Information on EC 5.3.99.2 - Prostaglandin-D synthase

SeCl4

Sulfobromophthalein

Tributyltin acetate

0.00009 mM, 50% inhibition

tributyltin bromide

Gallus gallus

0.00003 mM, 50% inhibition

Tributyltin chloride

Gallus gallus

0.00001 mM, 50% inhibition

U-46619

additional information

the lipid transporter activity of the enzyme is competitively inhibited by pamitate, stearate and arachnoate

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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%

715626

glutathione

13 entries

guanidinium hydrochloride

Mg2+

704977

phorbol 12-myrisate 13-acetate

thymic stromal lymphopoietin

stimulates mRNA synthesis

Urea

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0.0023 - 0.5

(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate

8 entries

3 - 5

1-chloro-2,4-dinitrobenzene

0.1 - 8

glutathione

5 entries

0.0005 - 0.0328

prostaglandin H2

24 entries

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0.37 - 21.7

(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate

4 entries

1-chloro-2,4-dinitrobenzene

conjugation of glutathione to 1-chloro-2,4-dinitrobenzene

2 - 15

glutathione

0.06 - 5.84

prostaglandin H2

12 entries

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110 - 27050

prostaglandin H2

12 entries

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0.075

4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine

pH 8.0

0.023

L-thyroxine

649905

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0.1

1-benzoyl piperazine

Homo sapiens;

larger than 0.100 mM

0.1

1-benzoyl piperidine

Homo sapiens;

larger than 0.100 mM

0.1

1-benzoyl-4-(methylsulfonyl)piperazine

Homo sapiens;

larger than 0.100 mM

0.1

1-phenyl-1-(2-thienyl)methanamine

Homo sapiens;

larger than 0.100 mM

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+

662057

0.000021

2-phenyl-5-(1H-pyrazol-3-yl)-1,3-thiazole

Homo sapiens;

37°C

693542

0.0007

2-phenyl-5-(1H-pyrazol-3-yl)thiazole

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0875

3-benzoylpyrrole

Homo sapiens;

0.00092

3-phenyl-5-(1H-pyrazol-3-yl)-1,2-oxazole

Homo sapiens;

37°C

693542

0.003

4-dibenzo [a,d]cyclohepten-5-ylidene-1-[4-(2H-tetrazol-5-yl)-butyl]-piperidine

Homo sapiens;

inhibition of enzyme in lipocalin-type prostaglandin-D synthase-expressing TE-671 cells after stimulation with Ca2+-ionophore A23187

0.000138 - 0.0014

4-[[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino]-2-hydroxybenzoic acid

0.0019

5-(3-aminophenyl)-N-benzhydrylthiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.023

5-amino-4-[[(3'-hydroxybiphenyl-4-yl)carbonyl]amino]-5-oxopentanoic acid

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.1

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

Homo sapiens;

larger than 0.100 mM

0.1

cyclohexyl-phenylketone

Homo sapiens;

larger than 0.100 mM

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 25°C

0.0248

N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3,3'-dihydroxybiphenyl-4-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0037

N-(1-amino-1-oxo-3-phenylpropan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0012

N-(1-amino-1-oxo-3-phenylpropan-2-yl)-6-(thiophen-2-yl)nicotinamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.001

N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-3'-hydroxybiphenyl-4-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0021

N-(1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0013

N-(1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0071

N-(1-amino-4-methyl-1-oxopentan-2-yl)-5-(3-hydroxyphenyl)-thiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.008

N-(2-amino-2-oxoethyl)-5-(3-hydroxyphenyl)thiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0108

N-(diphenylmethyl)-2-(3-hydroxyphenyl)-1,3-thiazole-4-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.0007

N-benzhydryl-5-(3-hydroxyphenyl)thiophene-2-carboxamide

Homo sapiens;

in 0.1 M Tris-HCl, pH 8.0, at 25°C

0.1

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;

37°C

693542

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 25°C

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;

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1.68

1.7

1.89

4.5

11.7

Q8QFM7;

pH 8.0, 25°C

14.9

434

wild-type, pH 8.0, 25°C

679990

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7 - 8

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additional information

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glutathione-requiring enzyme

arachnoid barrier layer

lipocalin-type prostaglandin D synthase (beta-trace) is upregulated in the alphaB-crystallin-positive astrocytes in the chronic multiple sclerosis

662954

bone marrow

glutathione-requiring enzyme

bone marrow-derived macrophage

primary cell

central nervous system

glutathione-independent enzyme

dermal dendritic cell

endometrial stromal cell

enzyme is found in luminal and glandular epithelial cells and in stroma during late pregnancy

enzyme is found in luminal and glandular epithelial cells and in stroma during late pregnancy

L-PGDS is constitutively expressed in the epithelium of the glandular base

gut

glutathione-requiring enzyme

glutathione-requiring enzyme

cultivated rat leptomeningeal cells

precursor cells of platelets, CMK cells, Dami cells. The activity is undetectable in platelets and appears during differentiation of megakaryoblasts to megakaryocytes

3119

megakaryotic cell line

plasmacytoid dendritic cell

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

epidermal melanocyte

of gut mucosa

myeloid dendritic cell

auricle, ventricle

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

secretes the enzyme

secretes the enzyme

primary bone marrow-derived macrophage

pulmonary venous myocardium

glutathione-requiring enzyme

determination of the correlation between content of enzyme in seminal plasma and on the surface of sperm

glutathione-independent enzyme

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

glutathione-requiring enzyme

uterine endometrium

vascular smooth muscle cell

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

681106

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glutathione-requiring enzyme

30425

rough endoplasmic reticulum

endoplasmic reticulum

rough endoplasmic reticulum membrane

enzyme from basophilc leukemia cell line RBL-1

outer

perinuclear L-type prostaglandin synthase/arrestin-3 co-localization is observed in prostaglandin D2-producing MG-63 cells

5634

715626

enzyme from mast cells

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Homo sapiens;

Mus musculus;

Rattus norvegicus;

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19000

x * 19000, SDS-PAGE

20000

L-PGDS

20749

x * 20749 or 21232, calculation from nucleotide sequence

3124

21000

L-PGDS bound to biliverdin

705407

21016

x * 21016, calculation from nucleotide sequence

3123

22732

Gallus gallus

x * 22732, deduced from nucleotide sequence

23000

23298

x * 23298, deduced from nucleotide sequence

649720

23359

x * 23359, deduced from nucleotide sequence

25000

26000

28000

x * 28000, SDS-PAGE, molecular mass is the same for several isoforms showing pI values from 4.2 to 7.0

682618

28600

Danio rerio

Q8QGV4;

x * 28600, calculated

34000

gel filtration

80000

1 * 80000, SDS-PAGE

80000 - 85000

85000

gel filtration

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dimer

crystallization

homodimer

2 * 23000 Da

monomer

additional information

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glycoprotein

5 entries

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crystals of H-PGDS are first grown by hanging-drop vapor diffusion method with PEG6000 as the precipitant at 20°C in the presence of 5 mM Mg2+ and the native crystals are then soaked in the precipitant solution with a saturating concentration of 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride for 2 weeks. Structure of the enzyme complexed with 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride at 1.9 A resolution in the presence of Mg2+. The styryl group of the inhibitor penetrates to the bottom of the active site cleft, and the tetrazole ring is stabilized by the stacking interaction with TRp104, inducing large movement around the alpha5-helix, which causes the space group of the complex crystal to change from P2(1) to P1 upon binding of 2-(2'-benzothiazolyl)-5-styryl-3-(4'-phthalhydrazyl) tetrazolium chloride

662057

H-PGDS is crystallized in a microgravity environment at 20°C, using 30% (w/v) PEG 6000, 10 mM dithiothreitol, 10 mM glutathione, 1% (v/v) dioxane and 1 mM magnesium chloride in 50 mM Tris-HCl pH 8.4

713649

macro-seeding using a solution containing 14% polyethylene glycol 6000, 50 mM Tris-HCl, pH 8.4, 5 mM reduced glutathione, 5 mM dithiothreitol, 2.5 mM CaCl2 or MgCl2 and 1% dioxane, structure resolution at 1.8 A

mutant C65A in complex with oleic acid and palmitoleic acid, hanging drop vapor diffusion method, using 0.1 M citric acid (pH 4.0) and 1.7 M ammonium sulfate

purified His-tagged recombinant enzyme, in complex with 9,11-epoxymethano prostaglandin H2, hanging drop vapor diffusion method, condition A: 0.1 M potassium thiocyanate and 30% PEG-MME 2000 in 1:1 protein-reservoir ratio, 5 days, 4°C, condition B: 1.4 M tri-sodium citrate, pH 6.5, using a similar method except in 2:1 protein-reservoir ratio. Micro-crystals from condition A are used to seed crystallization of ligand-free L-PGDS in the same condition but in the absence of SA U44069. Cryoprotection of condition A crystals using reservoir with 25% glycerol added, while crystals from condition B are cryo-protected with 1.6 M tri-sodium citrate solution. X-ray diffraction structure analysis at 1.88-2.09 A resolution

728090

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

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4°C, 24 h, 40% loss of activity

3098

4°C, 24 h, 5% loss of activity

3098

4°C, 24 h, 40% loss of activity

3098

4°C, 24 h, 60% loss of activity

3098

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57.4

melting temperature, mutant C89A/C186A

59.6

melting temperature, mutant C186A

purified recombinant enzyme, sodium phosphate, pH 7.0, containing 5% v/v ethanol, stable up to

65 - 90

purified recombinant enzyme, thermal unfolding in the absence and presence of small lipophilic ligands, two-state unfolding transition, overview

69.3

melting temperature, wild-type

69.4

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 60.3°C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions

692292

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glutathione prevents inactivation

3099

thiol compounds, including glutathione stabilize

3100

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-80°C, stable for at least 1 month

3100

22°C, stable for one month

4°C, 24 h, 50% loss of activity

3098

4°C, stable up to 7 weeks

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4 entries

by ammonium sulfate precipitation, and on a GSH Sepharose 4B and a Superdex 75 pg column

704977

collected from the media using a Ni-column

704365

glutathione-Sepharose column chromatography and Mono-Q column chromatography

713649

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

optimized expression protocol for recombinant enzyme in Escherichia coli and purification protocol yielding large amounts of isotopically labeled enzyme

recombinant C-terminally His6-tagged enzyme from Escherichia coli strain Rosetta BL21(DE3) by nickel affinity chromatography and gel filtration

recombinant enzyme

recombinant GST-tagged truncated enzyme mutant C65A/C167A from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, and dialysis

727534

recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography, gel filtration, and dialysis

recombinant PDGS

recombinant PGDS

recombinant PGDS-glutathione transferase fusion protein

649905

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

705407

two-step purification method using cerebrospinal fluid

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9 entries

expressed in 3T3-L1 cells

714066

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli C41(DE3) cells

expression as glutathione S-transferase fusion protein in Escherichia coli

692921

expression in Escherichia coli

expression in Escherichia coli; expression of cDNA in Escherichia coli

649547

expression of C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta BL21(DE3)

728090

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)

727534

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)

for expression in Escherichia coli BL21DE3 cells

705407

for expression in Escherichia coli cells

into the vector pET17b for expression in Escherichia coli BL21DE3 cells

into the vector pT7-7 for expression in Escherichia coli BL21DE3 cells

704977

into the vectors pUB6/V5-His and pIRESneo, cDNA of positions 76-648 is cloned into the vector pGEM-T Easy

704365

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

705307

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enzyme expression is increased in H2O2-treated neuronal cells

expression levels of L-PGDS mRNA and protein are significantly increased after 14 days of hypoxia

702057

L-PGDS knockout mice are generated

705932

L-PGDS, but not H-PGDS, is induced on fibroblasts close to infiltrating cells in the Helicobacter pylori-infected gastric mucosa

705307

level of L-PGDS mRNA expression decreases as gastritis becomes more severe

705307

lipopolysaccharide, LPS, reduces H-PGDS expression

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

705351

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

705351

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G59C

Danio rerio

Q8QGV4;

C59 is an essential residue for enzyme activity in mammals. Mutant G59C does not show enzymic activity

C65A

inactive

C65A/C167A

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

M94A

the mutation reduces the catalytic efficiency

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

692921

C89A/C186A

mutant retains wild-type like activity and is stable

DELTA1-24_C65A

mutant

DELTA1-24_C65A L-PGDS

mutant, preserves a disulfide bond between Cys89 and Cys186

DELTA1-24_C65A+H111A

mutant

DELTA1-24_C65A+P110A

mutant

DELTA1-24_C65A+W54A

mutant

DELTA1-24_L-PGDS

mutant

DELTA1-24_L-PGDS+H111A

mutant

DELTA1-24_L-PGDS+H116A

mutant

DELTA1-24_L-PGDS+P110A

mutant

DELTA1-24_L-PGDS+S45A

mutant

DELTA1-24_L-PGDS+S45A/S81A

mutant

DELTA1-24_L-PGDS+S45A/T67A

mutant

DELTA1-24_L-PGDS+S45A/T67A/S81A

mutant

DELTA1-24_L-PGDS+S81A

mutant

DELTA1-24_L-PGDS+T67A

mutant

DELTA1-24_L-PGDS+T67A/S81A

mutant

DELTA1-24_L-PGDS+W45A

mutant

DELTA1-24_L-PGDS+W54A/H111A

mutant

W54A

mutant retains wild-type like activity and is stable

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

682619

C156L

loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity

C156Y

loss of prostaglandin D synthase activity, retention of glutathione S-transferase activity

C186A

C65A

C65A/C89A/C186A

mutant is properly folded with well-defined tertiary structures

C89A/C186A

D51A

creation of new glycosylation site 1, significant inhibition of the ability of enzyme to induce apoptosis and significant decrease in catalytic activity

682619

D78A

creation of new glycosylation site 2, no significant changes in enzyme activity or ability to induce apoptosis

682619

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

12 entries

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complete recovery of activity after denaturation with 2 M guanidinium hydrochloride or 4 M urea

649547

thermal unfolding is completely reversible at pH 4.0. Differential scanning calorimetry data show no concentration dependency. Presence of an intermediate state I between the native state N and the unfolded state U. Transition temperatures of the N-I and I-U transitions are 48.2 and 60.3°C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions

692292