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 hide
5.3.99.2
-
RECOMMENDED NAME
GeneOntology No.
Prostaglandin-D synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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 hide
LITERATURE
intramolecular oxidoreduction
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
52227-78-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Mus musculus C57BL/6
male
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
(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
(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-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
4-hydroxynon-2-enal + glutathione
?
show the reaction diagram
conjugation of glutathione
-
?
4-nitrobenzyl chloride + glutathione
?
show the reaction diagram
conjugation of glutathione
-
?
7-chloro-4-nitrobenz-2-oxa-1,3-diazole + glutathione
?
show the reaction diagram
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
benzyl isothiocyanate + glutathione
?
show the reaction diagram
cumene hydroperoxide
cumene hydroxide
show the reaction diagram
-
-
?
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
show the reaction diagram
glutathione + 1-chloro-2,4-dinitrobenzene
?
show the reaction diagram
-
-
-
?
Prostaglandin G2
15-Hydroperoxyprostaglandin D2
show the reaction diagram
-
-
-
-
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
show the reaction diagram
(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
(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-chloro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
1-fluoro-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
1-iodo-2,4-dinitrobenzene + glutathione
?
show the reaction diagram
allyl isothiocyanate + glutathione
?
show the reaction diagram
benzyl isothiocyanate + glutathione
?
show the reaction diagram
cumene hydroperoxide + 2 GSH
cumene hydroxide + GSSG + H2O
show the reaction diagram
Prostaglandin H2
Prostaglandin D2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
increase in activity
Ca2+
-
half maximal effective concentration at 0.4 mM, 1.5fold increase in activity
Sr2+
-
increase in activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
0.00003 mM, 50% inhibition
Cibacron blue 3GA
-
-
CMB5190724
-
-
CMB5256165
-
-
cyclohexyl-phenylketone
-
-
cyclopentyl-phenylketone
-
-
EDJ300520
-
-
-
Ethacrynic acid
-
-
haematin
0.00008 mM, 50% inhibition
HQL-79
iodoacetamide
-
-
L-thyroxine
-
0.0039 mM, 50% inhibition, noncompetitve inhibition
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
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
-
-
phenyl(thiophen-2-yl)methanone
phenyl-(2-thienyl)-methanol
-
-
phenyl-(3-thienyl)-methanone
-
-
retinoic acid
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
Sulfobromophthalein
-
-
Tributyltin acetate
0.00009 mM, 50% inhibition
tributyltin bromide
0.00003 mM, 50% inhibition
Tributyltin chloride
0.00001 mM, 50% inhibition
U-46619
-
-
additional information
-
the lipid transporter activity of the enzyme is competitively inhibited by pamitate, stearate and arachnoate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
guanidinium hydrochloride
Mg2+
-
-
phorbol 12-myrisate 13-acetate
-
-
thymic stromal lymphopoietin
-
stimulates mRNA synthesis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.5
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
3 - 5
1-chloro-2,4-dinitrobenzene
0.1 - 8
glutathione
0.0005 - 0.0328
prostaglandin H2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37 - 21.7
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
5
1-chloro-2,4-dinitrobenzene
Rattus norvegicus
-
conjugation of glutathione to 1-chloro-2,4-dinitrobenzene
2 - 15
glutathione
0.06 - 5.84
prostaglandin H2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110 - 27050
prostaglandin H2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.1
1-benzoyl piperazine
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+
0.000021
2-phenyl-5-(1H-pyrazol-3-yl)-1,3-thiazole
Homo sapiens
-
37C
0.0007
2-phenyl-5-(1H-pyrazol-3-yl)thiazole
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0875
3-benzoylpyrrole
Homo sapiens
-
-
0.00092
3-phenyl-5-(1H-pyrazol-3-yl)-1,2-oxazole
Homo sapiens
-
37C
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 25C
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 25C
0.1
AB179670
Homo sapiens
-
larger than 0.100 mM
0.0622
benzophenone
Homo sapiens
-
-
0.0002
Cibacron blue 3GA
Homo sapiens
-
-
0.117
CMB5190724
Homo sapiens
-
-
0.1
CMB5256165
0.016
cyclopentyl-phenylketone
Homo sapiens
-
-
0.1223
Ethacrynic acid
Homo sapiens
-
-
0.0018 - 0.0059
HQL-79
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
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 25C
0.0108
N-(diphenylmethyl)-2-(3-hydroxyphenyl)-1,3-thiazole-4-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.0007
N-benzhydryl-5-(3-hydroxyphenyl)thiophene-2-carboxamide
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.1
N-phenyl-2-thiophene-carboxamide
Homo sapiens
-
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
Homo sapiens
-
37C
0.065
nocodazole
Homo sapiens
-
-
0.105
NSC151248
Homo sapiens
-
-
0.0092
NSC4502
Homo sapiens
-
-
0.3
oxfendazole
Homo sapiens
-
larger than 0.300 mM
0.0128
phenyl(thiophen-2-yl)methanone
Homo sapiens
-
in 0.1 M Tris-HCl, pH 8.0, at 25C
0.1
phenyl-(2-thienyl)-methanol
Homo sapiens
-
larger than 0.100 mM
0.0114
phenyl-(3-thienyl)-methanone
Homo sapiens
-
-
0.027
Sulfobromophthalein
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.89
-
-
4.5
-
-
11.7
pH 8.0, 25C
434
-
wild-type, pH 8.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
-
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
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
glutathione-requiring enzyme
Manually annotated by BRENDA team
-
cultivated rat leptomeningeal cells
Manually annotated by BRENDA team
-
-
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
-
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
-
secretes the enzyme
Manually annotated by BRENDA team
-
glutathione-requiring 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
-
glutathione-independent 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
-
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
glutathione-requiring 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
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
L-PGDS
21000
-
L-PGDS bound to biliverdin
23000
-
monomer
34000
-
gel filtration
80000 - 85000
-
-
85000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
crystallization
homodimer
-
2 * 23000 Da
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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
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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
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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
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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
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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
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the structure of H-PGDS in complex with GSH and nocodazole is solved to a resolution of 1.9 A
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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
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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
recombinant enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
57.4
-
melting temperature, mutant C89A/C186A
59.6
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melting temperature, mutant C186A
60
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purified recombinant enzyme, sodium phosphate, pH 7.0, containing 5% v/v ethanol, stable up to
65 - 90
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purified recombinant enzyme, thermal unfolding in the absence and presence of small lipophilic ligands, two-state unfolding transition, overview
69.3
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melting temperature, wild-type
69.4
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melting temperature, mutant C65A
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
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
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4C, stable up to 7 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precipitation, and on a GSH Sepharose 4B and a Superdex 75 pg column
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collected from the media using a Ni-column
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glutathione-Sepharose column chromatography and Mono-Q column chromatography
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GST-Prep column chromatography
Ni-affinity column chromatography and Superdex G75 gel filtration
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Ni-NTA agarose column chromatography and glutathione-Sepharose column chromatography
on a GSTPrep FF 16/10 column
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optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme
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recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta BL21(DE3) by nickel affinity chromatography and gel filtration
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recombinant enzyme
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recombinant GST-tagged truncated enzyme mutant C65A/C167A from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, and dialysis
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recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, gel filtration, and dialysis
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recombinant PDGS
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recombinant PGDS
recombinant PGDS-glutathione transferase fusion protein
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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
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two-step purification method using cerebrospinal fluid
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in 3T3-L1 cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli C41(DE3) cells
expression as glutathione S-transferase fusion protein in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli; expression of cDNA in Escherichia coli
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expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta BL21(DE3)
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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)
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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for expression in Escherichia coli BL21DE3 cells
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for expression in Escherichia coli cells
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into the vector pET17b for expression in Escherichia coli BL21DE3 cells
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into the vector pT7-7 for expression in Escherichia coli BL21DE3 cells
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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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mutant C65A is expressed in Escherichia coli BL21(DE3) cells
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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
enzyme expression is increased in H2O2-treated neuronal cells
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expression levels of L-PGDS mRNA and protein are significantly increased after 14 days of hypoxia
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L-PGDS knockout mice are generated
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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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level of L-PGDS mRNA expression decreases as gastritis becomes more severe
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lipopolysaccharide, LPS, reduces H-PGDS expression
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G59C
C59 is an essential residue for enzyme activity in mammals. Mutant G59C does not show enzymic activity
C65A
-
inactive
C65A/C167A
C89A/C167A/C186A
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site-directed mutagenesis
C89A/C186A
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site-directed mutagenesis
D93N
-
not activated by Ca2+ or Mg2+
D96N
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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
M94A
-
the mutation reduces the catalytic efficiency
S45A
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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
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mutant retains wild-type like activity and is stable
DELTA1-24_C65A
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mutant
DELTA1-24_C65A L-PGDS
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mutant, preserves a disulfide bond between Cys89 and Cys186
DELTA1-24_C65A+H111A
-
mutant
DELTA1-24_C65A+P110A
-
mutant
DELTA1-24_C65A+W54A
-
mutant
DELTA1-24_L-PGDS
-
mutant
DELTA1-24_L-PGDS+H111A
-
mutant
DELTA1-24_L-PGDS+H116A
-
mutant
DELTA1-24_L-PGDS+P110A
-
mutant
DELTA1-24_L-PGDS+S45A
-
mutant
DELTA1-24_L-PGDS+S45A/S81A
-
mutant
DELTA1-24_L-PGDS+S45A/T67A
-
mutant
DELTA1-24_L-PGDS+S45A/T67A/S81A
-
mutant
DELTA1-24_L-PGDS+S81A
-
mutant
DELTA1-24_L-PGDS+T67A
-
mutant
DELTA1-24_L-PGDS+T67A/S81A
-
mutant
DELTA1-24_L-PGDS+W45A
-
mutant
DELTA1-24_L-PGDS+W54A/H111A
-
mutant
W54A
-
mutant retains wild-type like activity and is stable
A106S
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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
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
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 hide
LITERATURE
analysis
medicine
nutrition
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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
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optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme