: 0.1-1 mM; required
glutathione
-
not required
glutathione
-
required
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
-
required
glutathione
-
brain enzyme is glutathione-independent
glutathione
-
the spleen enzyme is a sigma-class glutathione transferase
glutathione
-
-
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
glutathione
-
required
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
Mg2+
-
-
phorbol 12-myrisate 13-acetate
-
-
thymic stromal lymphopoietin
-
stimulates mRNA synthesis
-
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
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
0.2
(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
3.2
1-chloro-2,4-dinitrobenzene
-
-
5
1-chloro-2,4-dinitrobenzene
-
-
0.1
glutathione
-
-
0.2
glutathione
-
-
0.3
glutathione
-
; glutathione S-transferase activity
0.5
glutathione
-
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
8
glutathione
-
glutathione S-transferase activity
0.0005
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+S45A
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
0.0013
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+W45A
0.0014
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+H111A; mutant DELTA1-24_L-PGDS+H116A
0.0015
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+S81A
0.0016
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+P110A
0.0021
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+S45A/T67A; mutant DELTA1-24_L-PGDS+T67A/S81A
0.0028
prostaglandin H2
-
mutant DELTA1-24_L-PGDS+T67A
0.004
prostaglandin H2
-
-
0.005
prostaglandin H2
-
-
0.008
prostaglandin H2
-
-
0.0102
prostaglandin H2
-
mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0123
prostaglandin H2
-
mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0127
prostaglandin H2
-
mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0138
prostaglandin H2
-
wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0154
prostaglandin H2
-
mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0161
prostaglandin H2
-
mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0202
prostaglandin H2
-
mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0204
prostaglandin H2
-
mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0245
prostaglandin H2
-
mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0252
prostaglandin H2
-
mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0325
prostaglandin H2
-
mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.0328
prostaglandin H2
-
mutant enzyme L79A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.37
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
-
-
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
-
-
5
1-chloro-2,4-dinitrobenzene
-
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
2
glutathione
-
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
15
glutathione
-
-
0.06
prostaglandin H2
-
mutant enzyme L79A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.63
prostaglandin H2
-
mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.81
prostaglandin H2
-
mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
0.87
prostaglandin H2
-
mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
2.23
prostaglandin H2
-
mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
2.24
prostaglandin H2
-
mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
2.4
prostaglandin H2
-
mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
2.64
prostaglandin H2
-
wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
2.91
prostaglandin H2
-
mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
3.67
prostaglandin H2
-
mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
5.73
prostaglandin H2
-
mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
5.84
prostaglandin H2
-
mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
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 25C
612
1170
prostaglandin H2
-
mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
1890
prostaglandin H2
-
mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
2120
prostaglandin H2
-
mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
6570
prostaglandin H2
-
mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
6660
prostaglandin H2
-
mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
8940
prostaglandin H2
-
mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
9420
prostaglandin H2
-
mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
11490
prostaglandin H2
-
wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
14290
prostaglandin H2
-
mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
24840
prostaglandin H2
-
mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
27050
prostaglandin H2
-
mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25C
612
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
0.023
L-thyroxine
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
1-benzoyl piperazine
-
larger than 0.100 mM
0.1
1-benzoyl piperidine
-
larger than 0.100 mM
0.1
1-benzoyl-4-(methylsulfonyl)piperazine
-
larger than 0.100 mM
0.1
1-phenyl-1-(2-thienyl)methanamine
-
larger than 0.100 mM
0.0362
2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride
-
IC50: 0.0362 mM in presence of EDTA, 0.0981 in presence of Mg2+
0.000021
2-phenyl-5-(1H-pyrazol-3-yl)-1,3-thiazole
-
37C
0.0007
2-phenyl-5-(1H-pyrazol-3-yl)thiazole
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0875
3-benzoylpyrrole
-
-
0.00092
3-phenyl-5-(1H-pyrazol-3-yl)-1,2-oxazole
-
37C
0.003
4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine
-
inhibition of enzyme in lipocalin-type prostaglandin-D synthase-expressing TE-671 cells after stimulation with Ca2+-ionophore A23187
0.000138
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
-
37C
0.0014
4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0019
5-(3-aminophenyl)-N-benzhydrylthiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.023
5-amino-4-[[(3'-hydroxybiphenyl-4-yl)carbonyl]amino]-5-oxopentanoic acid
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.1
AB179670
-
larger than 0.100 mM
0.0622
benzophenone
-
-
0.0002
Cibacron blue 3GA
-
-
0.117
CMB5190724
-
-
0.1
CMB5256165
-
larger than 0.100 mM
0.1
cyclohexyl-phenylketone
-
larger than 0.100 mM
0.016
cyclopentyl-phenylketone
-
-
0.1223
Ethacrynic acid
-
-
0.0018
HQL-79
-
-
0.0038
HQL-79
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0059
HQL-79
-
pH and temperature not specified in the publication
0.0046
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0248
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3,3'-dihydroxybiphenyl-4-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0037
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0012
N-(1-amino-1-oxo-3-phenylpropan-2-yl)-6-(thiophen-2-yl)nicotinamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.001
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0021
N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0013
N-(1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0071
N-(1-amino-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.008
N-(2-amino-2-oxoethyl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0108
N-(diphenylmethyl)-2-(3-hydroxyphenyl)-1,3-thiazole-4-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0007
N-benzhydryl-5-(3-hydroxyphenyl)thiophene-2-carboxamide
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.1
N-phenyl-2-thiophene-carboxamide
-
larger than 0.100 mM
0.000075
N-[4-methyl-3-[([3-[(4-methylpiperazin-1-yl)methyl]phenyl]carbonyl)amino]phenyl]-3-phenylisothiazole-5-carboxamide
-
37C
0.065
nocodazole
-
-
0.105
NSC151248
-
-
0.0092
NSC4502
-
-
0.3
oxfendazole
-
larger than 0.300 mM
0.0128
phenyl(thiophen-2-yl)methanone
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.1
phenyl-(2-thienyl)-methanol
-
larger than 0.100 mM
0.0114
phenyl-(3-thienyl)-methanone
-
-
0.027
Sulfobromophthalein
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.89
-
-
4.5
-
-
11.7
Q8QFM7
pH 8.0, 25C
14.9
Q8QGV4
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
434
-
wild-type, pH 8.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
enzyme assay
8
-
activity assay
8
-
kinetic assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
enzyme assay
25
-
activity assay
25
-
kinetic assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
lipocalin-type prostaglandin D synthase (beta-trace) is upregulated in the alphaB-crystallin-positive astrocytes in the chronic multiple sclerosis
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
prostaglandin-H2 D-isomerase is produced in the membrane system surrounding the brain and is secreted into the cerebrospinal fluid to become beta-trace
Manually annotated by BRENDA team
-
glutathione-independent enzyme
Manually annotated by BRENDA team
-
enzyme mRNA is up-regulated in mouse model of globoid cell leukodystrophy or Krabbes 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
Manually annotated by BRENDA team
-
ischemic region, contralateral cortex
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
richest source of the enzyme
Manually annotated by BRENDA team
-
qualitative and quantitative fluctuations of prostaglandin D synthase isoforms from cerebrospinal fluid reflect both major and subtle brain pathophysiology
Manually annotated by BRENDA team
-
identification of several enzyme isoforms
Manually annotated by BRENDA team
-
second major protein
Manually annotated by BRENDA team
-
glutathione-independent enzyme
Manually annotated by BRENDA team
-
enzyme is found in luminal and glandular epithelial cells and in stroma during late pregnancy
Manually annotated by BRENDA team
-
glutathione-independent enzyme
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
enzyme is found in luminal and glandular epithelial cells and in stroma during late pregnancy
Manually annotated by BRENDA team
-
L-PGDS is constitutively expressed in the epithelium of the glandular base
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
epidermal Langerhans cell
Manually annotated by BRENDA team
-
cultivated rat leptomeningeal cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
of gut mucosa
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
precursor cells of platelets, CMK cells, Dami cells. The activity is undetectable in platelets and appears during differentiation of megakaryoblasts to megakaryocytes
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
epidermal melanocyte
Manually annotated by BRENDA team
-
of gut mucosa
Manually annotated by BRENDA team
-
auricle, ventricle
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
lipocalin-type prostaglandin D synthase (beta-trace) is upregulated in the alphaB-crystallin-positive oligodendrocytes in the chronic multiple sclerosis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
secretes the enzyme
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
pigment epithelium
Manually annotated by BRENDA team
-
glutathione-independent enzyme
Manually annotated by BRENDA team
P22057
interphotoreceptor matrix, the enzyme is predominantly expressed in retinal pigment epithelium and actively accumulates in interphotoreceptor matrix
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
determination of the correlation between content of enzyme in seminal plasma and on the surface of sperm
Manually annotated by BRENDA team
-
dermis, epidermis
Manually annotated by BRENDA team
-
glutathione-independent enzyme
Manually annotated by BRENDA team
-
the glutathione-independent PGD synthase is accumulated
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
e.g. epididymal
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
rough endoplasmic reticulum membrane
Manually annotated by BRENDA team
-
secreted in culture medium
-
Manually annotated by BRENDA team
-
secreted to the cerebrospinal fluid
-
Manually annotated by BRENDA team
-
the N-terminal 22-amino acid residues correspond to the putative secretion signal peptide of the enzyme
-
Manually annotated by BRENDA team
-
rough endoplasmic reticulum membrane
Manually annotated by BRENDA team
-
enzyme from basophilc leukemia cell line RBL-1
Manually annotated by BRENDA team
-
perinuclear L-type prostaglandin synthase/arrestin-3 co-localization is observed in prostaglandin D2-producing MG-63 cells
Manually annotated by BRENDA team
-
enzyme from mast cells
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
L-PGDS
705407
21000
-
L-PGDS bound to biliverdin
705407
23000
-
monomer
704977
25000
-
SDS-PAGE
715626
26000
-
determined by SDS-PAGE and Western Blot analysis
701618
26000
-
determined by SDS-PAGE and Western Blot analysis
705934
34000
-
gel filtration
3099
80000 - 85000
-
-
3098
85000
-
gel filtration
3100
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 19000, SDS-PAGE
?
-
x * 20749 or 21232, calculation from nucleotide sequence
?
-
x * 21016, calculation from nucleotide sequence
?
-
x * 23000-29000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
-
x * 23000, SDS-PAGE
?
O73888
x * 22732, deduced from nucleotide sequence
?
-
x * 23298, deduced from nucleotide sequence
?
-
x * 23359, deduced from nucleotide sequence
?
-
x * 28000, SDS-PAGE, molecular mass is the same for several isoforms showing pI values from 4.2 to 7.0
?
Q8QGV4
x * 28600, calculated
dimer
-
crystallization
homodimer
-
2 * 23000 Da
monomer
-
1 * 80000, SDS-PAGE
monomer
-
x-ray crystallography
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
glycoprotein
-
N-glycosylated at two positions: Asn51 and Asn78
glycoprotein
-
N-glycosylated
glycoprotein
P22057
-
glycoprotein
-
N-glycosylated at two positions: Asn51 and Asn78
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of H-PGDS are first grown by hanging-drop vapor diffusion method with PEG6000 as the precipitant at 20C 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 20C, 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
-
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, 4C, 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
O09114
recombinant enzyme
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
4C, 24 h, 40% loss of activity
3098
6
-
4C, 24 h, 5% loss of activity
3098
7
-
4C, 24 h, 40% loss of activity
3098
8
-
4C, 24 h, 60% loss of activity
3098
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57.4
-
melting temperature, mutant C89A/C186A
691128
59.6
-
melting temperature, mutant C186A
691128
60
-
purified recombinant enzyme, sodium phosphate, pH 7.0, containing 5% v/v ethanol, stable up to
726907
65 - 90
-
purified recombinant enzyme, thermal unfolding in the absence and presence of small lipophilic ligands, two-state unfolding transition, overview
726907
69.3
-
melting temperature, wild-type
691128
69.4
-
melting temperature, mutant C65A
691128
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 60.3C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions
692292
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glutathione prevents inactivation
-
thiol compounds, including glutathione stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, stable for at least 1 month
-
22C, stable for one month
-
4C, 24 h, 50% loss of activity
-
4C, stable up to 7 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
two-step purification method using cerebrospinal fluid
-
recombinant PGDS
O73888
by ammonium sulfate precipitation, and on a GSH Sepharose 4B and a Superdex 75 pg column
-
collected from the media using a Ni-column
-
glutathione-Sepharose column chromatography and Mono-Q column chromatography
-
GST-Prep column chromatography
-
Ni-affinity column chromatography and Superdex G75 gel filtration
-
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
-
on a GSTPrep FF 16/10 column
-
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 PDGS
-
two-step purification method using cerebrospinal fluid
-
GST-Prep column chromatography
-
Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
-
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
-
optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme
-
recombinant enzyme
-
recombinant PGDS
-
recombinant PGDS-glutathione transferase fusion protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q8QGV4
expression of cDNA in Escherichia coli
O73888
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 vector pET17b for expression in Escherichia coli BL21DE3 cells
-
into the vector pT7-7 for expression in Escherichia coli BL21DE3 cells
-
into the vectors pUB6/V5-His and pIRESneo, cDNA of positions 76-648 is cloned into the vector pGEM-T Easy
-
mutant C65A is expressed in Escherichia coli BL21(DE3) cells
-
the coding region of human L-PGDS is sub-cloned into pCR-Script Amp SK+ vector
-
expressed in 3T3-L1 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli C41(DE3) cells
-
expression as glutathione S-transferase fusion protein in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli; expression of cDNA in Escherichia coli
-
for expression in Escherichia coli BL21DE3 cells
-
for expression in Escherichia coli cells
-
expression in Escherichia coli
-
expression of cDNA in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
level of L-PGDS mRNA expression decreases as gastritis becomes more severe
-
lipopolysaccharide, LPS, reduces H-PGDS expression
-
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
-
enzyme expression is increased in H2O2-treated neuronal cells
-
L-PGDS knockout mice are generated
-
expression levels of L-PGDS mRNA and protein are significantly increased after 14 days of hypoxia
-
the level of L-PGDS mRNA expression is increased 20fold in ulcerative colitis and increases with disease activity
-
mice lacking PPARgamma2 have elevated levels of lipocalin prostaglandin D synthase expression in brown adipose tissue and subcutaneous white adipose tissue
-
mice lacking PPARgamma2 have elevated levels of lipocalin prostaglandin D synthase expression in brown adipose tissue and subcutaneous white adipose tissue
Mus musculus C57BL/6
-
-
oral pretreatment with the inhibitor EDJ300520 prevents the lipopolysaccharide-induced PGD2 increase in plasma and lungs
-
the synthesis of PGD2 is increased in plasma and lungs in response to systemic lipopolysaccharide injection
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C65A
-
inactive
C65A/C167A
-
site-directed mutagenesis
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
C89A/C167A/C186A
-
site-directed mutagenesis
C89A/C186A
-
site-directed mutagenesis
D93N
-
not activated by Ca2+ or Mg2+
D96N
-
very high basal activity, no activation in the presence of Ca2+ or Mg2+
D97N
-
not activated by Ca2+ or Mg2+
F83A
-
the mutation reduces the catalytic efficiency by almost 10fold
K59A
-
the mutation enhances the catalytic efficiency by more than 2fold
L131A
-
the mutation reduces the catalytic efficiency by almost 10fold
L79A
-
the mutation reduces the catalytic efficiency by almost 10fold
M64A
-
the mutation reduces the catalytic efficiency by almost 10fold
S45A
-
the mutation reduces the catalytic efficiency
S81A
-
the mutation reduces the catalytic efficiency
T147A
-
the mutation slightly enhances the catalytic efficiency
W43F/C65A/C167A
-
site-directed mutagenesis, the W43F mutant cannot be purified owing to the inclusion body formation of protein
W54A
-
the mutation reduces the catalytic efficiency
W54F/C65A/W112F/C167A
-
site-directed mutagenesis, the mutant still provides the disulfide bond between Cys89 and Cys186
Y149A
-
the mutation enhances the catalytic efficiency by more than 2fold
Y63S/T67S/C89A/C186A
-
site-directed mutagenesis
Y8F
-
active site mutant
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
C89A/C186A
-
mutant retains wild-type like activity and is stable
DELTA1-24_C65A
-
mutant
DELTA1-24_C65A L-PGDS
-
mutant, preserves a disulfide bond between Cys89 and Cys186
DELTA1-24_C65A+H111A
-
mutant
DELTA1-24_C65A+P110A
-
mutant
DELTA1-24_C65A+W54A
-
mutant
DELTA1-24_L-PGDS
-
mutant
DELTA1-24_L-PGDS+H111A
-
mutant
DELTA1-24_L-PGDS+H116A
-
mutant
DELTA1-24_L-PGDS+P110A
-
mutant
DELTA1-24_L-PGDS+S45A
-
mutant
DELTA1-24_L-PGDS+S45A/S81A
-
mutant
DELTA1-24_L-PGDS+S45A/T67A
-
mutant
DELTA1-24_L-PGDS+S45A/T67A/S81A
-
mutant
DELTA1-24_L-PGDS+S81A
-
mutant
DELTA1-24_L-PGDS+T67A
-
mutant
DELTA1-24_L-PGDS+T67A/S81A
-
mutant
DELTA1-24_L-PGDS+W45A
-
mutant
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
-
mutant is properly folded with well-defined tertiary structures
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
-
mutant is properly folded with well-defined tertiary structures
C65A
-
no significant change in conformation. Urea-induced unfolding at 5.125 mol/l compared with 5.75 mol/l for wild-type
C65A/C89A/C186A
-
mutant is properly folded with well-defined tertiary structures
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
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
G59C
Q8QGV4
C59 is an essential residue for enzyme activity in mammals. Mutant G59C does not show enzymic activity
additional information
Q8QGV4
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
M94A
-
the mutation reduces the catalytic efficiency
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
DELTA1-24_L-PGDS+W54A/H111A
-
mutant
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
-
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
-
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
-
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
-
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
W54A
-
mutant retains wild-type like activity and is stable
additional information
Mus musculus C57BL/6
-
generation of double knock out mice lacking lipocalin prostaglandin D synthase and PPARgamma2
-
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 60.3C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
PGD synthase is a useful marker for identifying the differentiation stage of human megakaryocytic cells
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
-
enzyme mRNA is up-regulated in mouse model of globoid cell leukodystrophy or Krabbes 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
medicine
-
hematopoietic prostaglandin D2 synthase derived prostaglandins may protect against inflammatory diseases, where T-lymphocytes play a pathogenic role, as in rheumatoid arthritis, atopic eczema, and chronic rejection
medicine
-
hematopoitic prostaglandin synthase controls an inhibitory effect on intestinal tumours
medicine
-
the lipocalin-type prostaglandin D synthase, prostaglandin D2, and prostaglandin D receptor system plays a pivotal role in the regulation of physiological sleep
medicine
-
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. Potential therapeutic use of enzyme or prostaglandin D2 against Pseudomonas pneumoniae
medicine
-
orally administered AT-56, i.e. 4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine, below 30 mg/kg body weight decreases the prostaglandin D2 production to 40% in the brain of H-PGDS-deficient mice after a stab-wound injury in a dose-dependent manner without affecting the production of prostaglandin E2 and prostaglandin F2alpha, and also suppresses the accumulation of eosinophils and monocytes in the bronco-alveolar lavage fluid from the antigen-induced lung inflammation model of human L-PGDS-transgenic mice
medicine
-
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
medicine
-
induction of L-PGDS expression in the heart as a response to hemodynamic stress
medicine
-
L-PGDS is beneficial for protecting the brain against transient and permanent cerebral ischemia, these results provide a better understanding of the role played by the enzymes that control eicosanoid synthesis and how they can be utilized as potential targets to prevent damage following either acute or potentially chronic neurological disorders
medicine
-
the results demonstrate that the neuroprotective effects of hematopoietic prostaglandin D synthase in the model are mediated by suppression of activation and infiltration of inflammatory cells
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
analysis
-
particle concentration fluorescence immunoassay for prostaglandin D synthase is suitable for determining the content of prostaglandin D synthetase in various regions of the rat CNS. The method allows to assay a large number of samples with reasonable sensitivity
medicine
-
prostaglandin D2 produced by hematopoietic prostaglandin D synthase contributes to lipopolysaccharide-induced fever
synthesis
-
optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme