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Information on EC 1.1.1.141 - 15-hydroxyprostaglandin dehydrogenase (NAD+) and Organism(s) Homo sapiens and UniProt Accession P15428
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EC Tree
1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+)IUBMB Comments
Acts on prostaglandin E2, F2alpha and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
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Word Map
- 1.1.1.141
- cox-2
- cyclooxygenase-2
- fetal
-
arachidonic
- pregnancy
- chorion
- labor
-
pgf2alpha
- indomethacin
-
parturition
-
nsaid
- trophoblast
-
preterm
- myometrium
-
chemoprevention
-
15-keto
-
eicosanoids
-
thromboxane
-
prostanoids
- decidua
- synthase-1
-
nadp-linked
-
15-keto-pge2
-
clubbing
-
cesarean
- osteoarthropathy
- prostacyclin
- amnion
-
beta-hydroxysteroid
-
lipoxins
- calcitriol
-
9-ketoreductase
- medicine
-
slco2a1
-
6-keto-pgf1
- drug development
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
15-pgdh, 15-hydroxyprostaglandin dehydrogenase, prostaglandin dehydrogenase, 15-prostaglandin dehydrogenase, 15-hydroxy prostaglandin dehydrogenase, nad+-dependent 15-hydroxyprostaglandin dehydrogenase, 15-oh-pgdh, nad-dependent 15-hydroxyprostaglandin dehydrogenase, 15-hydroxyprostaglandin-dehydrogenase, 15-hydroxy-prostaglandin-dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAD+-dependent 15-hydroxyprostaglandin dehydrogenase
-
nicotinamide adenine dinucleotide-dependent 15-hydroxyprostaglandin dehydrogenase
-
11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase
-
-
-
-
15-hydroxyprostaglandin dehydrogenase
-
-
15-hydroxyprostanoic dehydrogenase
-
-
-
-
15-OH-PGDH
-
-
-
-
15-PGDH
-
-
dehydrogenase, 15-hydroxyprostaglandin
-
-
-
-
NAD+-dependent 15-hydroxyprostaglandin dehydrogenase
-
-
NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I)
-
-
-
-
NAD+-linked 15-hydroxyprostaglandin dehydrogenase
-
-
NAD-specific 15-hydroxyprostaglandin dehydrogenase
-
-
-
-
PGDH
prostaglandin dehydrogenase
PGDH
-
-
-
-
prostaglandin dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
single displacement mechanism
-
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
ordered bi-bi-mechanism
-
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
displacement reaction mechanism, at pH 7.0 a kinetically significant ternary complex is formed, while at pH 9.0 the ternary complex is not kinetically significant, Theorell-Chance mechanism
-
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
residues and domains involved in catalysis and substrate binding, overview
-
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
substrate binidng and catalytic mechanism of the enzyme, homology modeling, docking and molecular dynamics simulation, residues Gln148, Ser138, Tyr151, and Lys155 are important, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase
Acts on prostaglandin E2, F2alpha and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
CAS REGISTRY NUMBER
COMMENTARY
9030-87-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
?
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
-
-
i.e. 15-hydroxyprostaglandin or (15S)-PGE2
-
r
(5Z,8E,10E,12S)-12-hydroxy-5,8,10-heptadecatrienoic acid + NAD+
(5Z,8E,10E)-12-oxo-5,8,10-heptadecatrienoic acid + NADH
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
15(S)-hydroperoxy-5,8,11,13-(Z,Z,Z,E)-eicosatetraenoic acid + NAD+
15-oxo-5,8,11,13-(Z,Z,Z,E)-eicosatetraenoic acid + NADH
-
-
-
-
?
5,6-chrysenequinone + NADH
? + H2O2
-
formation of potentially hazardous semiquinones, reaction mechanism, overview
-
-
?
6-ketoprostaglandin F1alpha + NAD+
6,15-diketoprostaglandin F1alpha + NADH + H+
-
-
-
?
9,10-phenanthrenequinone + NADH
? + H2O2
-
formation of potentially hazardous semiquinones, reaction mechanism, overview
-
-
?
prostaglandin D1 + NAD+
15-ketoprostaglandin D1 + NADH + H+
-
very low activity
-
?
prostaglandin E1 + NAD+
15-ketoprostaglandin E1 + NADH + H+
-
-
-
-
?
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
?
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
?
prostaglandin E2 + NAD+
15-oxoprostaglandin E2 + NADH + H+
-
-
-
?
prostaglandin E2 + NAD+
15-oxoprostaglandin E2 + NADH + H+
-
-
-
?
prostaglandin E2 + NAD+
15-oxoprostaglandin E2 + NADH + H+
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
r
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
i.e. prostaglandin E1
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
i.e. prostaglandin E1
i.e. 15-ketoprostaglandin E1
r
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
catabolism of (15S)-PGE2
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
first step in prostaglandin catabolism
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
first step in prostaglnadin catabolism
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
i.e. 15-hydroxyprostaglandin or (15S)-PGE2
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
key step in prostaglandin catabolism, enzyme activation leads to reduced cell proliferation, the enzyme is an antagonist of ibuprofen
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
key step in prostaglandin inactivation
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
PGE2 degradation
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
prostaglandin E2, PGE2, a proinflammatory bioactive lipid, promotes cancer progression by modulating proliferation, apoptosis, and angiogenesis, PGE2 is a downstream product cyclooxygenase and is biochemically inactivated by the enzyme
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
reciprocal regulation of cyclooxygenase-2 and 15-hydroxyprostaglandin dehydrogenase expression in A549 human lung adenocarcinoma cells, overview
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
the enzyme is a putative cyclooxygenase-2 antagonist and and tumor suppressor
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
transcriptional regulation and biological functions, the enzyme cooperates with cyclooxygenase-2 to control cellular prostaglandin levels, reciprocal regulation of the two enzymes, overview
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
i.e. 15-hydroxyprostaglandin or (15S)-PGE2, inactivation
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
i.e. 15-hydroxyprostaglandin or (15S)-PGE2, substrate binding structure analysis, determination of interactions
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
i.e. 15-hydroxyprostaglandin or PGE2
-
-
?
(5Z,8E,10E,12S)-12-hydroxy-5,8,10-heptadecatrienoic acid + NAD+
(5Z,8E,10E)-12-oxo-5,8,10-heptadecatrienoic acid + NADH
-
-
-
?
(5Z,8E,10E,12S)-12-hydroxy-5,8,10-heptadecatrienoic acid + NAD+
(5Z,8E,10E)-12-oxo-5,8,10-heptadecatrienoic acid + NADH
-
-
-
?
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
-
-
-
?
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
-
-
-
?
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
-
-
-
?
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
-
-
-
?
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
-
specific for NAD+
-
?
11alpha,15(S)-dihydroxy-9-ketoprost-5,13-dienoic acid + NAD(P)+
11alpha-hydroxy-9,15-diketoprost-5,13-dienoic acid + NADH
-
specific for NAD+
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
-
-
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
physiological inactivation of prostaglandin by catalyzing the first step in catabolism
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
physiological inactivation of prostaglandin by catalyzing the first step in catabolism
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
physiological inactivation of prostaglandin by catalyzing the first step in catabolism
-
?
prostaglandin E2 + NAD+
15-ketoprostaglandin E2 + NADH + H+
-
-
-
-
?
prostaglandin E2 + NAD+
15-ketoprostaglandin E2 + NADH + H+
-
the wild type enzyme is highly active against prostaglandin E2 and NAD+
-
-
?
prostaglandin F2alpha + NAD+
15-ketoprostaglandin F2alpha + NADH + H+
-
-
-
?
prostaglandin F2alpha + NAD+
15-ketoprostaglandin F2alpha + NADH + H+
-
-
-
?
prostaglandin F2alpha + NAD+
15-ketoprostaglandin F2alpha + NADH + H+
-
-
-
?
prostaglandin F2alpha + NAD+
15-ketoprostaglandin F2alpha + NADH + H+
-
specific for NAD+
-
?
prostaglandin F2alpha + NAD+
15-ketoprostaglandin F2alpha + NADH + H+
-
specific for NAD+
-
?
additional information
?
-
-
dexamethasone and phorbol ester play a role in enzyme regulation in erythroleukemia cells
-
-
?
additional information
?
-
-
key enzyme for metabolic inactivation of prostaglandins, enzyme levels are reduced in inflammatory bowel disease involving TNF-alpha
-
-
?
additional information
?
-
-
the enzyme is a tumor suppressor of human breast cancer, expression of the enzyme and the estrogen receptor is correlated, silencing of the enzyme results in enhanced cancer cell proliferation, the enzyme expression is silenced in vivo in cancer cells due to promoter methylation
-
-
?
additional information
?
-
-
the enzyme is involved in anti-proliferative effect of non-steroidal anti-inflammatory drugs COX-1 inhibitors on a medullary thyroid carcinoma cell line
-
-
?
additional information
?
-
-
15-hydroxyprostaglandin dehydrogenase may be repressed by an epigenetic mechanism involving histone deacetylation, resulting in increased prostaglandin E2 activity in tumors
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
-
-
i.e. 15-hydroxyprostaglandin or (15S)-PGE2
-
r
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
?
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
?
prostaglandin E2 + NAD+
15-oxoprostaglandin E2 + NADH + H+
-
-
-
?
prostaglandin E2 + NAD+
15-oxoprostaglandin E2 + NADH + H+
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
-
-
-
r
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
catabolism of (15S)-PGE2
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
first step in prostaglandin catabolism
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
first step in prostaglnadin catabolism
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
key step in prostaglandin catabolism, enzyme activation leads to reduced cell proliferation, the enzyme is an antagonist of ibuprofen
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
key step in prostaglandin inactivation
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
PGE2 degradation
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
prostaglandin E2, PGE2, a proinflammatory bioactive lipid, promotes cancer progression by modulating proliferation, apoptosis, and angiogenesis, PGE2 is a downstream product cyclooxygenase and is biochemically inactivated by the enzyme
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
reciprocal regulation of cyclooxygenase-2 and 15-hydroxyprostaglandin dehydrogenase expression in A549 human lung adenocarcinoma cells, overview
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
the enzyme is a putative cyclooxygenase-2 antagonist and and tumor suppressor
-
-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
-
transcriptional regulation and biological functions, the enzyme cooperates with cyclooxygenase-2 to control cellular prostaglandin levels, reciprocal regulation of the two enzymes, overview
-
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
physiological inactivation of prostaglandin by catalyzing the first step in catabolism
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
physiological inactivation of prostaglandin by catalyzing the first step in catabolism
-
?
15-hydroxyprostaglandin + NAD+
15-oxoprostaglandin + NADH + H+
-
physiological inactivation of prostaglandin by catalyzing the first step in catabolism
-
?
additional information
?
-
-
dexamethasone and phorbol ester play a role in enzyme regulation in erythroleukemia cells
-
-
?
additional information
?
-
-
key enzyme for metabolic inactivation of prostaglandins, enzyme levels are reduced in inflammatory bowel disease involving TNF-alpha
-
-
?
additional information
?
-
-
the enzyme is a tumor suppressor of human breast cancer, expression of the enzyme and the estrogen receptor is correlated, silencing of the enzyme results in enhanced cancer cell proliferation, the enzyme expression is silenced in vivo in cancer cells due to promoter methylation
-
-
?
additional information
?
-
-
the enzyme is involved in anti-proliferative effect of non-steroidal anti-inflammatory drugs COX-1 inhibitors on a medullary thyroid carcinoma cell line
-
-
?
additional information
?
-
-
15-hydroxyprostaglandin dehydrogenase may be repressed by an epigenetic mechanism involving histone deacetylation, resulting in increased prostaglandin E2 activity in tumors
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3,3-dimethylpiperidin-1-yl)[1-(3-methylphenyl)-1H-benzimidazol-5-yl]methanone
-
(3,5-dimethylpiperidin-1-yl)[1-(3-methylphenyl)-1H-benzimidazol-5-yl]methanone
-
(4-bromopiperidin-1-yl)[1-(3-methylphenyl)-1H-benzimidazol-5-yl]methanone
-
(piperidin-1-yl)[1-[3-(propan-2-yl)phenyl]-1H-benzimidazol-5-yl]methanone
-
(piperidin-1-yl)[1-[3-(trifluoromethyl)phenyl]-1H-benzimidazol-5-yl]methanone
-
(piperidin-1-yl)[1-[4-(trifluoromethyl)phenyl]-1H-benzimidazol-5-yl]methanone
-
2-[[(6-bromo-3H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl]benzonitrile
-
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-5,6,7,8,9,10-hexahydro[1,2,4]triazolo[4,3-a]azocine
-
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyridine
-
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9,10,11-hexahydro-5H-[1,2,4]triazolo[4,3-a]azonine
-
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-pyrrolo[1,2-a]azepine
-
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7-dihydro-5H-pyrrolo[2,1-c][1,2,4]triazole
-
3-[1-(3,4-dichlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[1-(3-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[1-(4-bromophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[1-(4-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[1-(4-fluorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[1-(4-methoxyphenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[1-(4-tert-butylphenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-(4-methylphenyl)-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-(4-nitrophenyl)-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-[4-(naphthalen-2-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-[4-(pyridin-2-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-[4-(pyridin-3-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-[4-(pyridin-4-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-1-[4-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
3-[2,5-dimethyl-3-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepin-3-yl)-1H-pyrrol-1-yl]benzonitrile
-
4-[2,5-dimethyl-3-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepin-3-yl)-1H-pyrrol-1-yl]benzonitrile
-
5-(2-chloro-3-(2-(pyridin-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(2-chloro-4-(2-(cyclohexyloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(2-chloro-4-(2-(propan-2-yloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(2-chloro-4-(2-cyclopentylethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-((4-(prop-1-en-2-yl)cyclohexyl)methoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-((5-oxo-5,6,7,8-tetrahydronaphthalen-1-yl)oxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(4-methyl-1,3-thiazolidin-5-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(5-ethylpyridin-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(5-nitrofuran-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(cyclohexyloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(propan-2-yloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(pyridin-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-(thiophen-2-yl)ethoxy)benzylidene)thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-cyclopentylethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-cyclopropylpropyl)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(2-thiomorpholine 1,1-dioxideethoxy)benzylidene)thiazolidine-2,4-dione
-
5-(3-chloro-4-(3-(2-nitroethenyl)phenoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(cyclobutylmethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(3-chloro-4-(cyclopentylmethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
-
5-(4-(1,3-benzodioxol-5-ylmethoxy)-3-chlorobenzylidene)-1,3-thiazolidine-2,4-dione
-
5-(4-(bicyclo[2.2.1]hept-2-ylmethoxy)-3-chlorobenzylidene)-1,3-thiazolidine-2,4-dione
-
ethyl 4-[2,5-dimethyl-3-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepin-3-yl)-1H-pyrrol-1-yl]benzoate
-
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](3-methylpiperidin-1-yl)methanone
-
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](3-phenylpiperidin-1-yl)methanone
-
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](4-methylpiperazin-1-yl)methanone
-
[1-(3-methylphenyl)-1H-benzimidazol-5-yl][3-(propan-2-yl)piperidin-1-yl]methanone
-
[1-(3-methylphenyl)-1H-benzimidazol-5-yl][3-(trifluoromethyl)piperidin-1-yl]methanone
-
[1-(3-methylphenyl)-1H-benzimidazol-5-yl][4-(trifluoromethyl)piperidin-1-yl]methanone
-
(4-([(4-chlorophenyl)sulfanyl]methyl)phenyl)(4-methylpiperidin-1-yl)methanone
-
-
(5Z)-5-[3-bromo-4-(2-cyclohexylethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[3-chloro-4-(2-cyclohexylethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[3-chloro-4-(3-cyclohexylpropoxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[3-chloro-4-(4-cyclohexylbutoxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[3-chloro-4-(cyclohexylmethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[4-(2-cyclohexylethoxy)-3-methoxybenzylidene]-1,3-thiazolidine-2,4-dione
-
-
(5Z)-5-[4-(2-cyclohexylethoxy)-3-methoxybenzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
-
-
2-hydroxy-5-(3,5-dimethoxycarbonyl-benzoyl)-benzene acetic acid
-
1000 times more potent inhibitor than sulfaphasalazine
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
-
-
5-[4-((1-methyl)-cyclohexylmethoxy)benzyl]-2,4-thiazolidenedione
-
trivial name ciglitazone
5-[[4-(ethoxycarbonyl)phenyl]azo]-2-hydroxy-benzeneacetic acid
-
CAY-10397, specific 15-PGDH inhibitor
CAY 10397
-
specific inhibitor, completely reverses the stimulating effect of ibuprofen on cell proliferation in TT cells
mixture of endogenous fatty acids
-
mixture contains palmitic acid, stearic acid linoleic acid and oleic acid, competitive vs. prostaglandine E2
-
[4-(4-methoxyphenyl)piperazin-1-yl](4-[(phenylsulfanyl)methyl]phenyl)methanone
-
-
1,2-naphthoquinone
-
0.0002 mM, time dependent inactivation, 1 mM glutathione or 40% glycerol protect from inactivation
12-O-tetradecanoylphorbol-13-acetate
-
10 nM, rapid loss of activity in eryrthroleukemia cells during 40 min, inhibition can be prevented by staurosporin indicating that protein kinase C is involved
12-O-tetradecanoylphorbol-13-acetate
-
induces the synthesis of 15-PGDH but inhibits the enzyme activity a protein kinase C mediated mechanism
7,8-benzo[a]pyrenequinone
-
0.0002 mM, time dependent inactivation, 40% glycerol protects from inactivation
additional information
-
histone deacetylase inhibitors, such as sodium butyrate, scriptaid, apicidin, and oxamflatin, and transforming growth factor-beta, TGF-beta1, induce enzyme expression in lung adenocarcinoma cells, overview
-
additional information
-
interleukin-1beta suppresses the enzyme expression, as well as down-regulation of cyclooxygenase-2 expression, whereas down-regulation of cyclooxygenase-1 has no effect on 15-PGDH expression, overview
-
additional information
-
pH-dependent inhibition and inhibition mechanism, at high substrate concentrations there is formation of unreactive complexes between the 15-hydroxyrostaglandin and both the free enzyme and enzyme-NADH complex and between the 15-ketoprostaglandin and both the free enzyme and enzyme NAD+ complex
-
additional information
-
the enzyme expression is suppressed by the epidermal growth factor via snail which interacts through its zinc finger structure, mechanism overview
-
additional information
-
TNF-alpha suppresses the enzyme expression in colonocytes
-
additional information
-
bile acids activate the signal transduction pathway protein kinase C-> extracellular signal-regulated kinase 1/2-> early growth response factor-1-> Snail and thereby suppress 15-PGDH transcription, unconjugated bile acids are much more potent inhibitors of 15-PGDH expression and activity than related conjugated bile acids, chenodeoxycholate and deoxycholate suppress the transcription of 15-PGDH resulting in reduced amounts of mRNA, protein, and enzyme activity
-
additional information
-
histone deacetylase 2 and the transcriptional regulator Snail play a central role in the suppression of 15-PGDH expression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
erlotinib
-
epidermal growth factor receptor tyrosine kinase inhibitor, trreatment of cells increases the expression of the enzyme in a subset of non-small-cell lung cancer lines
pioglitazone
-
upregulation of expression, involving peroxisome proliferator-activated receptor gamma. Upregulation results in reduced production of prostaglandin E2 and finally inhibition of lung cancer growth
rosiglitazone
-
upregulation of expression, involving peroxisome proliferator-activated receptor gamma. Upregulation results in reduced production of prostaglandin E2 and finally inhibition of lung cancer growth
Thionicotinamide adenine dinucleotide
-
5-33% of the activity with NAD+, depending on substrate
additional information
-
12-O-tetradecanoylphorbol-13-acetate induces the synthesis of 15-PGDH but inhibits the enzyme activity a protein kinase C mediated mechanism
-
additional information
-
enzyme activation leads to reduced cell proliferation
-
additional information
-
enzyme expression is inducible by indomethacin in LS174T cells, but not in HCA-7 and HCT-15 cells, and also not in enzyme-deficient HCT-116
-
additional information
-
enzyme up-regulation by the tumor suppressor gene CAAT/enhancer binding protein alpha
-
additional information
-
the enzyme is induced by the androgens dihydrotestosterone or testosterone and, to a lesser extent, by 17beta-estradiol and progesterone in androgen-sensitive LNCaP cells, not in hormone-independent PC3 cells, the induction of 15-PGDH is not blocked by steroid receptor antagonist RU 486 nor by antiandrogen, flutamide, but is inhibited by tyrosine kinase inhibitor, genistein, and by ERK kinase inhibitor, PD 98059, but not by protein kinase C inhibitor GF109203X, thus androgens induce 15-PGDH gene expression through an unconventional nongenomic pathway, no induction by dexamethasone, hydrocortisone, and RU 486
-
additional information
-
15-PGDH expression is increased by hepatocyte nuclear factor 3beta in lung cancer cells
-
additional information
-
flurbiprofen induces 15-PGDH expression in cancer cells, PD98059 and U-0126 elevate 15-PGDH levels very significantly
-
additional information
-
treatment of colorectal cancer cells with 5-aza-2'-deoxycytidine, 5 mM sodium butyrate or 5 mM valproic acid induces an increase in 15-PGDH protein expression
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
0.0012
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, I17L mutant
0.0026
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, N91D mutant
0.0034
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5
0.0035
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, V186K mutant
0.0045
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, V186A mutant
0.006
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, N91A mutant
0.0063
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5
0.0071
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5
0.0086
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, T11S mutant
0.011
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, I17A mutant
0.011
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, I17V mutant
0.013
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, Q15K/W37K double mutant
0.022
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, V186I mutant
0.026
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, Q15K mutant
0.0028
prostaglandin E2
-
pH 8.0, 25°C, 20 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
0.0037
prostaglandin E2
-
pH 8.0, 25°C, 10 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
0.0056
prostaglandin E2
-
pH 8.0, 25°C, 4 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
0.0064
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
0.0075
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
0.0135
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
37
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, V186K mutant
45
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, N91D mutant
73
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, N91A mutant
78
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, V186A mutant
127
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, I17A mutant
143
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, I17V mutant
210
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, I17L mutant
262
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate
-
37°C, pH 7.5, V186I mutant
6.1
prostaglandin E2
-
pH 8.0, 25°C, 20 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
7.5
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
10.3
prostaglandin E2
-
pH 8.0, 25°C, 10 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
11.1
prostaglandin E2
-
pH 8.0, 25°C, 4 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
12.4
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
14.1
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
900
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
1200
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
1800
prostaglandin E2
-
pH 8.0, 25°C, 10 nM 2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
2000
prostaglandin E2
-
pH 8.0, 25°C, 4 nM 3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
2100
prostaglandin E2
-
pH 8.0, 25°C, 20 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
2800
prostaglandin E2
-
pH 8.0, 25°C, 10 nM [1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0006
5-[4-((1-methyl)-cyclohexylmethoxy)benzylidene]-2,4-thiazolidenedione
-
37°C, pH 7.5
0.0022
5-[4-((1-methyl)-cyclohexylmethoxy)benzyl]-2,4-thiazolidenedione
-
37°C, pH 7.5
0.00009
5-[4-(cyclohexylethoxy)benzylidene]-2,4-thiazolidenedione
-
37°C, pH 7.5
0.00027
5-[4-(cyclohexylmethoxy)benzylidene]-2,4-thiazolidenedione
-
37°C, pH 7.5
0.00011
5-[4-(cyclohexylpropoxy)benzylidene]-2,4-thiazolidenedione
-
37°C, pH 7.5
additional information
additional information
-
0.0189, endogenous mixture of palmitic, stearic, oleic and linoleic acid
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000068
(1-butyl-1H-benzimidazol-5-yl)(piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000022
(1-phenyl-1H-benzimidazol-5-yl)(piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000034
(1-tert-butyl-1H-benzimidazol-5-yl)(piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000068
(3,3-dimethylpiperidin-1-yl)[1-(3-methylphenyl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000271
(3,5-dimethylpiperidin-1-yl)[1-(3-methylphenyl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000076
(4-bromopiperidin-1-yl)[1-(3-methylphenyl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000068
(piperidin-1-yl)[1-[3-(propan-2-yl)phenyl]-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000048
(piperidin-1-yl)[1-[3-(trifluoromethyl)phenyl]-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.00086
(piperidin-1-yl)[1-[4-(trifluoromethyl)phenyl]-1H-benzimidazol-5-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000242
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-5,6,7,8,9,10-hexahydro[1,2,4]triazolo[4,3-a]azocine
Homo sapiens
pH and temperature not specified in the publication
0.000192
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-5,6,7,8-tetrahydro[1,2,4]triazolo[4,3-a]pyridine
Homo sapiens
pH and temperature not specified in the publication
0.000383
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9,10,11-hexahydro-5H-[1,2,4]triazolo[4,3-a]azonine
Homo sapiens
pH and temperature not specified in the publication
0.000054
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-pyrrolo[1,2-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.00304
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7-dihydro-5H-pyrrolo[2,1-c][1,2,4]triazole
Homo sapiens
pH and temperature not specified in the publication
0.000022
3-[1-(3,4-dichlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000034
3-[1-(3-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000048
3-[1-(4-bromophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000038
3-[1-(4-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000121
3-[1-(4-fluorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000086
3-[1-(4-methoxyphenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000136
3-[1-(4-tert-butylphenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000034
3-[2,5-dimethyl-1-(4-methylphenyl)-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000108
3-[2,5-dimethyl-1-(4-nitrophenyl)-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000048
3-[2,5-dimethyl-1-[3-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000108
3-[2,5-dimethyl-1-[4-(naphthalen-2-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.001078
3-[2,5-dimethyl-1-[4-(pyridin-2-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000271
3-[2,5-dimethyl-1-[4-(pyridin-3-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000383
3-[2,5-dimethyl-1-[4-(pyridin-4-yl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000068
3-[2,5-dimethyl-1-[4-(trifluoromethyl)phenyl]-1H-pyrrol-3-yl]-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
pH and temperature not specified in the publication
0.000076
3-[2,5-dimethyl-3-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepin-3-yl)-1H-pyrrol-1-yl]benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.000264
4-((2,5-dioxopyrrolidin-3-ylidene)methyl)phenylthiophene-2-carboxylate
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000096
4-[2,5-dimethyl-3-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepin-3-yl)-1H-pyrrol-1-yl]benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.008915
5-(2-chloro-3-(2-(pyridin-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000211
5-(2-chloro-4-(2-(cyclohexyloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.00105
5-(2-chloro-4-(2-(propan-2-yloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000013
5-(2-chloro-4-(2-cyclohexylethoxy)benzylidene)-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000042
5-(2-chloro-4-(2-cyclopentylethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.00454
5-(2-chloro-4-(4-nitrobenzyloxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000081
5-(2-chloro-4-phenbutoxybenzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000178
5-(2-chloro-4-phenethoxybenzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000052
5-(2-chloro-4-phenpropoxybenzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000075
5-(3-chloro-4-((4-(prop-1-en-2-yl)cyclohexyl)methoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000071
5-(3-chloro-4-((5-oxo-5,6,7,8-tetrahydronaphthalen-1-yl)oxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.005165
5-(3-chloro-4-(2-(4-methyl-1,3-thiazolidin-5-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.002077
5-(3-chloro-4-(2-(5-ethylpyridin-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000123
5-(3-chloro-4-(2-(5-nitrofuran-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.00002
5-(3-chloro-4-(2-(cyclohexyloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.002738
5-(3-chloro-4-(2-(propan-2-yloxy)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.00444
5-(3-chloro-4-(2-(pyridin-2-yl)ethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000084
5-(3-chloro-4-(2-(thiophen-2-yl)ethoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000099
5-(3-chloro-4-(2-cyclopentylethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000132
5-(3-chloro-4-(2-cyclopropylpropyl)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000223
5-(3-chloro-4-(2-thiomorpholine 1,1-dioxideethoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000059
5-(3-chloro-4-(3-(2-nitroethenyl)phenoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.0001
5-(3-chloro-4-(3-nitrophenoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000038
5-(3-chloro-4-(3-phenylpropoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.00093
5-(3-chloro-4-(4-nitrobenzyloxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000048
5-(3-chloro-4-(4-phenylbutoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000009
5-(3-chloro-4-(cyclobutylmethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000011
5-(3-chloro-4-(cyclopentylmethoxy)benzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.00002
5-(3-chloro-4-phenylethoxybenzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000193
5-(4-(1,3-benzodioxol-5-ylmethoxy)-3-chlorobenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000487
5-(4-(benzyloxy)-2-chlorobenzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000048
5-(4-(benzyloxy)-3-chlorobenzylidene)thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000165
5-(4-(bicyclo[2.2.1]hept-2-ylmethoxy)-3-chlorobenzylidene)-1,3-thiazolidine-2,4-dione
Homo sapiens
at pH 7.5, temperature not specified in the publication
0.000038
ethyl 4-[2,5-dimethyl-3-(6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepin-3-yl)-1H-pyrrol-1-yl]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.000383
N,N-diethyl-1-(3-methylphenyl)-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.001358
N-butyl-1-(3-methylphenyl)-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000961
N-cyclopentyl-1-(3-methylphenyl)-1H-benzimidazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000027
[1-(2-methoxyphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000012
[1-(3-chlorophenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000019
[1-(3-methoxyphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000022
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](3-methylpiperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000429
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](3-phenylpiperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.00271
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](4-methylpiperazin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.00304
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](morpholin-4-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000019
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000383
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](pyrrolidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000048
[1-(3-methylphenyl)-1H-benzimidazol-5-yl][3-(propan-2-yl)piperidin-1-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000068
[1-(3-methylphenyl)-1H-benzimidazol-5-yl][3-(trifluoromethyl)piperidin-1-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.001524
[1-(3-methylphenyl)-1H-benzimidazol-5-yl][4-(trifluoromethyl)piperidin-1-yl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.000171
[1-(3-tert-butylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.00022
[1-(4-chlorophenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.00019
[1-(4-methoxyphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.00019
[1-(4-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000054
[1-(4-tert-butylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.000631
(4-([(4-chlorophenyl)sulfanyl]methyl)phenyl)(4-methylpiperidin-1-yl)methanone
Homo sapiens
-
pH 8, 25°C
0.000089
(4-[(2-bromophenoxy)methyl]phenyl)(piperidin-1-yl)methanone
Homo sapiens
-
pH 8, 25°C
0.000019
(5Z)-5-[3-bromo-4-(2-cyclohexylethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
(5Z)-5-[3-chloro-4-(2-cyclohexylethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
(5Z)-5-[3-chloro-4-(3-cyclohexylpropoxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000024
(5Z)-5-[3-chloro-4-(4-cyclohexylbutoxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000028
(5Z)-5-[3-chloro-4-(cyclohexylmethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000047
(5Z)-5-[3-chloro-4-(cyclohexyloxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000025
(5Z)-5-[4-(2-cyclohexylethoxy)-3-methoxybenzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.05
(5Z)-5-[4-(2-cyclohexylethoxy)-3-methoxybenzylidene]-3-methyl-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000051
(5Z)-5-[4-(2-cyclohexylethoxy)benzylidene]-1,3-thiazolidine-2,4-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000141
2-([(6-bromo-4H-imidazo[4,5-b]pyridin-2-yl)sulfanyl]methyl)benzonitrile
Homo sapiens
-
pH 8, 25°C
0.00089
3-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine
Homo sapiens
-
pH 8, 25°C
0.000052
5-(4-((4-methylcyclohexyl)methoxy)benzylidene) thiazolidine-2,4-dione
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.000031
5-(4-(2-(thiophen-2-yl)ethoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00006
5-(4-(2-(thiophen-3-yl)ethoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.000116
5-(4-(2-cyclopentylethoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.000124
5-(4-(4-(chloromethyl)benzyloxy)benzylidene) thiazolidine-2,4-dione
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.000045
5-(4-(cyclopentylmethoxy)benzylidene)thiazolidine-2,4-dione
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.000056
[1-(3-methylphenyl)-1H-benzimidazol-5-yl](piperidin-1-yl)methanone
Homo sapiens
-
pH 8, 25°C
0.01
[4-(4-methoxyphenyl)piperazin-1-yl](4-[(phenylsulfanyl)methyl]phenyl)methanone
Homo sapiens
-
value above, pH 8, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
6.1 pmol/min per 1000000 cells, enzyme activity in LNCaP cells
additional information
-
in vivo activity in absence and presence of different androgens, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
strong increase in activity between pH 8.0 and 9.5, sharp decrease above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
15-hydroxyprostaglandin dehydrogenase is expressed mainly in keratinocytes and melanocytes
invasiveapocrine carcinoma cells correspond to a distinct molecular subtype of breast carcinomas characterized by the expression of 15-prostaglandin dehydrogenase alone or in combination with a novel form of acyl-CoA synthetase medium-chain family member 1, 15-prostaglandin dehydrogenase is not expressed by other breast cancer types
in hair follicle, 15-hydroxyprostaglandin dehydrogenase is expressed mainly in keratinocytes and melanocytes
in hair follicle, 15-hydroxyprostaglandin dehydrogenase is expressed mainly in keratinocytes and melanocytes
-
non-small cell lung carcinoma cell line A549, expression of 15-PGDH is induced by dexamethason, prednisolone, betamethasone and triamcinolone
-
55000 Da form of enzyme, level increases with preterm premature rupture of membrane
-
expression of the enzyme and the estrogen receptor is correlated
-
in preterm chorion, levles of 15-hydroxyprostaglandin dehydrogenase protein and activity are lower when compared to term, and are further reduced with the presence of infection. Preterm premature rapture of membranes and subclinical inflammation do not affect the levels of 29000 Da 15-hydroxyprostaglandin dehydrogenase protein in the fetal membranes
-
-
285914, 285915, 285916, 285919, 285920, 285922, 285923, 285927, 285932, 285933, 285934, 285935, 285937, 654361, 657210, 711448
additional information
-
up-regulation of cyclooxygenase-2 expression by pro-inflammatory cytokines is accompanied by down-regluation of 15-hydroxyprostaglandin dehydrogenase expression. Over-expression of cyclooxygenase-2 but not -1 also attenuates 15-hydroxyprostaglandin dehydrogenase expression. Similarly, overexpression of 15-hydroxyprostaglandin dehydrogenase inhibits interleukin 1beta-induced cyclooxygenase-2 expression and results in apoptosis. The levels of 15-hydroxyprostaglandin dehydrogenase expression in transfected cells correlate positively with those of mesenchymal markers, and negatively with those of epithelial markers
-
loss of 15-hydroxyprostaglandin expression in 65% of lung cancers. Enzyme acts as a tumor suppressor in lung cancer
-
NSCLC cell, much lower expression of 15-hydroxyprostaglandin dehydrogenase in all NSCLC histologic groups compared with healthy lung cell. Treatment with the epidermal growth factor receptor tyrosine kinase inhibitor erlotinib increases the expression of the enzyme in a subset of NSCLC lines
-
reduced expression of 15-PGDH occurrs in tumor cells and is paralleled by decreased 15-PGDH activity in tumors
-
the amount of 15-PGDH is frequently decreased in NSCLC cells compared with adjacent normal lung
-
androgen-sensitive cancer cells LNCaP and hormone-independent PC3 cells, enzyme expression is induced by steroids
additional information
-
distribution of enzyme expression in normal and pathological tissues, overview, no enzyme expression in spleen, heart, HCT-116 cells, CacO-2 cells and Colo 201 cells
additional information
-
enzyme expression analysis, PGDH expression is repressed in multiple human cancers
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is a tumor suppressor in various malignancies including colon cancer. The product (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate (15-keto PGE2) stimulates the Nrf2-HO-1 axis through the generation of ROS in normal colon epithelial cells, which contributes to the potential role of this lipid mediator in preventing cancer development associated with oxidative stress and inflammatory tissue damage
physiological function
the enzyme inhibits cholangiocarcinoma cell proliferation and migration
malfunction
physiological function
malfunction
-
MKN45 cells stably transfected with the 15-PGDH siRNA plasmid have a significantly increased proliferation rate. SGC7901 cells (disclosing a low expression level of 15-PGDH) stably transfected with the 15-PGDH cDNA have a significantly decreased growth rate. Increased expression of 15-PGDH suppresses clone formation of gastric cancer cells in plate and soft agar colony formation assays in vitro and suppressed tumor formation in athymic nude mice in vivo. Stable silencing of 15-PGDH in gastric cancer cells also enhances cell cycle entry in vitro
malfunction
-
overexpression of 15-PGDH inhibits HCC cell growth in vitro, whereas knockdown of 15-PGDH enhances tumor growth parameters
physiological function
-
15-PGDH has a suppressive role and that its upregulation could partly reverse the malignant growth potential of gastric cancer cells both in vitro and in vivo
physiological function
-
15-PGDH inhibits hepatocellular carcinoma growth through 15-keto-PGE2/PPARgamma-mediated activation of p21WAF1/Cip1
physiological function
-
in a tumor xenograft model in severe combined immunodeficiency mice, inoculation of human HCC cells (Huh7) with overexpression of 15-PGDH leads to significant inhibition of tumor growth, whereas knockdown of 15-PGDH enhances tumor growth
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PGDH_HUMAN
266
0
28977
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
structure analysis using the tertiary complex crystal structure of the enzyme with bound NAD+ and 15-hydroxyprostaglandin, homology modeling, docking and molecular dynamics simulation, three-dimensional structure model, detailed overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of structure for mutant A140P. Mutation disrupts binding of the substrate prostaglandin E2 both because the pyrrolidine ring of Pro140 fills a space that in the wildtype complex is occupied by the prostaglandin E2 target side-chain 15-OH and because there is a resulting loss of catalytically important hydrogen bonding of the 15-OH to the nearby serine at residue 138
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A140P
Q15K/D36A/W37R
-
no activity with NAD+ as cofactor, low activity with NADP+ as cofactor
Q15K/D36S/W37R
-
no activity with NAD+ as cofactor, low activity with NADP+ as cofactor
Q15K/W37R
-
approx. 350% of wild-type activity, strong activity with NADP+ as cofactor
Q15R/W37R
-
approx. 200% of wild-type activity, strong activity with NADP+ as cofactor
S193P
-
the missense mutation in exon 6 of the human HPGD gene encoding NAD+ dependent 15-hydroxyprostaglandin dehydrogenase is involved in the pathogenesis of isolated congenital nail clubbing
Y151A
Y151F
Y151S
additional information
A140P
-
naturally occuring mutation in patients with pulmonary hypertropic osteoarthropathy. Homozygous individuals develop pulmonary hypertrophic osteoarthropathy secondary to chronically elevated prostaglandin E2 levels. Heterozygous relatives also show milder biochemical and clinical manifestations. After expression in Escherichia coli, the mutations renders the protein largely insoluble at 37°C, but mostly souble at 20°C. Mutant exhibits less than 1.5% of wild-type activity
A140P
-
the mutant shows no detectable activity, the A140P substitution renders the enzyme largely insoluble at 37°C, at 27°C, the mutant protein is partially soluble, and at 20°C it is mostly soluble
Y151F
-
site-directed mutagenesis, highly reduced activity compared to the enzyme
additional information
-
identfication of catalytically important residues by site-directed mutagenesis
additional information
-
injection of wild-type enzyme, but not mutant enzyme, into mice transfected with A549 cells, reduces the ability of the cancer cell to proliferate in the mice, transfected A549 cells overexpressing the enzyme undergo apoptosis, overview
additional information
-
interleukin-1beta suppresses the enzyme expression, as well as down-regulation of cyclooxygenase-2 expression, whereas down-regulation of cyclooxygenase-1 has no effect on 15-PGDH expression, overview, silencing of IL-1beta-induced expression of COX-2 by RNAi method
additional information
-
identification of an insertion-deletion mutation in 15-hydroxyprostaglandin dehydrogenase exon 3, this alters the open reading frame from codon 78, truncating the protein after ten altered amino acids, and of a homozygous 2-bp deletion within the duplicated dinucleotide CTCT at nucleotides 175 and 176. This alters the reading frame from residue 59 and truncates the HPGD protein at residue 65 after seven altered amino acids. Both of these predicted truncated proteins lack the entire PGE2-binding domain and cause primary hypertrophic asteoarthropathy
additional information
-
up-regulation of cyclooxygenase-2 expression by pro-inflammatory cytokines is accompanied by down-regluation of 15-hydroxyprostaglandin dehydrogenase expression. Over-expression of cyclooxygenase-2 but not -1 also attenuates 15-hydroxyprostaglandin dehydrogenase expression. Similarly, overexpression of 15-hydroxyprostaglandin dehydrogenase inhibits interleukin 1beta-induced cyclooxygenase-2 expression and results in apoptosis. The levels of 15-hydroxyprostaglandin dehydrogenase expression in transfected cells correlate positively with those of mesenchymal markers, and negatively with those of epithelial markers
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
when expression is induced at 37°C, almost all wild type recombinant HPGD protein is soluble
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the assay mix containing 50 mM Tris HCl, pH 7.5, 1 mM dithiothreitol, 100 mM prostaglandin E2 and 1 mM NAD+ at 22°C is not optimal for HPGD activity, but avoids a sharp, unphysiological pH optimum around pH 9
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 5 mM potassium phosphate, pH 7.0, 50% glycerol, 1 mM EDTA, 7 months, 10% loss of activity
-
-20°C, purified enzyme in a buffer containing 50% glycerol, 5 mM potassium phosphate, pH 7.0, and 1 mM EDTA, loss less than 10% of its initial activity in 2 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence, expression analysis and transcriptional regulation, overview
-
stable expression of wild-type and mutant enzymes in AD-293 cells using an adenovirus shuttle vector
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
15-deoxy-DELTA(12,14)-prostaglandin J2 upregulates the expression and the activity of the enzyme through reactive oxygen species-mediated activation of extracellular-signal related kinase1/2 and subsequently Elk-1 in human breast cancer MDA-MB-231 cells
15-hydroxyprostaglandin dehydrogenase is upregulated by hydroxychloroquine in rheumatoid arthritis fibroblast-like synoviocytes
enzyme mRNA levels are significantly higher in aorta samples from patients undergoing abdominal aortic aneurysm repair than in those from healthy multiorgan donors
the enzyme is downregulated in human hepatoma cells with a high cyclooxygenase-2 expression
interleukin 4 induces up-regulation of 15-PGDH expression in A549 cells as well as in other lung cancer cell lines
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
A140P is a naturally occuring mutation in patients with pulmonary hypertrophic osteoarthropathy. Homozygous individuals develop pulmonary hypertrophic osteoarthropathy secondary to chronically elevated prostaglandin E2 levels. Heterozygous relatives also show milder biochemical and clinical manifestations. Identification of an insertion-deletion mutation in 15-hydroxyprostaglandin dehydrogenase exon 3, this alters the open reading frame from codon 78, truncating the protein after ten altered amino acids, and of a homozygous 2-bp deletion within the duplicated dinucleotide CTCT at nucleotides 175 and 176. This alters the reading frame from residue 59 and truncates the HPGD protein at residue 65 after seven altered amino acids. Both of these predicted truncated proteins lack the entire PGE2-binding domain and cause primary hypertrophic osteoarthropathy
medicine
-
in non-small-cell lung cancer cells, i.e. NSCLC cells, much lower expression of 15-hydroxyprostaglandin dehydrogenase in all histologic groups compared with healthy lung cell. Treatment with the epidermal growth factor receptor tyrosine kinase inhibitor erlotinib increases the expression of the enzyme in a subset of NSCLC lines
medicine
-
loss of 15-hydroxyprostaglandin expression in 65% of lung cancers. Enzyme acts as a tumor suppressor in lung cancer and is a direct downstream effector of hepatocyte nuclear factor 3beta
medicine
-
thiazolidinediones rosiglitazone and pioglitazone upregulate expression of 15-hydroxyprostaglandin dehydrogenase, involving peroxisome proliferator-activated receptor gamma. Upregulation results in reduced production of prostaglandin E2 and finally inhibition of lung cancer growth
medicine
-
up-regulation of cyclooxygenase-2 expression by pro-inflammatory cytokines is accompanied by down-regluation of 15-hydroxyprostaglandin dehydrogenase expression. Over-expression of cyclooxygenase-2 but not -1 also attenuates 15-hydroxyprostaglandin dehydrogenase expression. Similarly, overexpression of 15-hydroxyprostaglandin dehydrogenase inhibits interleukin 1beta-induced cyclooxygenase-2 expression and results in apoptosis. The levels of 15-hydroxyprostaglandin dehydrogenase expression in transfected cells correlate positively with those of mesenchymal markers, and negatively with those of epithelial markers
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, S.C.; Levine, L.
Prostaglandin metabolism. II. Identification of two 15-hydroxyprostaglandin dehydrogenase types
J. Biol. Chem.
250
548-552
1975
Canis lupus familiaris, Gallus gallus, Homo sapiens, Platyrrhini, Sus scrofa
Tombach, B.; Kusseler, R.; Schlegel, W.
Purification of human placental prostaglandin 15-hydroxydehydrogenase
J. Chromatogr.
521
231-238
1990
Homo sapiens
Braithwaite, S.S.; Jabarak, J.
Studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Purification and partial characterization
J. Biol. Chem.
250
2315-2318
1975
Homo sapiens
Jabarak, J.; Braithwaite, S.S.
Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta
Arch. Biochem. Biophys.
177
245-254
1976
Homo sapiens
Jung, A.; Schlegel, W.; Jackisch, R.; Friedrich, E.J.; Wendel, A.; Ruckrich, M.F.
15-Hydroxyprostaglandin dehydrogenase from human placenta. 1. Isolation and characterization
Hoppe-Seyler's Z. Physiol. Chem.
356
787-798
1975
Homo sapiens
Ruckrich, M.F.; Wendel, A.; Schlegel, W.; Jackisch, R.; Jung, A.
15-Hydroxyprostaglandin dehydrogenase from human placenta, II. Steady state kinetics and influence of prostaglandin F2alpha analogues
Hoppe-Seyler's Z. Physiol. Chem.
356
799-809
1975
Homo sapiens
Krook, M.; Marekov, L.; Jrnvall, H.
Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family
Biochemistry
29
738-743
1990
Homo sapiens
Jabarak, J.
Isolation and properties of an NAD+-dependent 15-hydroxyprostaglandin dehydrogenase from human placenta
Methods Enzymol.
86
126-130
1982
Homo sapiens
Schlegel, W.; Demers, L.M.; Hildebrandt-Stark, H.E.; Behrman, H.R.; Greep, R.O.
Partial purification of human placental 15-hydroxy-prostaglandin dehydrogenase: kinetic properties
Prostaglandins
5
417-433
1974
Homo sapiens
Xun, C.Q.; Ensor, C.M.; Tai, H.H.
Regulation of synthesis and activity of NAD+-dependent 15-hydroxy-prostaglandin dehydrogenase (15-PGDH) by dexamethasone and phorbol ester in human erythroleukemia (HEL) cells
Biochem. Biophys. Res. Commun.
177
1258-1265
1991
Homo sapiens
Jarabak, J.
Polycyclic aromatic hydrocarbon quinones may be either substrates for or irreversible inhibitors of the human placental NAD-linked 15-hydroxyprostaglandin dehydrogenase
Arch. Biochem. Biophys.
292
239-243
1992
Homo sapiens
Mibe, M.; Nagai, K.; Oshige, T.; Mori, N.
Endogenous inhibitors of human placental prostaglandin dehydrogenase
Prostaglandins Leukot. Essent. Fatty Acids
46
241-245
1992
Homo sapiens
Chavan, A.J.; Ensoe, C.M.; Wu, P.; Haley, B.E.; Tai, H.H.
Photoaffinity labeling of human placental NAD+-linked 15-hydroxyprostaglandin dehydrogenase with [alpha-32]2N3NAD+
J. Biol. Chem.
268
16437-16442
1993
Homo sapiens
Hhl, W.; Stahl, B.; Mundkowski, R.; Hofmann, U.; Meese, C.O.; Kuhlmann, U.; Schlegel, W.
Mass determination of 15-hydroxyprostaglandin dehydrogenase from human placenta and kinetic studies with (5Z,8E,10E,12S)-12-hydroxy-5,8,10,-heptadecatrienoic acid as substrate
Eur. J. Biochem.
214
67-73
1993
Homo sapiens
Ensoe, C.M.; Tai, H.H.
Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase
Biochim. Biophys. Acta
1208
151-156
1994
Homo sapiens
Okita, R.T.; Okita, J.R.
Prostaglandin-metabolizing enzymes during pregnancy: characterization of NAD+-dependent prostaglandin dehydrogenase, carbonyl reductase, and cytochrome P450-dependent prostaglandin omega-hydroxylase
CRC Crit. Rev. Biochem.
31
101-126
1996
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Tong, M.; Tai, H.H.
Induction of NAD+-linked 15-hydroxyprostaglandin dehydrogenase expression by androgens in human prostate cancer cells
Biochem. Biophys. Res. Commun.
276
77-81
2000
Homo sapiens
Tai, H.H.; Ensor, C.M.; Zhou, H.; Yan, F.
Structure and function of human NAD+-linked 15-hydroxyprostaglandin dehydrogenase
Adv. Exp. Med. Biol.
507
245-250
2002
Homo sapiens
Cho, H.; Tai, H.H.
Thiazolidinediones as a novel class of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase inhibitors
Arch. Biochem. Biophys.
405
247-251
2002
Homo sapiens
Cho, H.; Oliveira, M.A.; Tai, H.H.
Critical residues for the coenzyme specificity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase
Arch. Biochem. Biophys.
419
139-146
2003
Homo sapiens
Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.
Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase
Arch. Biochem. Biophys.
433
447-453
2005
Homo sapiens
Tong, M.; Tai, H.H.
15-Hydroxyprostaglandin dehydrogenase can be induced by dexamethasone and other glucocorticoids at the therapeutic level in A549 human lung adenocarcinoma cells
Arch. Biochem. Biophys.
435
50-55
2005
Homo sapiens
Cho, H.; Tai, H.H.
Threonine 11 of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase may interact with NAD(+) during catalysis
Prostaglandins
66
505-509
2002
Homo sapiens
Cho, H.; Tai, H.H.
Inhibition of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH) by cyclooxygenase inhibitors and chemopreventive agents
Prostaglandins
67
461-465
2002
Homo sapiens
Otani, T.; Yamaguchi, K.; Scherl, E.; Du, B.; Tai, H.H.; Greifer, M.; Petrovic, L.; Daikoku, T.; Dey, S.K.; Subbaramaiah, K.; Dannenberg, A.J.
Levels of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase are reduced in inflammatory bowel disease: evidence for involvement of TNF-alpha
Am. J. Physiol.
290
G361-G368
2006
Homo sapiens
Tong, M.; Ding, Y.; Tai, H.H.
Histone deacetylase inhibitors and transforming growth factor-beta induce 15-hydroxyprostaglandin dehydrogenase expression in human lung adenocarcinoma cells
Biochem. Pharmacol.
72
701-709
2006
Homo sapiens
Hamza, A.; Cho, H.; Tai, H.H.; Zhan, C.G.
Understanding human 15-hydroxyprostaglandin dehydrogenase binding with NAD+ and PGE2 by homology modeling, docking and molecular dynamics simulation
Bioorg. Med. Chem.
13
4544-4551
2005
Homo sapiens
Mann, J.R.; Backlund, M.G.; Buchanan, F.G.; Daikoku, T.; Holla, V.R.; Rosenberg, D.W.; Dey, S.K.; DuBois, R.N.
Repression of prostaglandin dehydrogenase by epidermal growth factor and snail increases prostaglandin E2 and promotes cancer progression
Cancer Res.
66
6649-6656
2006
Homo sapiens
Wolf, I.; OKelly, J.; Rubinek, T.; Tong, M.; Nguyen, A.; Lin, B.T.; Tai, H.H.; Karlan, B.Y.; Koeffler, H.P.
15-hydroxyprostaglandin dehydrogenase is a tumor suppressor of human breast cancer
Cancer Res.
66
7818-7823
2006
Homo sapiens
Ding, Y.; Tong, M.; Liu, S.; Moscow, J.A.; Tai, H.H.
NAD+-linked 15-hydroxyprostaglandin dehydrogenase (15-PGDH) behaves as a tumor suppressor in lung cancer
Carcinogenesis
26
65-72
2005
Homo sapiens
Tong, M.; Ding, Y.; Tai, H.H.
Reciprocal regulation of cyclooxygenase-2 and 15-hydroxyprostaglandin dehydrogenase expression in A549 human lung adenocarcinoma cells
Carcinogenesis
27
2170-2179
2006
Homo sapiens
Tai, H.H.; Cho, H.; Tong, M.; Ding, Y.
NAD+-linked 15-hydroxyprostaglandin dehydrogenase: structure and biological functions
Curr. Pharm. Des.
12
955-962
2006
Homo sapiens
Backlund, M.G.; Mann, J.R.; Holla, V.R.; Buchanan, F.G.; Tai, H.H.; Musiek, E.S.; Milne, G.L.; Katkuri, S.; DuBois, R.N.
15-Hydroxyprostaglandin dehydrogenase is down-regulated in colorectal cancer
J. Biol. Chem.
280
3217-3223
2005
Homo sapiens, Mus musculus
Quidville, V.; Segond, N.; Lausson, S.; Frenkian, M.; Cohen, R.; Jullienne, A.
15-Hydroxyprostaglandin-dehydrogenase is involved in anti-proliferative effect of non-steroidal anti-inflammatory drugs COX-1 inhibitors on a human medullary thyroid carcinoma cell line
Prostaglandins Other Lipid Mediat.
81
14-30
2006
Homo sapiens
Yang, L.; Amann, J.M.; Kikuchi, T.; Porta, R.; Guix, M.; Gonzalez, A.; Park, K.H.; Billheimer, D.; Arteaga, C.L.; Tai, H.H.; DuBois, R.; Carbone, D.P.; Johnson, D.H.
Inhibition of epidermal growth factor receptor signaling elevates 15-hydroxyprostaglandin dehydrogenase in non-small-cell lung cancer
Cancer Res.
67
5587-5593
2007
Homo sapiens
Huang, G.; Eisenberg, R.; Yan, M.; Monti, S.; Lawrence, E.; Fu, P.; Walbroehl, J.; Loewenberg, E.; Golub, T.; Merchan, J.; Tenen, D.G.; Markowitz, S.D.; Halmos, B.
15-Hydroxyprostaglandin dehydrogenase is a target of hepatocyte nuclear factor 3beta and a tumor suppressor in lung cancer
Cancer Res.
68
5040-5048
2008
Homo sapiens
Michelet, J.F.; Colombe, L.; Gautier, B.; Gaillard, O.; Benech, F.; Pereira, R.; Boulle, C.; Dalko-Csiba, M.; Rozot, R.; Neuwels, M.; Bernard, B.A.
Expression of NAD(+) dependent 15-hydroxyprostaglandin dehydrogenase and protection of prostaglandins in human hair follicle
Exp. Dermatol.
17
821-828
2008
Homo sapiens (P15428), Homo sapiens
Hazra, S.; Batra, R.K.; Tai, H.H.; Sharma, S.; Cui, X.; Dubinett, S.M.
Pioglitazone and rosiglitazone decrease prostaglandin E2 in non-small-cell lung cancer cells by up-regulating 15-hydroxyprostaglandin dehydrogenase
Mol. Pharmacol.
71
1715-1720
2007
Homo sapiens
Uppal, S.; Diggle, C.P.; Carr, I.M.; Fishwick, C.W.; Ahmed, M.; Ibrahim, G.H.; Helliwell, P.S.; Latos-Biele?ska, A.; Phillips, S.E.; Markham, A.F.; Bennett, C.P.; Bonthron, D.T.
Mutations in 15-hydroxyprostaglandin dehydrogenase cause primary hypertrophic osteoarthropathy
Nat. Genet.
40
789-793
2008
Homo sapiens
Tai, H.H.; Tong, M.; Ding, Y.
15-hydroxyprostaglandin dehydrogenase (15-PGDH) and lung cancer
Prostaglandins Other Lipid Mediat.
83
203-208
2007
Homo sapiens
Rizek, R.M.; Watson, C.S.; Keating, S.; Tai, H.; Challis, J.R.; Bocking, A.D.
15-Hydroxyprostaglandin dehydrogenase protein expression in human fetal membranes with and without subclinical inflammation
Reprod. Sci.
14
260-269
2007
Homo sapiens
Miyaki, A.; Yang, P.; Tai, H.H.; Subbaramaiah, K.; Dannenberg, A.J.
Bile acids inhibit NAD+-dependent 15-hydroxyprostaglandin dehydrogenase transcription in colonocytes
Am. J. Physiol. Gastrointest. Liver Physiol.
297
G559-G566
2009
Homo sapiens
Chi, X.; Freeman, B.M.; Tong, M.; Zhao, Y.; Tai, H.H.
15-Hydroxyprostaglandin dehydrogenase (15-PGDH) is up-regulated by flurbiprofen and other non-steroidal anti-inflammatory drugs in human colon cancer HT29 cells
Arch. Biochem. Biophys.
487
139-145
2009
Homo sapiens
Hughes, D.; Otani, T.; Yang, P.; Newman, R.A.; Yantiss, R.K.; Altorki, N.K.; Port, J.L.; Yan, M.; Markowitz, S.D.; Mazumdar, M.; Tai, H.H.; Subbaramaiah, K.; Dannenberg, A.J.
NAD+-dependent 15-hydroxyprostaglandin dehydrogenase regulates levels of bioactive lipids in non-small cell lung cancer
Cancer Prev. Res. (Phila.)
1
241-249
2008
Homo sapiens
Backlund, M.G.; Mann, J.R.; Holla, V.R.; Shi, Q.; Daikoku, T.; Dey, S.K.; DuBois, R.N.
Repression of 15-hydroxyprostaglandin dehydrogenase involves histone deacetylase 2 and Snail in colorectal cancer
Cancer Res.
68
9331-9337
2008
Homo sapiens
Tariq, M.; Azeem, Z.; Ali, G.; Chishti, M.S.; Ahmad, W.
Mutation in the HPGD gene encoding NAD+ dependent 15-hydroxyprostaglandin dehydrogenase underlies isolated congenital nail clubbing (ICNC)
J. Med. Genet.
46
14-20
2009
Homo sapiens
Celis, J.E.; Gromov, P.; Cabezon, T.; Moreira, J.M.; Friis, E.; Jirstroem, K.; Llombart-Bosch, A.; Timmermans-Wielenga, V.; Rank, F.; Gromova, I.
15-prostaglandin dehydrogenase expression alone or in combination with ACSM1 defines a subgroup of the apocrine molecular subtype of breast carcinoma
Mol. Cell. Proteomics
7
1795-1809
2008
Homo sapiens (P15428)
Wei, C.; Zhu, P.; Shah, S.J.; Blair, I.A.
15-oxo-Eicosatetraenoic acid, a metabolite of macrophage 15-hydroxyprostaglandin dehydrogenase that inhibits endothelial cell proliferation
Mol. Pharmacol.
76
516-525
2009
Homo sapiens
Wu, Y.; Tai, H.H.; Cho, H.
Synthesis and SAR of thiazolidinedione derivatives as 15-PGDH inhibitors
Bioorg. Med. Chem.
18
1428-1433
2010
Homo sapiens
Liu, Z.; Wang, X.; Lu, Y.; Du, R.; Luo, G.; Wang, J.; Zhai, H.; Zhang, F.; Wen, Q.; Wu, K.; Fan, D.
15-Hydroxyprostaglandin dehydrogenase is a tumor suppressor of human gastric cancer
Cancer Biol. Ther.
10
780-787
2010
Homo sapiens
Chi, X.; Tai, H.H.
Interleukin-4 up-regulates 15-hydroxyprostaglandin dehydrogenase (15-PGDH) in human lung cancer cells
Exp. Cell Res.
316
2251-2259
2010
Homo sapiens
Wu, Y.; Karna, S.; Choi, C.H.; Tong, M.; Tai, H.H.; Na, D.H.; Jang, C.H.; Cho, H.
Synthesis and biological evaluation of novel thiazolidinedione analogues as 15-hydroxyprostaglandin dehydrogenase inhibitors
J. Med. Chem.
54
5260-5264
2011
Homo sapiens
Thill, M.; Fischer, D.; Kelling, K.; Hoellen, F.; Dittmer, C.; Hornemann, A.; Salehin, D.; Diedrich, K.; Friedrich, M.; Becker, S.
Expression of vitamin D receptor (VDR), cyclooxygenase-2 (COX-2) and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) in benign and malignant ovarian tissue and 25-hydroxycholecalciferol (25(OH2)D3) and prostaglandin E2 (PGE2) serum level in ovarian cancer
J. Steroid Biochem. Mol. Biol.
121
387-390
2010
Homo sapiens
Lu, D.; Han, C.; Wu, T.
15-PGDH inhibits hepatocellular carcinoma growth through 15-keto-PGE2/PPARgamma-mediated activation of p21(WAF1/Cip1.)
Oncogene
33
1101-1112
2013
Homo sapiens
Niesen, F.; Schultz, L.; Jadhav, A.; Bhatia, C.; Guo, K.; Maloney, D.; Pilka, E.; Wang, M.; Oppermann, U.; Heightman, T.; Simeonov, A.
High-affinity inhibitors of human NAD+-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships
PLoS ONE
5
e13719
2010
Homo sapiens
Duveau, D.Y.; Yasgar, A.; Wang, Y.; Hu, X.; Kouznetsova, J.; Brimacombe, K.R.; Jadhav, A.; Simeonov, A.; Thomas, C.J.; Maloney, D.J.
Structure-activity relationship studies and biological characterization of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase inhibitors
Bioorg. Med. Chem. Lett.
24
630-635
2014
Homo sapiens (P15428), Homo sapiens
Choi, D.; Piao, Y.L.; Wu, Y.; Cho, H.
Control of the intracellular levels of prostaglandin E2 through inhibition of the 15-hydroxyprostaglandin dehydrogenase for wound healing
Bioorg. Med. Chem.
21
4477-4484
2013
Homo sapiens (P15428)
Castro-Sanchez, L.; Agra, N.; Llorente Izquierdo, C.; Motino, O.; Casado, M.; Bosca, L.; Martin-Sanz, P.
Regulation of 15-hydroxyprostaglandin dehydrogenase expression in hepatocellular carcinoma
Int. J. Biochem. Cell Biol.
45
2501-2511
2013
Homo sapiens (P15428), Homo sapiens
Lu, D.; Han, C.; Wu, T.
15-hydroxyprostaglandin dehydrogenase-derived 15-keto-prostaglandin E2 inhibits cholangiocarcinoma cell growth through interaction with peroxisome proliferator-activated receptor-gamma, SMAD2/3, and TAP63 proteins
J. Biol. Chem.
288
19484-19502
2013
Homo sapiens (P15428), Homo sapiens
Kim, H.J.; Lee, S.; Lee, H.Y.; Won, H.; Chang, S.H.; Nah, S.S.
15-hydroxyprostaglandin dehydrogenase is upregulated by hydroxychloroquine in rheumatoid arthritis fibroblast-like synoviocytes
Mol. Med. Rep.
12
4141-4148
2015
Homo sapiens (P15428), Homo sapiens
Kim, H.; Lee, H.; Lim, K.; Surh, Y.; Na, H.
15-Deoxy-DELTA12,14-prostaglandin J2 induces expression of 15-hydroxyprostaglandin dehydrogenase through Elk-1 activation in human breast cancer MDA-MB-231 cells
Mutat. Res.
768
6-15
2014
Homo sapiens (P15428), Homo sapiens
Sola-Villa, D.; Dilme, J.F.; Rodriguez, C.; Soto, B.; Vila, L.; Escudero, J.R.; Martinez-Gonzalez, J.; Camacho, M.
Expression and cellular localization of 15-hydroxy-prostaglandin-dehydrogenase in abdominal aortic aneurysm
PLoS ONE
10
e0136201
2015
Homo sapiens (P15428), Homo sapiens
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