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Information on EC 1.1.1.188 - prostaglandin-F synthase
for references in articles please use BRENDA:EC1.1.1.188
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.188 prostaglandin-F synthase
IUBMB Comments
Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2. Also catalyses the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone.
The enzyme appears in viruses and cellular organisms
- 1.1.1.188
- aldose
- endometrium
-
estrous
- mpges-1
-
reductase-like
- akr1b3
- synthase-2
-
rho-crystallins
-
ptgfr
-
luteotropic
-
9-ketoreductase
-
alpha-hsds
-
bitch
- medicine
- chlordecone
- synthesis
- drug development
- pharmacology
- molecular biology
Reaction Schemes
showSynonyms
pgfs, akr1b7, prostaglandin f synthase, pgf synthase, vas deferens protein, prostaglandin f synthetase, prostamide/pgf synthase, p100/11e, akr1cl, pgd2 11-ketoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AKR1B1
AKR1C3
aldo-keto reductase
LBRM2904_31.2170
m-PGFS
NADPH-dependent prostaglandin D2 11-keto reductase
-
-
-
-
PGD 11-ketoreductase
PGD2 11-ketoreductase
PGF
PGF synthase
PGF2alpha synthase
PGF2S
PGFS
PGFSI
-
-
-
-
PGFSII
-
-
-
-
PGH 9-,11-endoperoxide reductase
PGH2 9-,11-endoperoxide reductase
prostaglandin 11-keto reductase
-
-
-
-
prostaglandin 11-ketoreductase
-
-
-
-
prostaglandin D2-ketoreductase
-
-
-
-
prostaglandin F synthase
prostaglandin F synthetase
-
-
-
-
prostaglandin F2alpha synthase
prostaglandin-D2 11-reductase
-
-
-
-
prostamide/PGF synthase
prostamide/prostaglandin F synthase
reductase, 15-hydroxy-11-oxoprostaglandin
-
-
-
-
synthetase, prostaglandin F2alpha
-
-
-
-
Tc00.1047053508461.80
Tc00.1047053511287.49
TCDM_00059
TrcrA.00019.a.B1
additional information
PGD2 11-ketoreductase
-
-
-
-
PGF synthase
-
-
-
-
PGF2alpha synthase
-
-
-
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prostaglandin F synthase
-
-
-
-
additional information
-
enzyme belongs to the AKR aldo-keto-reductase superfamily
additional information
-
enzyme belongs to the AKR aldo-keto-reductase superfamily
additional information
enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity, i.e. 3alpha-HSD
additional information
enzyme belongs to the aldo-keto reductase AKR family, enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity, i.e. 3alpha-HSD
additional information
-
enzyme belongs to the AKR aldo-keto-reductase superfamily
additional information
-
enzyme belongs to the AKR aldo-keto-reductase superfamily
additional information
-
enzyme belongs to the AKR aldo-keto reductase superfamily
additional information
-
enzyme belongs to the AKR aldo-keto reductase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
-
-
-
-
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
substrate binding and catalytic mechanism, catalytic site residues are Y55 and H117, enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity, i.e. 3alpha-HSD
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
active site structure, enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity, i.e. 3alpha-HSD
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Tyr55 is critical for the reaction, the reactions with different substrates might follow different mechanisms
-
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
catalytic mechanisms, the catalytic sites for PGD2 11-ketoreductase and PGH2 9,11-endoperoxide reductase activities are located differently in the active site cavity, residue Y55 is important for the PGD2 11-ketoreductase activity, but not for the PGH2 9,11-endoperoxide reductase activity, involved structural features, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
C20 prostanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate:NADP+ 11-oxidoreductase
Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2. Also catalyses the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone.
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CAS REGISTRY NUMBER
COMMENTARY
55976-95-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
(5Z,13E)-(15S)-9alpha,11beta,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11beta,15-trihydroxyprosta-5,13-dienoate + NADP+
4-nitrobenzaldehyde + NADPH
4-nitrobenzalcohol + NADP+
-
Substrates: high activity
Products: -
Products: -
?
5beta-androstane-3,17-dione + NADPH
5beta-androstan-3alpha-ol-17-one + NADP+
-
Substrates: -
Products: -
Products: -
r
9alpha,11beta-prostaglandin F2 + NADPH + H+
prostaglandin D2 + NADP+
Substrates: -
Products: -
Products: -
r
prostaglandin D2 + NADP+
9alpha,11beta-prostaglandin F2 + NADPH
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADP+
9alpha,11beta-prostaglandin F2 + NADPH + H+
Substrates: -
Products: -
Products: -
r
prostaglandin D2 + NADPH + H+
9-alpha,11-beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
r
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2alphabeta + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin D2 ethanolamide + NADPH
prostaglandin 9alpha,11beta-F2 ethanolamide + NADP+
Substrates: i.e. prostamide D2
Products: i.e. 91lpha,11beta-prostamide F2
Products: i.e. 91lpha,11beta-prostamide F2
?
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
prostaglandin H2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostamide D2 + NADPH + H+
9alpha,11beta-prostamide F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostamide H2 + NADPH + H+
prostamide F2alpha + NADP+
-
Substrates: about 70% of prostamide H2 is converted to prostamide F2alpha after 2 min at 37°C
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
ir
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: transformation of endogenous prostaglandin D2 to prostaglandin F2alpha
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: prostaglandin F2alpha exhibits contraction of smooth muscles in the uterus, brochus trachea, luteolysis, the initiation of partutition and pain transmission
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11beta,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11beta,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH
4-nitrobenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
(4-nitrophenyl)methanol + NADP+
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NADPH + H+
(4-nitrophenyl)methanol + NADP+
-
Substrates: -
Products: -
Products: -
?
9,10-phenanthrenequinone + NADPH
?
-
Substrates: -
Products: -
Products: -
?
cyclohexanone + NADPH
cyclohexanol + NADP+
-
Substrates: high activity
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11alpha-prostaglandin F2alpha + NADP+
-
Substrates: reaction via formation of the endoperoxide ethanolamide intermediate prostaglandin H2
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11alpha-prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: amino acid residues Arg27, Arg91, His170, Arg223, and Asn306 are involved in substrate binding
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: i.e. 11-epi PGF2alpha
Products: i.e. 11-epi PGF2alpha
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: i.e. 11-epi PGF2alpha
Products: i.e. 11-epi PGF2alpha
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: i.e. 11-epi PGF2alpha
Products: i.e. 11-epi PGF2alpha
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: i.e. 11-epi PGF2alpha
Products: i.e. 11-epi PGF2alpha
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
Substrates: aldo-keto reductase has prostaglandin F2alpha synthase activity. AKR1B1 is a more efficient prostaglandin F2alpha synthase than AKR1C3
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: aldo-keto reductases AKR1B3 and AKR1B7 have prostaglandin F2alpha synthase activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11alpha-prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11alpha-prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: enzyme also shows PGH2 9-,11-endoperoxide reductase activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: His170 is involved in binding, and Asn306 is critical for catalytic activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: enzyme also shows PGH2 9-,11-endoperoxide reductase activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: enzyme also shows PGH2 9-,11-endoperoxide reductase activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: enzyme also shows PGH2 9-,11-endoperoxide reductase activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: no stereochemic determination/identification of the product
Products: no stereochemic determination/identification of the product
?
additional information
?
-
-
Substrates: two different active sites, one for the endoperoxide group of prostaglandin H2 and the other one for the keto group of prostaglandin D2 and other carbonyl compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: two different active sites, one for the endoperoxide group of prostaglandin H2 and the other one for the keto group of prostaglandin D2 and other carbonyl compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: two different active sites, one for the endoperoxide group of prostaglandin H2 and the other one for the keto group of prostaglandin D2 and other carbonyl compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: two different active sites, one for the endoperoxide group of prostaglandin H2 and the other one for the keto group of prostaglandin D2 and other carbonyl compounds
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is important for the production of lyteolytic prostaglandin F2alpha in the endometrium of cows, regulatory mechanisms, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the liver-type isozyme possesses two catalytic centres and a broad substrate specificity, D-xylose is a poor substrate, no activity with prostaglandin A1, prostaglandin B2, prostaglandin E2, 4-carboxybenzaldehyde, testosterone, 2,6-dichloroindophenol, D-glucose, D-glucuronic acid, and potassium ferricyanide, overview, the enzyme also exhibits aldose reductase, EC 1.1.1.21, and alcohol dehydrogenase, EC 1.1.1.1, activities, respectively
Products: -
Products: -
?
additional information
?
-
Substrates: PGFS activity of the recombinant proteins is evaluated using an assay based on in situ generation of the precursor of prostaglandin PGH2 biosynthesis. PGF2alpha is measured by ELISA. Comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PGFS activity of the recombinant proteins is evaluated using an assay based on in situ generation of the precursor of prostaglandin PGH2 biosynthesis. PGF2alpha is measured by ELISA. Comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no activity towards prostaglandin E2 synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity towards prostaglandin E2 synthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic enzyme synergistically interacts with cyclooxygenase 1 and 2, coupling, isozyme PGFS-I interacts predominantly with cyclooxygenase 2, i.e. COX-2
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate and product detection by liquid chromatographic-electrospray ionization-mass spectrometry
Products: -
Products: -
?
additional information
?
-
Substrates: substrate and product detection by liquid chromatographic-electrospray ionization-mass spectrometry
Products: -
Products: -
?
additional information
?
-
Substrates: Y55 and H117 are involved in catalysis, enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: Y55 and H117 are involved in catalysis, enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity
Products: -
Products: -
?
additional information
?
-
Substrates: acive site structure, enzyme also shows 3alpha-hydroxysteroid dehydrogenase type II activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has dual activity as PGD2 11-ketoreductase and PGH2 9,11-endoperoxide reductase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has dual activity as PGD2 11-ketoreductase and PGH2 9,11-endoperoxide reductase
Products: -
Products: -
?
additional information
?
-
-
Substrates: PGFS does not catalyze the reduction of prostaglandin E2
Products: -
Products: -
?
additional information
?
-
Substrates: PGFS does not catalyze the reduction of prostaglandin E2
Products: -
Products: -
?
additional information
?
-
Substrates: in the absence of NADPH or NADP+, enzyme catalyzes the isomerization of prostaglandin H2 to prostaglandin D2 with a Km value of 0.023 mM. This activity of AKR1B1 increases with increasing pH, with an optimum of pH 8.5. Residue His110 acts as a base in concert with Asp43 and Lys77 and as an acid to generate PGD2 and PGF2a in the absence of NADPH or NADP+ and in the presence of NADPH, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the absence of NADPH or NADP+, enzyme catalyzes the isomerization of prostaglandin H2 to prostaglandin D2 with a Km value of 0.023 mM. This activity of AKR1B1 increases with increasing pH, with an optimum of pH 8.5. Residue His110 acts as a base in concert with Asp43 and Lys77 and as an acid to generate PGD2 and PGF2a in the absence of NADPH or NADP+ and in the presence of NADPH, respectively
Products: -
Products: -
?
additional information
?
-
Substrates: AKR1C3 is overexpressed in keloids and mediates the conversion of PGD2 to 9alpha,11beta-PGF2 in keloid and normal fibroblasts
Products: -
Products: -
?
additional information
?
-
Substrates: PGFS activity of the recombinant proteins is evaluated using an assay based on in situ generation of the precursor of prostaglandin PGH2 biosynthesis. PGF2alpha is measured by ELISA. Comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PGFS activity of the recombinant proteins is evaluated using an assay based on in situ generation of the precursor of prostaglandin PGH2 biosynthesis. PGF2alpha is measured by ELISA. Comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: coupling ability between cyclooxygenase COX-2 and the prostanoid synthases performing the last stepes in the biosynthesis of prostaglandins PGE2, PGD2, PGF2alpha, and PGI2, regulation, overview, the 20alpha-hydroxysteroid dehydrogenase also shows prostaglandin F synthase activity in the endometrium during luteolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: prostaglandin F synthase and prostaglandin F receptor are involved in the control of testosterone release from Leydig cells and in spermatogenesis via the local pathway and the hypothalamo-hypophysial-testis-pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with prostaglandin D2 and prostaglandin E2
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the absence of NADPH or NADP+, enzyme catalyzes the isomerization of prostaglandin H2 to prostaglandin D2 with a Km value of 0.018 mM. This activity activity of AKR1B1 increases with increasing pH, with an optimum of pH 8.5. Residue His110 acts as a base in concert with Asp43 and Lys77 and as an acid to generate PGD2 and PGF2a in the absence of NADPH or NADP+ and in the presence of NADPH, respectively
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows no prostaglandin D2 11-ketoreductase activity, and no glutathione S-transferase activity, although it is similar to the glutathione S-transferase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme interacts with cyclooxygenase 1 and 2, isozyme PGFS-I interacts predominantly with cyclooxygenase 2, i.e. COX-2
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme does not reduce prostaglandins D2 and E2
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme does not reduce prostaglandins D2 and E2
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
(5Z,13E)-(15S)-9alpha,11beta,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
prostaglandin D2 + NADP+
9alpha,11beta-prostaglandin F2 + NADPH
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9-alpha,11-beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11alpha-prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
9alpha,11beta-prostaglandin F2alphabeta + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11alpha-prostaglandin F2alpha + NADP+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
9alpha,11beta-prostaglandin F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: transformation of endogenous prostaglandin D2 to prostaglandin F2alpha
Products: -
Products: -
?
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate + NADP+
-
Substrates: prostaglandin F2alpha exhibits contraction of smooth muscles in the uterus, brochus trachea, luteolysis, the initiation of partutition and pain transmission
Products: -
Products: -
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
Products: product is involved in bronchial, vascular, and arterial smooth muscle contraction, product inhibits platelet aggregation and activates urinary excretion
?
prostaglandin D2 + NADPH + H+
prostaglandin 9alpha,11beta-F2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADP+
prostaglandin F2alpha + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin D2 + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: enzyme also shows PGH2 9-,11-endoperoxide reductase activity
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
prostaglandin H2 + NADPH + H+
prostaglandin F2alpha + NADP+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is important for the production of lyteolytic prostaglandin F2alpha in the endometrium of cows, regulatory mechanisms, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cytosolic enzyme synergistically interacts with cyclooxygenase 1 and 2, coupling, isozyme PGFS-I interacts predominantly with cyclooxygenase 2, i.e. COX-2
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has dual activity as PGD2 11-ketoreductase and PGH2 9,11-endoperoxide reductase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has dual activity as PGD2 11-ketoreductase and PGH2 9,11-endoperoxide reductase
Products: -
Products: -
?
additional information
?
-
Substrates: AKR1C3 is overexpressed in keloids and mediates the conversion of PGD2 to 9alpha,11beta-PGF2 in keloid and normal fibroblasts
Products: -
Products: -
?
additional information
?
-
-
Substrates: coupling ability between cyclooxygenase COX-2 and the prostanoid synthases performing the last stepes in the biosynthesis of prostaglandins PGE2, PGD2, PGF2alpha, and PGI2, regulation, overview, the 20alpha-hydroxysteroid dehydrogenase also shows prostaglandin F synthase activity in the endometrium during luteolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: prostaglandin F synthase and prostaglandin F receptor are involved in the control of testosterone release from Leydig cells and in spermatogenesis via the local pathway and the hypothalamo-hypophysial-testis-pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme interacts with cyclooxygenase 1 and 2, isozyme PGFS-I interacts predominantly with cyclooxygenase 2, i.e. COX-2
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
enzyme PGF is specific for NADP+. Structures of PGF with and without NADP+ and structural differences between the bound and the unbound state of the enzyme with regard to its cofactor
NADP+
enzyme PGF is specific for NADP+. Structures of PGF with and without NADP+ and structural differences between the bound and the unbound state of the enzyme with regard to its cofactor
NADPH
-
-
NADPH
binding structure at the active site, catalytic structure and mechanism involving the cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z)-7-[(1R,2R,3R,5S)-3,5-dihydroxy-2-[(1E,3S)-3-hydroxy-5-phenylpent-1-en-1-yl]cyclopentyl]-N-ethylhept-5-enamide
bimatoprost
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
ONO1370
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
ONO1349
(5Z)-7-[(1S,4S,5S,6R)-2-methyl-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
ONO1373
(Z)-7-[(1R,4S,5S,6R)-((E)-6-oct-1-enyl)-2-aza-bicyclo[2.2.1]hept-5-yl]-hept-5-enoic acid
inhibition of PGH2 9,11-endoperoxide reductase activity, slight inhibition of prostamide D2 11-ketoreductase and PGD2 11-ketoreductase activity
(Z)-7-[(1R,4S,5S,6R)-2-methyl-6-((E)-oct-1-enyl)-2-aza-bicyclo[2.2.1]hept-5-yl]-hept-5-enoic acid
inhibition of PGH2 9,11-endoperoxide reductase activity, slight inhibition of prostamide D2 11-ketoreductase and PGD2 11-ketoreductase activity, competitive, binds to the active site
(Z)-7-[(1R,4S,5S,6R)-6-((E)-(S)-3-hydroxy-oct-1-enyl)-2-aza-bicyclo[2.2.1]hept-5-yl]-hept-5-enoic acid
inhibition of PGH2 9,11-endoperoxide reductase activity, slight inhibition of prostamide D2 11-ketoreductase and PGD2 11-ketoreductase activity
15-deoxy-DELTA12,14-prostaglandin J2
15d-PGJ2, the enzyme inhibitor attenuates proliferation, inhibits collagen gel contraction and induces activation of the apoptotic marker, caspase-3, in CRL1762 keloid fibroblasts
2-(1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl)-N-((trifluoromethyl)sulfonyl)acetamide
257fold selectivity for isoform AKR1C3 over isoform AKR1C2
3-(1-(4-chlorobenzoyl)-3-ethyl-5-methoxy-1H-indol-2-yl)-propanoic acid
540fold selectivity for isoform AKR1C3 over isoform AKR1C2
3-(1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl)-propanoic acid
257fold selectivity for isoform AKR1C3 over isoform AKR1C2
acetate
occupies the oxyanion hole of the active site, 2 complex structures
CuSO4
-
at 5 mM 93-96% inhibition, depending on the substrate; the liver-type isozyme is 2fold less sensitive than the lung-type isozyme
HgCl2
-
IC50 = 0.3 mM, the liver-type isozyme is 2fold less sensitive than the lung-type isozyme; at 1 mM 94-100% inhibition, depending on the substrate
indomethacin methyl ester
specific inhibition of isoform AKR1C3 versus AKR1C1 and AKR1C3
ponalrestat
specific inhibitor developed to block AKR1B1 activity. Application reduces prostaglandin F2alpha production in response to interleukin IL-1beta in both cultured endometrial cells and endometrial explants
9,10-phenanthrenequinone
-
competitive inhibition of PGD2 but not of PGH2 reduction; competitive inhibitor of the reduction of prostaglandin D2, not of prostaglandin H2
9,10-phenanthrenequinone
the prostaglandin D2 11-ketoreductase activity of PGFS is competitively inhibited by 9,10-phenanthrenequinone
9,10-phenanthrenequinone
-
competitive inhibition of the PGD2 11-ketoreductase activity, not of PGH2 9-,11-endoperoxide reductase activity
bimatoprost
ethyl amide analogue of 17-phenyl-trinor PGF2alpha, inhibits all enzyme activities noncompetitively at low concentration, binds to a site different from the active site; potent inhibitor
bimatoprost
inhibits the prostaglandin D2 11-ketoreductase activity as well as the prostaglandin H2 9,11-endoperoxide reductase activity of PGFS
Flufenamic acid
nonsteroidal anti-inflammatory drug, binds to both the active site and the beta-hairpin loop at the opposite end of the central beta-barrel, complex structure
indomethacin
nonsteroidal anti-inflammatory drug, 1 molecule binds to the active site, complex structure
indomethacin
specific inhibition of isoform AKR1C3 versus AKR1C1 and AKR1C3
indomethacin
inhibits AKR1C3, but does not inhibit highly related AKR1C1 or AKR1C2
indomethacin
-
at 0.005 mg/ml in vivo inhibition of prostaglandin formation
interferon tau
-
recombinant ovine interferon tau down-regulates mRNA gene expression of the prostaglandin F synthase at a concentration of 0.000001 mg/ml
-
interferon tau
-
recombinant bovine interferon tau down-regulates mRNA gene expression of the prostaglandin F synthase after stimulation with oxytocin
-
N-(4-chlorobenzoyl)-melatonin
specific inhibition of isoform AKR1C3 versus AKR1C1 and AKR1C3, not inhibitory to cyclooxygenases. Uncompetitive versus 9,10-phenynthrenequinone, competitive versus DELTA4-andostene-3,17-dione
N-(4-chlorobenzoyl)-melatonin
exhibits uncompetitive inhibition patterns for the reduction of 9,10-phenanthrenequinone but competitive inhibition patterns for the reduction of androstenedione by AKR1C3
sorbinil
-
significantly inhibits the prostaglandin F2alpha synthase activity of AKR1B3 in a non-competitive fashion, whereas AKR1B7 is not sensitive to the inhibitor
Tolrestat
inhibition of all 3 enzyme activities, most effective inhibiting the PGD2 11-ketoreductase activity
Tolrestat
-
significantly inhibits the prostaglandin F2alpha synthase activity of AKR1B3 in a non-competitive fashion, whereas AKR1B7 is not sensitive to the inhibitor
additional information
-
AKR1C3 is potently inhibited by non-steroidal anti-inflammatory drugs, which are protective against breast cancer
-
additional information
AKR1C3 is potently inhibited by non-steroidal anti-inflammatory drugs, which are protective against breast cancer
-
additional information
heat treatment of AKR1B1 at 100°C for 5 min completely inactivates the prostaglandin F2alpha synthase activity, which is strictly dependent on the presence of NADPH
-
additional information
heat treatment of AKR1B1 at 100°C for 5 min completely inactivates the prostaglandin F2alpha synthase activity, which is strictly dependent on the presence of NADPH
-
additional information
-
heat treatment of AKR1B1 at 100°C for 5 min completely inactivates the prostaglandin F2alpha synthase activity, which is strictly dependent on the presence of NADPH
-
additional information
inhibitors such as alrestatin, ponalrestat, and EBPC exhibit distinct and characteristic inhibition of prostaglandin F2alpha production in different cell models
-
additional information
-
inhibitors such as alrestatin, ponalrestat, and EBPC exhibit distinct and characteristic inhibition of prostaglandin F2alpha production in different cell models
-
additional information
combination of indomethacin with tert-butyl hydroperoxide significantly inhibits the growth of radiation-resistant AKR1C3-over cells
-
additional information
-
heat treatment of AKR1B3 and AKR1B7 at 100°C for 5 min completely inactivates the prostaglandin F2alpha synthase activities, which is strictly dependent on the presence of NADPH
-
additional information
less than 10% inhibition at 0.05 mM: phenolphthalein, hexestrol, medroxyprogesterone acetate, progesterone, testosterone, cortisol, dehydroepiandrosterone
-
additional information
-
less than 10% inhibition at 0.05 mM: phenolphthalein, hexestrol, medroxyprogesterone acetate, progesterone, testosterone, cortisol, dehydroepiandrosterone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ammonium sulfate
activity of the purified recombinant enzyme is stimulated about 4fold by 1.5 M
chloride
-
stimulates the reduction of prostaglandin D2 and carbonyl compounds, but had no effect on prostaglandin H2 reduction
Gonadotropin
-
prostaglandin F synthase mRNA and protein levels are low before treatment with gonadotropin and peak 24-36 h after gonadotropin administration to granulosa cells
-
imidazole
-
in vitro stimulation of prostaglandin F2alpha and D2 production
lipopolysaccharides
-
strong induction of the membrane-bound lung isozyme, slight induction in spleen, kidney, testis, and pancreas, overview
-
Oxytoxin
-
stimulates enzyme expression and PGD2 11-ketoreductase activity in myometrial tissue of cyclic, but not significantly of early-pregnant, sows, at 0.0001 mM
additional information
-
PGF synthase I activity in HEK 293 cells is unaffected by interleukin-1beta
-
additional information
-
oxytoxin does not stimulate PGH2 9,11-endoperoxide reductase expression and activity in myometrial tissue of cyclic and early-pregnant sows
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Callosities
Whole-cell response characteristics of ciliated and microvillous olfactory receptor neurons to amino acids, pheromone candidates and urine in rainbow trout.
Carcinogenesis
Adrenal tumorigenesis targeted by the corticotropin-regulated promoter of the aldo-keto reductase AKR1B7 gene in transgenic mice.
Carcinogenesis
Localization of cyclooxygenases-1 and -2, and prostaglandin F synthase in human kidney and renal cell carcinoma.
Carcinoma
Localization of cyclooxygenases-1 and -2, and prostaglandin F synthase in human kidney and renal cell carcinoma.
Carcinoma
Preferential expression of hPGFS in primary SCCHN and tumour cell lines derived from respiratory and digestive organs.
Carcinoma, Renal Cell
Localization of cyclooxygenases-1 and -2, and prostaglandin F synthase in human kidney and renal cell carcinoma.
Carcinoma, Squamous Cell
Preferential expression of hPGFS in primary SCCHN and tumour cell lines derived from respiratory and digestive organs.
Cardiomegaly
Identification of a novel aldose reductase-like gene upregulated in the failing heart of cardiomyopathic hamster.
Dental Caries
CovR and VicRKX regulate transcription of the collagen binding protein Cnm of Streptococcus mutans.
Diabetes Complications
A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase.
Diabetes Complications
The Human Aldose Reductase AKR1B1 Qualifies as the Primary Prostaglandin F Synthase in the Endometrium.
Diabetes Mellitus
Aldo-keto reductase 1B7 is a target gene of FXR and regulates lipid and glucose homeostasis.
Dystocia
Do uterine PTGS2, PGFS, and PTGFR expression play a role in canine uterine inertia?
Endocarditis
CovR and VicRKX regulate transcription of the collagen binding protein Cnm of Streptococcus mutans.
Fatty Liver
Aldo-keto reductase 1B7 is a target gene of FXR and regulates lipid and glucose homeostasis.
Hematologic Neoplasms
Primary graft failure after myeloablative allogeneic hematopoietic cell transplantation for hematologic malignancies.
Herpes Zoster
Adrenocorticotropin-dependent changes in SF-1/DAX-1 ratio influence steroidogenic genes expression in a novel model of glucocorticoid-producing adrenocortical cell lines derived from targeted tumorigenesis.
Hypertriglyceridemia
Role of the pregnane X receptor in binge ethanol-induced steatosis and hepatotoxicity.
Infections
CovR and VicRKX regulate transcription of the collagen binding protein Cnm of Streptococcus mutans.
Liver Diseases
Aldo-keto reductase 1B7 is a target gene of FXR and regulates lipid and glucose homeostasis.
Lung Diseases
Clinical evaluation of main urinary metabolite of PGFs in chronic lung diseases.
Neoplasms
ACTH and PRL sensitivity of highly differentiated cell lines obtained by adrenocortical targeted oncogenesis.
Neoplasms
Adrenocorticotropin-dependent changes in SF-1/DAX-1 ratio influence steroidogenic genes expression in a novel model of glucocorticoid-producing adrenocortical cell lines derived from targeted tumorigenesis.
Neoplasms
Intramammary lipopolysaccharide infusion alters gene expression but does not induce lysis of the bovine corpus luteum.
Neoplasms
Lipopolysaccharides, cytokines, and nitric oxide affect secretion of prostaglandins and leukotrienes by bovine mammary gland epithelial cells.
Neoplasms
Selective inhibition of human type-5 17?-hydroxysteroid dehydrogenase (AKR1C3) by baccharin, a component of Brazilian propolis.
Obesity
Depressed Levels of Prostaglandin F2? in Mice Lacking Akr1b7 Increase Basal Adiposity and Predispose to Diet-Induced Obesity.
Obstetric Labor, Premature
Expression of the prostaglandin F synthase AKR1B1 and the prostaglandin transporter SLCO2A1 in human fetal membranes in relation to spontaneous term and preterm labor.
Obstetric Labor, Premature
Increase in prostaglandin H synthase 2, but not prostaglandin F2alpha synthase mRNA in intrauterine tissues during betamethasone-induced premature labor and spontaneous term labor in sheep.
prostaglandin-f synthase deficiency
ER stress-induced adipocytes secrete-aldo-keto reductase 1B7-containing exosomes that cause nonalcoholic steatohepatitis in mice.
Pyometra
Identifying diagnostic endocrine markers and changes in endometrial gene expressions during pyometra in cats.
Pyometra
Prostaglandin synthesis genes are differentially transcripted in normal and pyometra endometria of bitches.
Venous Thromboembolism
Long-term follow-up of prophylactic greenfield filters in multisystem trauma patients.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics of 3alpha-hydroxysteroid dehydrogenase type II activity
-
0.01
prostaglandin PGH2
-
recombinant liver-type isozyme, mutants R91Q, R223L and N306Y, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
9,10-phenanthrenequinone
-
37°C, liver-type isozyme, versus prostaglandin D2
additional information
additional information
Ki values for the nonsteroidal anti-inflammatory drug inhibitors with 3alpha-androstanediol as a substrate
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005 - 0.06
(5Z)-7-[(1R,2R,3R,5S)-3,5-dihydroxy-2-[(1E,3S)-3-hydroxy-5-phenylpent-1-en-1-yl]cyclopentyl]-N-ethylhept-5-enamide
0.3 - 1
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
0.13 - 1
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
0.06 - 1
(5Z)-7-[(1S,4S,5S,6R)-2-methyl-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
0.00021
2-(1-(4-chlorobenzoyl)-5-methoxy-1H-indol-3-yl )-N-((trifluoromethyl)sulfonyl)acetamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00009
3-(1-(4-chlorobenzoyl)-3-ethyl-5-methoxy-1H-indol-2-yl)-propanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00022
3-(1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl)-propanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.3
HgCl2
Bos taurus
-
IC50 = 0.3 mM, the liver-type isozyme is 2fold less sensitive than the lung-type isozyme
0.005
(5Z)-7-[(1R,2R,3R,5S)-3,5-dihydroxy-2-[(1E,3S)-3-hydroxy-5-phenylpent-1-en-1-yl]cyclopentyl]-N-ethylhept-5-enamide
Homo sapiens
recombinant enzyme, using prostaglandin D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.006
(5Z)-7-[(1R,2R,3R,5S)-3,5-dihydroxy-2-[(1E,3S)-3-hydroxy-5-phenylpent-1-en-1-yl]cyclopentyl]-N-ethylhept-5-enamide
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.06
(5Z)-7-[(1R,2R,3R,5S)-3,5-dihydroxy-2-[(1E,3S)-3-hydroxy-5-phenylpent-1-en-1-yl]cyclopentyl]-N-ethylhept-5-enamide
Homo sapiens
recombinant enzyme, using prostamide D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.3
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
IC50 about 1 mM, recombinant enzyme, using prostaglandin D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
IC50 about 1 mM, recombinant enzyme, using prostamide D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.13
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
IC50 about 1 mM, recombinant enzyme, using prostaglandin D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
(5Z)-7-[(1R,4S,5S,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
IC50 about 1 mM, recombinant enzyme, using prostamide D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.06
(5Z)-7-[(1S,4S,5S,6R)-2-methyl-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
(5Z)-7-[(1S,4S,5S,6R)-2-methyl-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
IC50 about 1 mM, recombinant enzyme, using prostaglandin D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
(5Z)-7-[(1S,4S,5S,6R)-2-methyl-6-[(1E)-oct-1-en-1-yl]-2-azabicyclo[2.2.1]hept-5-yl]hept-5-enoic acid
Homo sapiens
IC50 about 1 mM, recombinant enzyme, using prostamide D2 as substrate, in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.005
bimatoprost
Homo sapiens
recombinant enzyme, using prostaglandin D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.006
bimatoprost
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.06
bimatoprost
Homo sapiens
recombinant enzyme, using prostamide D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.13
ONO1349
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
ONO1349
Homo sapiens
recombinant enzyme, using prostaglandin D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
ONO1349
Homo sapiens
recombinant enzyme, using prostamide D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.3
ONO1370
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
ONO1370
Homo sapiens
recombinant enzyme, using prostaglandin D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
ONO1370
Homo sapiens
recombinant enzyme, using prostamide D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.06
ONO1373
Homo sapiens
recombinant enzyme, using prostaglandin H2 2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
ONO1373
Homo sapiens
recombinant enzyme, using prostaglandin D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
1
ONO1373
Homo sapiens
recombinant enzyme, using prostamide D2 2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.1
Tolrestat
Homo sapiens
recombinant enzyme, using prostaglandin D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.3
Tolrestat
Homo sapiens
recombinant enzyme, using prostaglandin H2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
0.45
Tolrestat
Homo sapiens
recombinant enzyme, using prostamide D2 as substrate,in 0.1 M potassium phosphate buffer, pH 6.5, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.003
0.041
purified recombinant enzyme, pH 7.0, 25°C, in presence of 0.05 mM 9,10-phenanthrenequinone
0.046
0.078
purified recombinant enzyme, pH 7.0, 25°C, in presence of 0.05 mM 9,10-phenanthrenequinone
0.089
0.095
0.31
0.339
additional information
additional information
-
expression levels in the placentome of pregnant cows at different developmental stages
additional information
-
at 37°C in 100 mM Tris/HCl (pH 7.0), the reaction product, 9-alpha,11-beta-prostaglandin F2 is detected as well as the substrate prostaglandin D2 in the reaction solution after reaction for 1 h, the amount of the product increases linearly for 1 h and then gradually plateaues
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
6.5
7.5
6.5
assay at, PGD2 11-ketoreductase activity and PGH2 9,11-endoperoxide reductase activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
-
the activity increases gradually as the temperature increases from 25 to 37°C, and then decreases significantly at 45°C compared with that at 37°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the result of amino acid analysis and sequence comparison suggest that epsilon-crystallin of the lens and prostaglandin F synthase are identical enzymes
-
-
brenda
2 isozymes PGFS-I and PGFS-II, soluble and membrane-associated isozymes
-
-
brenda
isozymes: 1 soluble not-inducible and 1 membraneous inducible by lipopolysaccharides
-
-
brenda
several isozymes, e.g. the endometrium-type, the lung-type and the liver-type isozymes
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
AKR1B3 mRNA 9 is expressed in preadipocytes, and its level increases about 4fold at day 1 after initiation of adipocyte differentiation, and then quickly decreases the following day to a level lower than that in the preadipocytes
brenda
-
expression of genes for PGE2 synthesis, with low levels of prostaglandin transporters and dehydrogenase
brenda
normal breast expresses very high levels of AKR1C3 relative to other tissues
brenda
-
production of PGE2, PGF2 and PGD2 and high prostaglandin turnover
brenda
-
peri- and postimplantation conceptus. Prostaglandin H synthase and prostaglandin E synthase are down-regulated, and prostaglandin G synthase, prostaglandin F synthase and carbonyl reductase/prostaglandin 9-reductase are down-regulated in conceptuses during trophoblasic elongation. After initiation of implantation, expression of prostaglandin G synthase, prostaglandin F synthase and carbonyl reductase/prostaglandin 9-reductase in conceptuses increases and remains higher until days 24-25 of pregnancy
brenda
isoform AKR1B1 is expressed at a high level during the menstrual cycle during the secretory phase and in both epithelial and stromal cells
brenda
isoform AKR1B1 is expressed at a high level during the menstrual cycle during the secretory phase and in both epithelial and stromal cells
brenda
-
co-localization of cyclooxygenase-1, prostaglandin F receptor and prostaglandin F synthase
brenda
-
enzyme co-localizes with myelin basic protein in myelin sheaths but not in axons
brenda
-
cultured oligodendrocytes at 7 days in vitro express the enzyme in cytoplasmic processes where the enzyme is co-localized with myelin basic protein
brenda
-
the enzyme is associated with the cyclooxygenase-II, COX-II
brenda
AKR1C3 is overexpressed in skin squamous cell carcinoma (SCC) and affects SCC growth via prostaglandin metabolism
brenda
additional information
-
enzyme is expressed preferentially in the white matter bundles of the entire central nervous system of adult mice with less marked expression inneuronal cell bodies. The enzyme co-localizes with myelin basic protein in myelin sheaths but not in axons
brenda
18fold increase in the median AKR1C3 mRNA levels in breast cancer patients as compared to those without disease
brenda
of invasive ductal carcinoma of the breast, immunohistochemical analysis
brenda
no or very low expression of prostaglandin F2alpha synthase synthase
brenda
high expression level of the lung-type and the microsomal endometrium-type isozymes
brenda
-
at days 12-14 of pregnancy and the estrous cycle, the expression of prostaglandin E2 synthase, prostaglandin F synthase, and carbonyl reductase/prostaglandin 9-ketoreductase genes and prostaglandin E2 synthase/prostaglandin F synthase ratio are significantly higher in corpora lutea of the pregnant gilts compared to the corpora lutea from the parallel ovaries of the cyclic gilts. There is no difference in expression of prostaglandin E2 synthase, prostaglandin F synthase, and carbonyl reductase/prostaglandin 9-ketoreductase genes and prostaglandin E2 synthase/prostaglandin F synthase ratio between corpora lutea ipsi- and contralateral to the uterine horn with the developing embryos
brenda
-
during luteolysis, activity of 20alpha-hydroxysteroid dehydrogenase synthesizing prostaglandin F2alpha
brenda
from cyclic and pregnant animals, high expression level of the microsomal endometrium-type isozyme, spatiotemporal expression during estrous cycle and early pregnancy
brenda
-
liver-type isozyme, sinusoidal endothelial cells in the liver
brenda
-
isozyme PGF synthase I in endothelial cells of the whole area of the spinal cord, and isozyme PGF synthase II in endothelial cells of the blood vessels only
brenda
both activities of enzymes AKR1C1/AKR1C2 and AKR1C3 are present in the periovuatory granulosa cell
brenda
-
both activities of enzymes AKR1C1/AKR1C2 and AKR1C3 are present in the periovuatory granulosa cell
-
brenda
-
both activities of enzymes AKR1C1/AKR1C2 and AKR1C3 are present in the periovuatory granulosa cell. Prostaglandin F synthase mRNA and protein levels are low before treatment with gonadotropin and peak 24-36 h after gonadotropin administration
brenda
-
both activities of enzymes AKR1C1/AKR1C2 and AKR1C3 are present in the periovuatory granulosa cell. Prostaglandin F synthase mRNA and protein levels are low before treatment with gonadotropin and peak 24-36 h after gonadotropin administration
-
brenda
-
proximal tubule, the enzyme is associated with the cyclooxygenase-I, COX-I
brenda
high expression level of the lung-type and the liver-type isozymes
brenda
-
in pregnant myometrium, PGI2, PGD2 and PGF2 synthases are highly expressed while prostaglandin dehydrogenase is underexpressed. Myometrium from non-pregnant women has lower levels of prostaglandin synthases and higher levels of prostaglandin dehydrogenase than pregnant myometrium
brenda
-
PGH2 9-,11-endoperoxide reductase activity is expressed and active at early pregnant sows, probably also in cyclic sows
brenda
-
expression levels in uninucleated trophoblasts of the placentome of pregnant cows, especially chorionic plate and apical tertiary villi, overview
brenda
-
the prostaglandin synthase expression profile favours production of PGD2, PGE2 and PGF2, with high levels of prostaglandin transporters and catabolic prostaglandin dehydrogenase suggesting rapid prostaglandin turnover
brenda
promastigotes synthesize prostaglandin F2alpha in the presence of arachidonic acid, with peak production in the stationary growth phase under heat stress
brenda
-
promastigotes synthesize prostaglandin F2alpha in the presence of arachidonic acid, with peak production in the stationary growth phase under heat stress
-
brenda
AKR1C3 is overexpressed in the fibrotic area of keloids (scarfs) while relatively weak staining is detected in normal skin
brenda
-
colocalization of prostaglandin F2alpha receptor FP and PGFS I
brenda
-
expression of both cyclooxygenase-1 and prostaglandin F synthase proteins in wild-type and prostaglandin F-receptor deficient strain
brenda
the bovine endometrium produces huge amounts of PGF2alpha
brenda
at oestrus and mid and late phases of pseudopregnancy
brenda
utero/placental expression of PGFS (AKR1C3) is identified in the superficial uterine glands throughout gestation and in the trophoblast cells within the feto-maternal contact zone during placentation. Colocalization of 15-hydroxyprostaglandin dehydrogenase (HPGD) with PGFS (AKR1C3) expression. Uterine PGFS (AKR1C3) is up-regulated postimplantation and declined prepartum
brenda
the prostaglandin F synthase AKR1B1 is upregulated while prostaglandin transporter is downregulated during term labor. The amnion is more responsive than choriodecidua to stimulation with proinflammatory cytokines. The mechanisms of term and preterm labor are different, overview
brenda
-
PGFS mRNA and protein expression in the endometrium does not differ between pregnancy and oestrous cycle but PGFS mRNA in the myometrium increases during pregnancy both in the gravid and the non-gravid uterine horns
brenda
additional information
quantitative enzyme expression analysis during pregnancy and prepartum
brenda
additional information
-
quantitative enzyme expression analysis during pregnancy and prepartum
brenda
additional information
AKR1B1 shows decreased expression in neoplastic disease, with decreased AKR1B1 immunoreactivity in carcinoma cells compared with nonneoplastic ductal cells, suggesting that AKR1B1 activity might be suppressed in tumor cells in breast cancer tissues
brenda
additional information
AKR1B1 shows decreased expression in neoplastic disease, with decreased AKR1B1 immunoreactivity in carcinoma cells compared with nonneoplastic ductal cells, suggesting that AKR1B1 activity might be suppressed in tumor cells in breast cancer tissues
brenda
additional information
isozyme expression levels and tissue distribution, overview
brenda
additional information
-
isozyme expression levels and tissue distribution, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
enriched in the secretory site of the parasite cell body, the flagellar pocket
brenda
-
enriched in the secretory site of the parasite cell body, the flagellar pocket
-
brenda
-
cultured oligodendrocytes at 7 days in vitro express the enzyme in cytoplasmic processes where the enzyme is co-localized with myelin basic protein
brenda
additional information
-
no liver-type isozyme in mitochondrion, nucleus, or Golgi apparatus
-
brenda
additional information
-
on gestation day GD90 enzyme PGFS is immunolocalized in the cytoplasm of large luteal cells only, whereas on GD108, sparse small luteal cells also display positive staining. PTGF receptor shows membranous localization within large luteal cells on both days of pregnancy. Immunohistochemic analysis of enzyme and prostaglandin F2 receptor during geestation, overview
-
brenda
additional information
-
on gestation day GD90 enzyme PGFS is immunolocalized in the cytoplasm of large luteal cells only, whereas on GD108, sparse small luteal cells also display positive staining. PTGF receptor shows membranous localization within large luteal cells on both days of pregnancy. Immunohistochemic analysis of enzyme and prostaglandin F2 receptor during geestation, overview
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
most prostaglandin F2alpha synthases (PGFS) identified to date are aldo-ketoreductases, AKRs
malfunction
the enzyme inhibitor 15-deoxy-delta12,14-prostaglandin J2 attenuates proliferation, inhibits collagen gel contraction and induces activation of the apoptotic marker, caspase-3, in CRL1762 keloid fibroblasts, overview
malfunction
although attenuating AKR1C3 expression in squamous cell carcinoma cells by siRNA does not affect growth, treatment with PGD2 and its dehydration metabolite, 15delta-PGJ2, decreases squamous cell carcinoma, SCC, proliferation in a PPARgamma-dependent manner. In addition, treatment with the PPARgamma agonist pioglitazone profoundly inhibits squamous cell carcinoma proliferation. SCC-AKR1C3 metabolizes protaglandin D2, PGD2, to 9alpha,11beta-prostaglandin F2 12fold faster than the parent cell line and is protected from the antiproliferative effect mediated by PGD2. PGD2 and its metabolite 15delta-prostaglandin J2 attenuate SCC proliferation in a PPARgamma-dependent manner, therefore activation of PPARgamma by agonists such as pioglitazone may benefit those at high risk of SCC
malfunction
administration of an AKR1C3 inhibitor significantly decreases 11beta-PGF2alpha concentrations in culture media of breast cancer cells
metabolism
AKR1B1 is involved in the synthesis of PGF2alpha. Pathways of prostaglandin F2alpha biosynthesis in human cells, overview
metabolism
AKR1B1 is able to produce PGF2alpha in the endometrium in addition toAKR1C3. The PGF synthase activity of AKR1B1 proves to be much higher than that of AKR1C3
metabolism
AKR1C3 is able to produce PGF2alpha in the endometrium in addition to AKR1B1. The PGF synthase activity of AKR1B1 proves to be much higher than that of AKR1C3
metabolism
the prostaglandin H2 (PGH2) is the common precursor of prostaglandin F2alpha (PGF2alphha) and prostaglandin E2 (PGE2). PGH2 is converted into one of the active prostaglandins by a specific terminal synthase, such as PGE2 synthase (PGES), which is responsible for PGE2 production or 9,11-endoperoxidase reductase, which has PGF2alpha synthase (PGFS) activity
metabolism
availability of prostaglandins can be regulated by changes in 15-hydroxyprostaglandin dehydrogenase, HPGD, an enzyme that catabolizes prostaglandin E2 and prostaglandin F2alpha to their inactive metabolites 13,14-dihydro-15keto-PGF2alpha and 13,14-dihydro-15-keto prostaglandin E2 (PGEM)
metabolism
enzyme PGF is involved in essential lipid metabolism pathways
metabolism
enzyme PGF is involved in essential lipid metabolism pathways
metabolism
there are three different pathways for the synthesis of the uterotonic PGF2alpha: 1. from PGH2 by PGH 9-,11-endoperoxide reductase, 2. from PGD2 by PGD 11-ketoreductase, 3. from PGE2 by PGE 9-ketoreductase
metabolism
AKR1C3 is an enzyme responsible for the metabolism of steroid hormones such as androgens, progesterones and estrogens in addition to the reduction of PGD2 to 11beta-PGF2alpha
metabolism
-
enzyme PGF is involved in essential lipid metabolism pathways
-
physiological function
prostamide/PGF synthase may play an important functional role in the central nervous system. It directly synthesizes prostamide/PGF2alpha from prostamide/PGH2 better than PGF synthase
physiological function
-
prostamide/PGF synthase may play an important functional role in the central nervous system
physiological function
-
knock-down by small interfering RNA for Akr1b3 suppresses PGF2 production and enhances the expression of adipogenic genes such as peroxisome proliferator-activated receptor gamma, fatty acid-binding protein 4, and stearoyl-CoA desaturase
physiological function
The major eicosanoid secreted by mast cells is prostaglandin D2 (PGD2), a relatively unstable pro-inflammatory mediator which can be spontaneously converted to 15-deoxy-(Delta12,14)-prostaglandin J2(15d-PGJ2) or enzymatically metabolized to 9alpha,11beta-PGF2 by aldo-keto reductase 1C3 (AKR1C3). Role of enzyme AKR1C3-mediated prostaglandin D2 (PGD2) metabolism in keloids, overview. Keloids are progressively expanding scars, mostly prevalent in individuals of African descent. Metabolism of PGD2 to 9a,11b-PGF2 by both, keloids and normal fibroblasts, is dependent on AKR1C3
physiological function
-
lentiviral vector-mediated delivery of the prostaglandin F synthase (PGFS) gene resultes in long-term reduction of intraocular pressure and may eliminate off-target tissue effects and the need for daily topical PGF2alpha self-administration
physiological function
prostaglandins (PGs) are important regulators of female reproductive function. The primary PGs produced in the endometrium are PGE2 and PGF2alpha. Role of aldo-ketoreductase (AKR)1B1 in increased PGF2alpha production by human endometrial cells following stimulation with interleukin-1beta (IL-1beta)
physiological function
PGF2alpha plays important roles in the regulation of ocular pressure, renal absorption, cardiovascular function, adipocyte differentiation, and female reproductive function. Role of bovine AKR1B1, previously known as AKR1B5, in the formation of PGF2alpha from PGH2 in the bovine endometrium
physiological function
PGF2alpha plays important roles in the regulation of ocular pressure, renal absorption, cardiovascular function, adipocyte differentiation, and female reproductive function. Role of AKR1C3 in the formation of PGF2alpha from PGH2 in the bovine endometrium
physiological function
-
prostaglandin F2alpha is the main luteolytic factor in pigs and its biosynthesis is catalyzed by prostaglandin F2alpha synthase, PGFS. The enzyme acts via specific seven-transmembrane G protein-coupled receptor (PTGFR) localized in large luteal cells. Intraluteal action of PGF2alpha causes a decrease in steroidogenic capacity and diminished production of progesterone. Intraluteal production of PGF2a is considered to be an important part of the luteolytic machinery
physiological function
the enzyme is involved in prostaglandins metabolism. The produced PGF2alpha can not only promote prostate cancer cell's proliferation but also enhance prostate cancer cells resistance to radition. Overexpression of AKR1C3 significantly enhances human prostate cancer cells PCa resistance to radiation (or tert-butyl hydroperoxide) through activation of MAPK pathway. AKR1C3 has a pivotal role in the radioresistance of esophageal cancer and non-small-cell lung cancer
physiological function
the utero/placental expression of PGFS (AKR1C3) is identified in the superficial uterine glands throughout gestation and in the trophoblast cells within the feto-maternal contact zone during placentation, suggesting a possible role for PGFS (AKR1C3) in the trophoblast invasion
physiological function
AKR1C3 is overexpressed in skin squamous cell carcinoma (SCC) and affects SCC growth via prostaglandin metabolism. AKR1C3 is overexpressed in various malignancies, suggesting a tumor promoting function. SCC-AKR1C3 metabolizes protaglandin D2, PGD2, to 9alpha,11beta prostaglandin F2. Unlike other AKR1C members, AKR1C3 can synthesize prostaglandin F2alpha from prostaglandin H2, an arachidonic acid derivative synthesized by cyclooxygenase
physiological function
in breast cancer, the status of the 11alpha-PGF2alpha and 11beta-PGF2alpha cognate FP receptor is associated with adverse clinical outcome only in the AKR1C3 positive cases, immunohistochemical analysis. FP receptor-mediated functions of 11beta-PGF2alpha using FP receptor expressed MCF-7 cell line shows that 11beta-PGF2alpha treatment phosphorylates ERK and CREB and induces Slug expression through FP receptor in MCF-FP, and MCF-FP cells demonstrate decreased chemosensitivity compared to parental controls. The actions of AKR1C3, but not of AKR1B1, can produce FP receptor ligands whose activation results in carcinoma cell survival in breast cancer. 11beta-PGF2alpha stimulates phosphorylation of ERK and CREB via FP receptor. AKR1C3-dependent signaling performs through 11beta-PGF2alpha and the FP receptor, overview
physiological function
in breast cancer, the status of the 11alpha-PGF2alpha and 11beta-PGF2alpha cognate FP receptor is associated with adverse clinical outcome only in the AKR1C3 positive cases, while there are no significant correlations between FP receptor status and any of the clinicathological parameters in AKR1B1 positive cases. AKR1B1 does not induce Slug expression
physiological function
parasites overexpressing PGFS show alteration of enzymes associated with oxidative stress protection such as superoxide dismutase A and trypanothione reductase. Transfected parasites are approximately 2 times more susceptible to benznidazole and 10 times more susceptible to H2O2, and to genetic damage and oxidative stress. Transfected parasites are less infective than wild-type parasites and they show higher alteration in mitochondrial membrane potential and cell cycle after treatment with benznidazole
physiological function
PGFS overexpressing parasites are less able to complete the infective cycle in cell culture infections and increase cardiac tissue parasitic load in infected mice. Parasites overexpressing the enzyme increase PGF2alpha synthesis from arachidonic acid and display increased susceptibility to benznidazole and nifurtimox but increased resistance to hydrogen peroxide
physiological function
overexpression of PGF2S leads to an increase of infectivity in vitro
physiological function
-
overexpression of PGF2S leads to an increase of infectivity in vitro
-
physiological function
-
parasites overexpressing PGFS show alteration of enzymes associated with oxidative stress protection such as superoxide dismutase A and trypanothione reductase. Transfected parasites are approximately 2 times more susceptible to benznidazole and 10 times more susceptible to H2O2, and to genetic damage and oxidative stress. Transfected parasites are less infective than wild-type parasites and they show higher alteration in mitochondrial membrane potential and cell cycle after treatment with benznidazole
-
physiological function
-
PGFS overexpressing parasites are less able to complete the infective cycle in cell culture infections and increase cardiac tissue parasitic load in infected mice. Parasites overexpressing the enzyme increase PGF2alpha synthesis from arachidonic acid and display increased susceptibility to benznidazole and nifurtimox but increased resistance to hydrogen peroxide
-
physiological function
-
prostaglandin F2alpha is the main luteolytic factor in pigs and its biosynthesis is catalyzed by prostaglandin F2alpha synthase, PGFS. The enzyme acts via specific seven-transmembrane G protein-coupled receptor (PTGFR) localized in large luteal cells. Intraluteal action of PGF2alpha causes a decrease in steroidogenic capacity and diminished production of progesterone. Intraluteal production of PGF2a is considered to be an important part of the luteolytic machinery
-
additional information
comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
additional information
-
comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
additional information
comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
additional information
-
comparisons of PGFS activity of recombinant bovine and human endometrial AKRs, overview
additional information
a loop with residues 201-205 (disordered) in LemaA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Leishmania major loop becomes ordered and a key interaction with one of the phosphates of NADP at Gln202 is likely to stabilize this region
additional information
-
a loop with residues 201-205 (disordered) in LemaA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Leishmania major loop becomes ordered and a key interaction with one of the phosphates of NADP at Gln202 is likely to stabilize this region
additional information
a loop with residues 188-196 in TrcrA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Trypanosoma cruzi loop becomes ordered and a key interaction with one of the phosphates of NADP at Ser193 is likely to stabilize this region
additional information
-
a loop with residues 188-196 in TrcrA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Trypanosoma cruzi loop becomes ordered and a key interaction with one of the phosphates of NADP at Ser193 is likely to stabilize this region
additional information
-
a loop with residues 188-196 in TrcrA.00019.a.B1 shows significant movement between the apoenzyme and holoenzyme. The Trypanosoma cruzi loop becomes ordered and a key interaction with one of the phosphates of NADP at Ser193 is likely to stabilize this region
-
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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). A0A3P3ZE14_LEIBR
284
0
31825
TrEMBL
-
E2IGW3_FELCA
134
0
15081
TrEMBL
other Location (Reliability: 4)
PGFS_LEIMA
284
0
31850
Swiss-Prot
other Location (Reliability: 3)
PGFS_TRYCC
Trypanosoma cruzi (strain CL Brener)
283
0
32571
Swiss-Prot
other Location (Reliability: 1)
Q9D5U2_MOUSE
291
0
33548
TrEMBL
other Location (Reliability: 1)
V5BT91_TRYCR
379
0
42208
TrEMBL
Secretory Pathway (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
35000
36000
36666
36670
36740
36742
-
1 * 36666, lung-type isozyme, sequence calculation, 1 * 36742, liver-type isozyme, sequence calculation
37000
36666
-
1 * 36666, lung-type isozyme, sequence calculation, 1 * 36742, liver-type isozyme, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
monomer
-
1 * 36666, lung-type isozyme, sequence calculation, 1 * 36742, liver-type isozyme, sequence calculation
additional information
enzyme has a (alpha/beta)8 barrel structure, from crystal structure determination
additional information
-
enzyme has a (alpha/beta)8 barrel structure, from crystal structure determination
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
16 mg/ml purified enzyme complexed with inhibitors acetate, flufenamic acid or indomethacin, hanging drop vapour diffusion method in 0.006 ml drops, 1:1 mixture of protein solution containing 10 mM potassium phosphate, pH 7.0, 1 mM DTT, 1 mM EDTA, 2 mM NADP+, with reservoir solution containing 25% w/v PEG 4000, 100 mM sodium citrate, pH 6.0, 2.5% v/v 2-methyl-2,4-pentanediol, and 800 mM ammonium acetate, 6 days to maximum size, X-ray diffraction structure determination of the complexes and analysis at 1.2-2.1 A resolution
20 mg/ml purified recombinant enzyme in a solution containing 1.4 mM PGD2 or inhibitor rutin, 1.2 mM NADP+ and NADPH, 50 mM MES, pH 6.0, and 25% w/v PEG 8000, hanging drop vapour diffusion method, 2-3 days, thick plate-shaped crystals of enzyme with NADP+ and PGD2 and of enzyme with NADPH and rutin, X-ray diffraction structure determination and analysis at 1.69 A resolution
in complex with bimatoprost and NADPH, hanging drop vapor diffusion method, using 1.0 mM BMP, 1.0 mM NADPH, 0.14 M NaCl, 50 mM MES buffer (pH 7.0), and 26% (w/v) PEG 8000
purified recombinant enzyme in complex with NADPH and bimatoprost BMP, an ocular hypotensive agent bound near the PGD2 binding site located on the alpha- and omega-chains, hanging drop vapour diffusion method, from 50 mM MES, pH 7.0, containing 7 mg/ml protein, 0.14 M NaCl, 26% w/v PEG 8000, 1.0 mM NADPH, and 1.0 mM BMP, added in a 95% ethanol solution, 4°C, 14 days, thick plate-shaped crystals, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified recombinant apoenzyme or enzyme with bound cofactor NADPH, mixing of 20 mg/ml protein in 25 mM Tris, pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with the reservoir solution containing 0.1 M sodium citrate pH 5.50, 20% PEG 3000 200 mM magnesium chloride, 100 mM Tris, pH 7.0, 10% PEG 8000 for apo- and complexed enzyme, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.8 A and 1.6 A resolution, respectively, molecular replacement
10 mg/ml purified recombinant enzyme from 0.1 M HEPES/NaOH, pH 7.5, 2.0 M ammonium sulfate, 5% w/v PEG 400, and 0.5 M NADPH by hanging drop vapour diffusion method, 20°C, 3 weeks, X-ray diffraction structure determination at room temperature and analysis at 2.6 A resolution
-
purified recombinant apoenzyme or enzyme with bound cofactor NADP+, mixing of 20 mg/ml protein in 25 mM Tris pH 8.0, 200 mM NaCl, 1% v/v glycerol, 1 mM TCEP with reservoir solution. For the apoenzyme, the reservoir solution contains 0.1 M MES-imidazole, pH 6.5, 10% PEG 20 000, 20% PEG 550 MME, 0.02 M glutamic acid, glycine, serine, alanine, and lysine, and for the cofactor complexed enzyme, it contains 0.2 M ammonium acetate, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350, cryoprotectant is 15% ethylene glycol, 16°C, 2-4 weeks, X-ray diffraction structure determination and analysis at 1.25 A and 2.6 A resolution, respectively, molecular replacement
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H170C
K225S
N306Y
R223L
R27E
R91Q
S301R
Y48F
69% of wild-type activity in presence of NADPH, 138% of wild-type isomerization activity in absence of NADPH, 0.2% of wild-type activity reducing 4-nitrobenzaldehyde
Y55F
P85W
mutagenesis to the corresponding residue in other mammalian AKR1C subfamily enzymes, results in broad substrate specificity for nonsteroidal carbonyls and alcohols
Y55F
-
complete elimination of PGD2, and PQ reductase activities, 27fold stimulation of PGH2 reductase activity
additional information
H170C
-
site-directed mutagenesis, increased Km for prostaglandin PGD2 and 8fold decreased Km for prostaglandin PGH2 compared to the wild-type enzyme
K225S
-
site-directed mutagenesis, slightly increased Km for prostaglandin PGD2 and PGH2 compared to the wild-type enzyme
N306Y
-
site-directed mutagenesis, increased Km for prostaglandin PGD2 and 5fold increased activity with prostaglandin PGH2 compared to the wild-type enzyme
R223L
-
site-directed mutagenesis, increased Km for prostaglandin PGD2 compared to the wild-type enzyme
R27E
-
site-directed mutagenesis, increased Km for prostaglandin PGD2 compared to the wild-type enzyme
R91Q
-
site-directed mutagenesis, increased Km for prostaglandin PGD2 compared to the wild-type enzyme
S301R
-
site-directed mutagenesis, slightly increased Km for prostaglandin PGD2 and PGH2 compared to the wild-type enzyme
Y55F
site-directed mutagenesis, the mutant loses its PGD2 11-ketoreductase activity, but not the PGH2 9,11-endoperoxide reductase
Y55F
the mutated enzyme loses the prostaglandin D2 11-ketoreductase activity but retains the prostaglandin H2 9,-11-endoperoxide reductase activity
additional information
-
lentiviral vector-mediated delivery of the prostaglandin F synthase (PGFS) gene to the eye. Expression of myc-tagged GFP-PGFS in non-human primate eyes via FIV vector leads to a significant reduction of intraocular pressure, IOP, the GFP-tag can still be detected after 48-52 weeks, the decrease in IOP lasts for 5 months. The IOP decrease is not as much as seen with topical prostaglandin therapy in monkey eyes, method evaluation. In human eye a single injection of lentiviral vectors into either the anterior or posterior chambers can induce a transient uveitis. Following transcorneal injection of vector into the living monkey eyes, biomicroscopic examination initially reveal cells and flare in the anterior chamber and some corneal haze that is largely resolved by 3 weeks post injection. This is not due to bacterial endotoxin contamination of the vector preparations and is likely the result of activation of innate viral sensors in the eye
additional information
-
coexpression of COX-1 and COX-2 increases the endogenous cytosolic PGFS-I activity, but only slightly the membrane-bound activity, overview
additional information
knockout of AKR1B1 gene expression in human endometrial cell lines using the CRISPR/Cas9 system. Clone 16-2 exhibits deletion of 68 and 2 nucleotides, respectively, on each of the alleles. Cells from this clone lose their ability to produce PGF2alpha but maintain their original human endometrial stromal cells-2 phenotype including the capacity to decidualize in the presence of progesterone (medroxyprogesterone acetate) and 8-bromo-cAMP. Knockout cells also maintain their ability to increase PGE2 production in response to interleukin-1beta
additional information
-
knockout of AKR1B1 gene expression in human endometrial cell lines using the CRISPR/Cas9 system. Clone 16-2 exhibits deletion of 68 and 2 nucleotides, respectively, on each of the alleles. Cells from this clone lose their ability to produce PGF2alpha but maintain their original human endometrial stromal cells-2 phenotype including the capacity to decidualize in the presence of progesterone (medroxyprogesterone acetate) and 8-bromo-cAMP. Knockout cells also maintain their ability to increase PGE2 production in response to interleukin-1beta
additional information
establishment of a stable overexpressing AKR1C3 cell line (AKR1C3-over) derived from the prostate cell line DU145
additional information
AKR1C3 overexpressing skin squamous cell carcinoma, SCC, cells are protected from the antiproliferative effects of prostaglandin D2
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
several freezing and thawing cycles reduce the activity of stored purified liver-type isozyme by 50%
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, concentration 1.5 mg per ml 10 mM potassium phosphate buffer pH 7.0, stable for several months
-
-80°C, purified liver-type isozyme at 1.5 mg/ml in 10 mM potassium phosphate, pH 7.0, stable for several months, several freezing and thawing cycles reduce the activity by 50%
-
25°C, concentration 1.5 mg per ml 10 mM potassium phosphate buffer pH 7.0, 80-90% activity, 1 month
-
4°C, concentration 1.5 mg per ml 10 mM potassium phosphate buffer pH 7.0, 80-90% activity, 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native liver-type isozyme from liver, 342fold to homogeneity by ammonium sulfate fractionation, anion exchange and adsorption chromatography
-
on Ni2+ column, 102- and 152fold purification of the prostamide F synthase and PGF synthase activities, respectively, achieved from the swine brain (90 g) with a yield of 1.4 and 2%, respectively. Mutants expressed to homogeneity
recombinant enzyme from Escherichia coli by GSH affinity chromatography, cleavage of the fusion protein glutathione S-tranferase by thrombin, and DEAE ion exchange chromatography
-
recombinant His-tagged canine-specific PGFS (AKR1C3) from Escherichia coli
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration followed by a polyether sulfon concentration
recombinant wild-type liver-type isoyzme and mutant enzymes from COS-7 cells, to homogeneity
-
to apparent homogeneity, on Ni-NTA resin and by gel filtration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration followed by a polyether sulfon concentration
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration followed by a polyether sulfon concentration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence analysis, expression analysis in endometrium of cyclic and pregnant animals
expressed in Escherichia coli HB101 cells
expression in Escherichia coli
expression of myc-tagged GFP-PGFS in non-human primate eyes via FIV vector leading to a significant reduction of intraocular pressure, IOP, the GFP-tag can still be detected after 48-52 weeks, the decrease in IOP lasted for 5 months, method evaluation
-
gene AKR1B1, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, recombinant expression in immortalized human endometrial stromal cells, HIESC-2 cells, expression analysis in clones 16-1, 16-2, and 16-4. Clones 16-1 and 16-2 present with a complete absence of AKR1B1 protein, while clone 16-4 is able to express the AKR1B1 protein. Following treatment of cells with interleukin-1beta, both wild-type and clone 16-4 cells exhibit a similar response, but clone 16-2 does not respond with increased production of eitherPGF2alpha or PGE2. At the protein level, IL-1beta induces an increase in mPGES-1 and COX-2 protein expression but in clone 16-2 the relative increase of Cox-2 protein is weaker
gene AKR1B1, recombinant expression of N-terminally His8-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene AKR1C3, recombinant expression of N-terminally His8-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene P100/11E, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene PGFS, quantitative expression analysis, recombinant expression of His-tagged canine-specific PGFS (AKR1C3) in Escherichia coli
gene Tc00.1047053511287.49, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
into vector pET-28a and expressed in Escherichia coli BL21 (DE3)
liver-type isozyme, full length cDNA from cDNA library, DNA and amino acid sequence determination and analysis, transient expression of wild-type and mutant enzymes in COS-7 cells
-
overexpression of AKR1C3 using a pLNCX retroviral vector in MCF-7 cell line
SCC cell line is infected with either AKR1C3 overexpressing retroviral construct (SCC-AKR1C3), quantitative AKR1C3 expression analysis in wild-type and mtransfected cells
wild-type and mutants, plasmid pCold II-PM/PGFS expressed in Escherichia coli BL21 cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after treatment with estradiol, PGFS mRNA expression increases 2.9fold after 4 h and reaches a maximum level of 3.8-4.4fold after 8 to 24 h
-
AKR1B1 expression is induced by interleukin-1beta leading to a higher production of prostaglandin F2alpha
AKR1B1 shows decreased expression in neoplastic disease, AKR1B1 activity might be suppressed in tumor cells in breast cancer tissues
AKR1B3 mRNA is expressed in preadipocytes, and its level increases about 4fold at day 1 after initiation of adipocyte differentiation, and then quickly decreases the following day to a level lower than that in the preadipocytes
-
AKR1C3 expression is induced by interleukin-1beta leading to a higher production of prostaglandin F2alpha
AKR1C3 is overexpressed in skin squamous cell carcinoma (SCC) and affects SCC growth via prostaglandin metabolism. It is upregulated by its substrate, prostaglandin D2
expression is significantly up-regulated by oestradiol plus progesterone at oestrus and the mid phase of pseudopregnancy and is also up-regulated by a single treatment with progesterone at late pseudopregnancy. Simultaneous incubation with oestradiol and progesterone up-regulates prostaglandin-endoperoxide synthase PTGS2 gene expression at oestrus and mid-luteal phase. Treatment with oestradiol and /or progesterone affects neither prostaglandin F2alpha secretion nor prostaglandin F2alpha synthase expression at any phase after 12 h of culture
expression of AKR1B1 is upregulated in the fetal membranes in association with term labor, during labor tumor necrosis factor TNF upregulates the AKR1B1 protein expression
expression of the enzyme increases between P9 and P14 during the postnatal development, presumably in accordance with myelinogenesis
-
flutamide, i.e. 2-methyl-N-[4-nitro-30-(trifluoromethyl)-phenyl]propamide, causes upregulation of enzyme PGFS mRNA and protein amount in pregnant female pigs at gestation days 90 and 108, whereas PTGF receptor protein expression is greater in both gestational periods
in cultured myometrial cells there is a dose-dependent stimulatory effect of interleukin 1beta and tumor necrosis factor alpha on PTGS2, PTGES and AKR1B1, i.e.PGF synthase expression
-
interleukin IL-1beta is able to upregulate COX-2 and AKR1B1 proteins as well as prostaglandin F2alpha production under normal glucose concentrations. The promoter activity of AKR1B1 gene is increased by IL-1beta particularly around the multiple stress response region
PGF2S is constitutively expressed throughout promastigote development
PGFS mRNA in the myometrium increases during pregnancy both in the gravid and the non-gravid uterine horns
-
treatment with estradiol and/or progesterone affects neither PGF2alpha secretion nor enzyme PGFS expression at any phase after 12 h of culture, while related enzymes PG-endoperoxide synthase (PTGS2) and PGE2 synthase (PGES) are both upregulated by estradiol and progesterone during pseudopregnancy
flutamide, i.e. 2-methyl-N-[4-nitro-30-(trifluoromethyl)-phenyl]propamide, causes upregulation of enzyme PGFS mRNA and protein amount in pregnant female pigs at gestation days 90 and 108, whereas PTGF receptor protein expression is greater in both gestational periods
-
flutamide, i.e. 2-methyl-N-[4-nitro-30-(trifluoromethyl)-phenyl]propamide, causes upregulation of enzyme PGFS mRNA and protein amount in pregnant female pigs at gestation days 90 and 108, whereas PTGF receptor protein expression is greater in both gestational periods
-
-
PGF2S is constitutively expressed throughout promastigote development
PGF2S is constitutively expressed throughout promastigote development
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
prostaglandin formation is a key component of PGaction and the specific target of non-steroidal anti-inflammatory drugs
medicine
molecular biology
genome editing of human cell lines can be used to complement mouse KO models to validate the function of genes in differentiated tissues and cells
pharmacology
enzyme is a target for cyclooxygenase-independent antineoplastic actions of nonsteroidal anti-inflammatory drugs
synthesis
-
development of a coupled assay method for enzymatic formation of prostamide F2alpha from anandamide by the cyclooxygenase-II and the prostaglandin synthase F involving the intermediate metabolite, prostamide H2
medicine
-
peri- and postimplantation conceptus. Prostaglandin H synthase and prostaglandin E synthase are down-regulated, and prostaglandin G synthase, prostaglandin F synthase and carbonyl reductase/prostaglandin 9-reductase are down-regulated in conceptuses during trophoblasic elongation. After initiation of implantation, expression of prostaglandin G synthase, prostaglandin F synthase and carbonyl reductase/prostaglandin 9-reductase in conceptuses increases and remains higher until days 24-25 of pregnancy
medicine
AKR1C3 likely plays important roles in the development of hormone-dependent, and possibly hormone-independent, breast cancer. It is highly expressed in normal breast and upregulated in breast cancer, where its expression is associated with a worse prognosis
medicine
-
lentiviral vector-mediated delivery of the prostaglandin F synthase (PGFS) gene resultes in long-term reduction of intraocular pressure and may eliminate off-target tissue effects and the need for daily topical PGF2alpha self-administration
medicine
-
significantly higher expression of the prostaglandin-endoperoxide synthase PTGS 2 gene is detected in repeat-breeding cows with subclinical endometritis, whereas there is no significant difference in the expression of prostaglandin F2alpha synthase PTGFS and prostaglandin E2 microsomal synthase mPTGES 1 mRNAs between repeat-breeding cows with subclinical endometritis and those without it
medicine
-
estradiol causes a short-term increase in cyclooxygenase COX-2, which stimulates PGE2 and PGF2alpha secretion, and a subsequent decrease in COX-2 and an increase in cyclooxygenase COX-1 produce a high PGE2 : PGF2alpha ratio
medicine
mice infected with PGFS overexpressing parasites show an early parasitemia peak and higher heart muscle parasitic load
medicine
-
mice infected with PGFS overexpressing parasites show an early parasitemia peak and higher heart muscle parasitic load
-
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REF.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
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Immunocytochemical localization of lung-type prostaglandin F synthase in the rat spinal cord
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Identification of a novel prostaglandin F2.alpha. synthase in Trypanosoma brucei
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Detection and regulation of the messenger for a putative bovine endometrial 9-keto-prostaglandin E2 reductase: effect of oxytocin and interferon-tau
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Suzuki-Yamamoto, T.; Nishizawa, M.; Fukui, M.; Okuda-Ashitaka, E.; Nakajima, T.; Ito, S.; Watanabe, K.
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Xiao, C.W.; Murphy, B.D.; Sirois, J.; Goff, A.K.
Down-regulation of oxytocin-induced cyclooxygenase-2 and prostaglandin F synthase expression by interferon-.tau. in bovine endometrial cells
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60
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Bos taurus
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Prostaglandin F synthase is localized to contractile interstitial cells in bovine lung
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A lung type prostaglandin F synthase is expressed in bovine liver: cDNA sequence and expression in E. coli
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1238-1246
1992
Bos taurus
brenda
Chen, L.Y.; Watanabe, K.; Hayaishi, O.
Purification and characterization of prostaglandin F synthase from bovine liver
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296
17-26
1992
Bos taurus
brenda
Watanabe, K.; Fujii, Y.; Ohkubo, H.; Kuramitsu, S.; Kagamiyama, H.; Nakanishi, S.; Hayaishi, O.
Expression of bovine lung prostaglandin F synthase in Escherichia coli
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181
272-278
1991
Bos taurus
brenda
Watanabe, K.; Fujii, Y.; Nakayama, K.; Ohkubo, H.; Kuramitsu, S.; Hayashi, H.; Kagamiyama, H.; Nakanishi, S.; Hayaishi, O.
Cloning, nucleotide sequence and gene expression of bovine lung prostaglandin F synthetase
Adv. Prostaglandin Thromboxane Leukot. Res.
19
462-465
1988
Bos taurus
brenda
Wolfe, L.S.; Rostworowski, K.; Pellerin, L.; Sherwin, A.
Metabolism of prostaglandin D2 by human cerebral cortex into 9alpha,11beta-prostaglandin F2 by an active NADPH-dependent 11-ketoreductase:Metabolism of prostaglandin D2 by human cerebral cortex into 9alpha,11beta-prostaglandin F2 by an active NADPH-dependent 11-ketoreductase
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53
64-70
1989
Homo sapiens
brenda
Watanabe, K.; Fujii, Y.; Nakayama, K.; Ohkubo, H.; Karamitsu, S.; Kagamiyama, H.; Nakanishi, S.; Hayaishi, O.
Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog
Proc. Natl. Acad. Sci. USA
85
11-15
1988
Bos taurus, Rana temporaria
brenda
Goh, Y.; Urade, Y.; Fujimoto, N.; Hayaishi, O.
Content and formation of prostaglandins and distribution of prostaglandin-related enzyme activities in the rat ocular system
Biochim. Biophys. Acta
921
302-311
1987
Rattus norvegicus
brenda
Watanabe, K.; Yoshida, R.; Shimizu, T.; Hayaishi, O.
Enzymatic formation of prostaglandin F2 alpha from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung
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260
7035-7041
1985
Bos taurus
brenda
Wong, P.Y.K.
Purification of PGD2 11-ketoreductase from rabbit liver
Methods Enzymol.
86
117-125
1982
Oryctolagus cuniculus
brenda
Wong, P.Y.K.
Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver
Biochim. Biophys. Acta
659
169-178
1981
Oryctolagus cuniculus
brenda
Reingold, D.F.; Kawasaki, A.; Needleman, P.
A novel prostaglandin 11-keto reductase found in rabbit liver
Biochim. Biophys. Acta
659
179-188
1981
Oryctolagus cuniculus
brenda
Watanabe, K.; Shimizu, T.; Hayaishi, O.
Enzymic conversion of prostaglandin D2 to F2alpha in the rat lung
Biochem. Int.
2
603-610
1981
Rattus norvegicus
-
brenda
Suzuki-Yamamoto, T.; Fujii, Y.; Miyano, M.; Chen, L.Y.; Takahashi, T.; Yokoi, H.; Tsuruo, Y.; Ishimura, K.; Watanabe, K.
cDNA cloning and mutagenesis study of liver-type prostaglandin F synthase, and identification of the prostaglandin F producing cells in the liver
Adv. Exp. Med. Biol.
507
263-268
2002
Bos taurus
brenda
Koda, N.; Tsutsui, Y.; Niwa, H.; Ito, S.; Woodward, D.F.; Watanabe, K.
Synthesis of prostaglandin F ethanolamide by prostaglandin F synthase and identification of Bimatoprost as a potent inhibitor of the enzyme: new enzyme assay method using LC/ESI/MS
Arch. Biochem. Biophys.
424
128-136
2004
Homo sapiens, Homo sapiens (P42330)
brenda
Komoto, J.; Yamada, T.; Watanabe, K.; Takusagawa, F.
Crystal structure of human prostaglandin F synthase (AKR1C3)
Biochemistry
43
2188-2198
2004
Homo sapiens (P42330), Homo sapiens
brenda
Nakashima, K.; Ueno, N.; Kamei, D.; Tanioka, T.; Nakatani, Y.; Murakami, M.; Kudo, I.
Coupling between cyclooxygenases and prostaglandin F(2alpha) synthase. Detection of an inducible, glutathione-activated, membrane-bound prostaglandin F2alpha-synthetic activity
Biochim. Biophys. Acta
1633
96-105
2003
Homo sapiens, Rattus norvegicus, Mus musculus
brenda
Suzuki-Yamamoto, T.; Toida, K.; Watanabe, K.; Ishimura, K.
Immunocytochemical localization of prostaglandin F synthase II in the rat spinal cord
Brain Res.
969
27-35
2003
Rattus norvegicus
brenda
Lovering, A.L.; Ride, J.P.; Bunce, C.M.; Desmond, J.C.; Cummings, S.M.; White, S.A.
Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal anti-inflammatory drugs flufenamic acid and indomethacin
Cancer Res.
64
1802-1810
2004
Homo sapiens (P42330)
brenda
Okano, Y.; Inoue, T.; Kubata, B.K.; Kabututu, Z.; Urade, Y.; Matsumura, H.; Kai, Y.
Crystallization and preliminary X-ray crystallographic studies of Trypanosoma brucei prostaglandin F2 alpha synthase
J. Biochem.
132
859-861
2002
Trypanosoma brucei
brenda
Watanabe, K.
Prostaglandin F synthase
Prostaglandins
68-69
401-407
2002
Trypanosoma brucei, Ovis aries, Rattus norvegicus, Bos taurus, Homo sapiens, Oryctolagus cuniculus
brenda
Franczak, A.; Woclawek-Potocka, I.; Oponowicz, A.; Kurowicka, B.; Kotwica, G.
Oxytocin stimulates prostaglandin F2alpha secretion and prostaglandin F synthase protein expression in porcine myometrial tissue
Reprod. Biol.
4
177-184
2004
Sus scrofa
brenda
Waclawik, A.; Rivero-Muller, A.; Blitek, A.; Kaczmarek, M.M.; Brokken, L.J.; Watanabe, K.; Rahman, N.A.; Ziecik, A.J.
Molecular cloning and spatiotemporal expression of prostaglandin F synthase and microsomal prostaglandin E synthase-1 in porcine endometrium
Endocrinology
147
210-221
2006
Sus scrofa (Q2TJA5), Sus scrofa
brenda
Ueno, N.; Takegoshi, Y.; Kamei, D.; Kudo, I.; Murakami, M.
Coupling between cyclooxygenases and terminal prostanoid synthases
Biochem. Biophys. Res. Commun.
338
70-76
2005
Mus musculus
brenda
Sakurai, M.; Oishi, K.; Watanabe, K.
Localization of cyclooxygenases-1 and -2, and prostaglandin F synthase in human kidney and renal cell carcinoma
Biochem. Biophys. Res. Commun.
338
82-86
2005
Homo sapiens
brenda
Komoto, J.; Yamada, T.; Watanabe, K.; Woodward, D.F.; Takusagawa, F.
Prostaglandin F2alpha formation from prostaglandin H2 by prostaglandin F synthase (PGFS): crystal structure of PGFS containing bimatoprost
Biochemistry
45
1987-1996
2006
Homo sapiens, Homo sapiens (P42330)
brenda
Yang, W.; Ni, J.; Woodward, D.F.; Tang-Liu, D.D.; Ling, K.H.
Enzymatic formation of prostamide F2alpha from anandamide involves a newly identified intermediate metabolite, prostamide H2
J. Lipid Res.
46
2745-2751
2005
Homo sapiens
brenda
Schuler, G.; Teichmann, U.; Kowalewski, M.P.; Hoffmann, B.; Madore, E.; Fortier, M.A.; Klisch, K.
Expression of cyclooxygenase-II (COX-II) and 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD)/prostaglandin F-synthase (PGFS) in bovine placentomes: implications for the initiation of parturition in cattle
Placenta
27
1022-1029
2006
Bos taurus
brenda
Kowalewski, M.P.; Mutembei, H.M.; Hoffmann, B.
Canine prostaglandin F2alpha receptor (FP) and prostaglandin F2alpha synthase (PGFS): Molecular cloning and expression in the corpus luteum
Anim. Reprod. Sci.
107
161-175
2008
Canis lupus familiaris (Q5FYA7), Canis lupus familiaris
brenda
Byrns, M.C.; Steckelbroeck, S.; Penning, T.M.
An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3alpha-HSD, type 5 17beta-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies
Biochem. Pharmacol.
75
484-493
2008
Homo sapiens (P42330)
brenda
Suzuki-Yamamoto, T.; Sugimoto, Y.; Ichikawa, A.; Ishimura, K.
Co-localization of prostaglandin F synthase, cyclooxygenase-1 and prostaglandin F receptor in mouse Leydig cells
Histochem. Cell Biol.
128
317-322
2007
Mus musculus
brenda
Moriuchi, H.; Koda, N.; Okuda-Ashitaka, E.; Daiyasu, H.; Ogasawara, K.; Toh, H.; Ito, S.; Woodward, D.F.; Watanabe, K.
Molecular characterization of a novel type of prostamide/prostaglandin F synthase, belonging to the thioredoxin-like superfamily
J. Biol. Chem.
283
792-801
2008
Sus scrofa (A9CQL8), Sus scrofa, Mus musculus
brenda
Waclawik, A.; Ziecik, A.J.
Differential expression of prostaglandin (PG) synthesis enzymes in conceptus during peri-implantation period and endometrial expression of carbonyl reductase/PG 9-ketoreductase in the pig
J. Endocrinol.
194
499-510
2007
Sus scrofa
brenda
Wasielak, M.; Glowacz, M.; Kaminska, K.; Waclawik, A.; Bogacki, M.
The influence of embryo presence on prostaglandins synthesis and prostaglandin E2 and F2alpha content in corpora lutea during periimplantation period in the pig
Mol. Reprod. Dev.
75
1208-1216
2008
Sus scrofa
brenda
Dozier, B.L.; Watanabe, K.; Duffy, D.M.
Two pathways for prostaglandin F2 alpha synthesis by the primate periovulatory follicle
Reproduction
136
53-63
2008
Macaca fascicularis, Homo sapiens (P42330), Homo sapiens AKR1C3 (P42330), Macaca fascicularis AKR1C3
brenda
Byrns, M.; Penning, T.
Type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): Role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs
Chem. Biol. Interact.
178
221-227
2009
Homo sapiens, Homo sapiens (P42330)
brenda
Inagaki, S.; Esaka, Y.; Deyashiki, Y.; Uno, B.; Hara, A.; Toyooka, T.
Human liver dihydrodiol dehydrogenase 1-catalyzed reaction generating 9alpha,11beta-prostaglandin F2 from prostaglandin D2 followed by micellar electrokinetic chromatography
J. Sep. Sci.
31
735-740
2008
Homo sapiens
brenda
Kabututu, Z.; Manin, M.; Pointud, J.C.; Maruyama, T.; Nagata, N.; Lambert, S.; Lefrancois-Martinez, A.M.; Martinez, A.; Urade, Y.
Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1, 1B3 and 1B7
J. Biochem.
145
161-168
2009
Homo sapiens (P15121), Homo sapiens (P42330), Homo sapiens, Mus musculus
brenda
Suzuki-Yamamoto, T.; Toida, K.; Sugimoto, Y.; Ishimura, K.
Colocalization of prostaglandin F2alpha receptor FP and prostaglandin F synthase-I in the spinal cord
J. Lipid Res.
50
1996-2003
2009
Rattus norvegicus
brenda
Wasielak, M.; Kaminska, K.; Bogacki, M.
Effect of the conceptus on uterine prostaglandin-F2alpha and prostaglandin-E2 release and synthesis during the periimplantation period in the pig
Reprod. Fertil. Dev.
21
709-717
2009
Sus scrofa
brenda
Yoshikawa, K.; Takei, S.; Hasegawa-Ishii, S.; Chiba, Y.; Furukawa, A.; Kawamura, N.; Hosokawa, M.; Woodward, D.F.; Watanabe, K.; Shimada, A.
Preferential localization of prostamide/prostaglandin F synthase in myelin sheaths of the central nervous system
Brain Res.
1367
22-32
2011
Mus musculus
brenda
Fujimori, K.; Ueno, T.; Nagata, N.; Kashiwagi, K.; Aritake, K.; Amano, F.; Urade, Y.
Suppression of adipocyte differentiation by aldo-keto reductase 1B3 acting as prostaglandin F2alpha synthase
J. Biol. Chem.
285
8880-8886
2010
Mus musculus
brenda
Phillips, R.J.; Al-Zamil, H.; Hunt, L.P.; Fortier, M.A.; Lopez Bernal, A.
Genes for prostaglandin synthesis, transport and inactivation are differentially expressed in human uterine tissues, and the prostaglandin F synthase AKR1B1 is induced in myometrial cells by inflammatory cytokines
Mol. Hum. Reprod.
17
1-13
2011
Homo sapiens
brenda
Nagata, N.; Kusakari, Y.; Fukunishi, Y.; Inoue, T.; Urade, Y.
Catalytic mechanism of the primary human prostaglandin F2alpha synthase, aldo-keto reductase 1B1 - prostaglandin D2 synthase activity in the absence of NADP(H)
FEBS J.
278
1288-1298
2011
Homo sapiens (P15121), Homo sapiens, Mus musculus
brenda
Bresson, E.; Lacroix-Pepin, N.; Boucher-Kovalik, S.; Chapdelaine, P.; Fortier, M.A.
The prostaglandin F synthase activity of the human aldose reductase AKR1B1 brings new lenses to look at pathologic conditions
Front. Pharmacol.
3
98
2012
Homo sapiens (P15121), Homo sapiens
brenda
Bresson, E.; Boucher-Kovalik, S.; Chapdelaine, P.; Madore, E.; Harvey, N.; Laberge, P.Y.; Leboeuf, M.; Fortier, M.A.
The human aldose reductase AKR1B1 qualifies as the primary prostaglandin F synthase in the endometrium
J. Clin. Endocrinol. Metab.
96
210-219
2011
Homo sapiens (P15121), Homo sapiens
brenda
Liedtke, A.J.; Adeniji, A.O.; Chen, M.; Byrns, M.C.; Jin, Y.; Christianson, D.W.; Marnett, L.J.; Penning, T.M.
Development of potent and selective indomethacin analogues for the inhibition of AKR1C3 (Type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase) in castrate-resistant prostate cancer
J. Med. Chem.
56
2429-2446
2013
Homo sapiens (P42330)
brenda
Siemieniuch, M.J.; Jursza, E.; Kowalewski, M.P.; Majewska, M.; Skarzynski, D.J.
Prostaglandin endoperoxide synthase 2 (PTGS2) and prostaglandins F2alpha and E2 synthases (PGFS and PGES) expression and prostaglandin F2alpha and E2 secretion following oestrogen and/or progesterone stimulation of the feline endometrium
Reprod. Domest. Anim.
48
72-78
2013
Felis catus (E2IGW3), Felis catus
brenda
Moen, S.O.; Fairman, J.W.; Barnes, S.R.; Sullivan, A.; Nakazawa-Hewitt, S.; Van Voorhis, W.C.; Staker, B.L.; Lorimer, D.D.; Myler, P.J.; Edwards, T.E.
Structures of prostaglandin F synthase from the protozoa Leishmania major and Trypanosoma cruzi with NADP
Acta Crystallogr. Sect. F
71
609-614
2015
Leishmania major (P22045), Leishmania major, Trypanosoma cruzi (Q4DJ07), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4DJ07)
brenda
Gram, A.; Buechler, U.; Boos, A.; Hoffmann, B.; Kowalewski, M.P.
Biosynthesis and degradation of canine placental prostaglandins: prepartum changes in expression and function of prostaglandin F2?-synthase (PGFS, AKR1C3) and 15-hydroxyprostaglandin dehydrogenase (HPGD)
Biol. Reprod.
89
2-2
2013
Canis lupus familiaris (Q5FYA7), Canis lupus familiaris
brenda
Lee, E.S.; Rasmussen, C.A.; Filla, M.S.; Slauson, S.R.; Kolb, A.W.; Peters, D.M.; Kaufman, P.L.; Gabelt, B.T.; Brandt, C.R.
Prospects for lentiviral vector mediated prostaglandin F synthase gene delivery in monkey eyes in vivo
Curr. Eye Res.
39
859-870
2014
Bos taurus
brenda
Grzesiak, M.; Knapczyk-Stwora, K.; Slomczynska, M.
The impact of flutamide on prostaglandin F2alpha synthase and prostaglandin F2alpha receptor expression, and prostaglandin F2alpha concentration in the porcine corpus luteum of pregnancy
Domest. Anim. Endocrinol.
59
81-89
2017
Sus scrofa, Sus scrofa Large White x Polish Landrace
brenda
Mantel, A.; Carpenter-Mendini, A.; VanBuskirk, J.; Pentland, A.P.
Aldo-keto reductase 1C3 is overexpressed in skin squamous cell carcinoma (SCC) and affects SCC growth via prostaglandin metabolism
Exp. Dermatol.
23
573-578
2014
Homo sapiens (P42330)
brenda
Mantel, A.; Newsome, A.; Thekkudan, T.; Frazier, R.; Katdare, M.
The role of aldo-keto reductase 1C3 (AKR1C3)-mediated prostaglandin D2 (PGD2) metabolism in keloids
Exp. Dermatol.
25
38-43
2016
Homo sapiens (P42330)
brenda
Alzamil, H.A.; Pawade, J.; Fortier, M.A.; Bernal, A.L.
Expression of the prostaglandin F synthase AKR1B1 and the prostaglandin transporter SLCO2A1 in human fetal membranes in relation to spontaneous term and preterm labor
Front. Physiol.
5
272
2014
Homo sapiens (P15121), Homo sapiens
brenda
Yoda, T.; Kikuchi, K.; Miki, Y.; Onodera, Y.; Hata, S.; Takagi, K.; Nakamura, Y.; Hirakawa, H.; Ishida, T.; Suzuki, T.; Ohuchi, N.; Sasano, H.; McNamara, K.M.
11beta-Prostaglandin F2alpha, a bioactive metabolite catalyzed by AKR1C3, stimulates prostaglandin F receptor and induces slug expression in breast cancer
Mol. Cell. Endocrinol.
413
236-247
2015
Homo sapiens (P15121), Homo sapiens (P42330)
brenda
Lacroix Pepin, N.; Chapdelaine, P.; Rodriguez, Y.; Tremblay, J.P.; Fortier, M.A.
Generation of human endometrial knockout cell lines with the CRISPR/Cas9 system confirms the prostaglandin F2alpha synthase activity of aldo-ketoreductase 1B1
Mol. Hum. Reprod.
20
650-663
2014
Homo sapiens (P15121), Homo sapiens
brenda
Sun, S.Q.; Gu, X.; Gao, X.S.; Li, Y.; Yu, H.; Xiong, W.; Yu, H.; Wang, W.; Li, Y.; Teng, Y.; Zhou, D.
Overexpression of AKR1C3 significantly enhances human prostate cancer cells resistance to radiation
Oncotarget
7
48050-48058
2016
Homo sapiens (P42330)
brenda
Lacroix Pepin, N.; Chapdelaine, P.; Fortier, M.A.
Evaluation of the prostaglandin F synthase activity of human and bovine aldo-keto reductases: AKR1A1s complement AKR1B1s as potent PGF synthases
Prostaglandins Other Lipid Mediat.
106
124-132
2013
Bos taurus (P16116), Bos taurus, Homo sapiens (P15121), Homo sapiens
brenda
Janowski, T.; Baranski, W.; Lukasik, K.; Skarzynski, D.; Zdunczyk, S.; Malinowska, K.
Endometrial mRNA expression of prostaglandin synthase enzymes PTGS 2, PTGFS and mPTGES 1 in repeat-breeding cows with cytologically determined endometritis
Acta Vet. Hung.
65
96-104
2017
Bos taurus
brenda
Endo, S.; Matsunaga, T.; Hara, A.
Mouse Akr1cl gene product is a prostaglandin D2 11-ketoreductase with strict substrate specificity
Arch. Biochem. Biophys.
674
108096
2019
Mus musculus (Q9D5U2), Mus musculus
brenda
Diaz-Viraque, F.; Chiribao, M.L.; Trochine, A.; Gonzalez-Herrera, F.; Castillo, C.; Liempi, A.; Kemmerling, U.; Maya, J.D.; Robello, C.
Old yellow enzyme from Trypanosoma cruzi exhibits in vivo prostaglandin F2alpha synthase activity and has a key role in parasite infection and drug susceptibility
Front. Immunol.
9
456
2018
Trypanosoma cruzi (V5BT91), Trypanosoma cruzi Dm28c (V5BT91)
brenda
Alves-Ferreira, E.V.C.; Ferreira, T.R.; Walrad, P.; Kaye, P.M.; Cruz, A.K.
Leishmania braziliensis prostaglandin F2alpha synthase impacts host infection
Parasit. Vectors
13
009
2020
Leishmania braziliensis (A0A3P3ZE14), Leishmania braziliensis, Leishmania braziliensis MHOM/BR/75/M2904 (A0A3P3ZE14)
brenda
Garcia-Huertas, P.; Mejia-Jaramillo, A.M.; Machado, C.R.; Guimaraes, A.C.; Triana-Chavez, O.
Prostaglandin F2alpha synthase in Trypanosoma cruzi plays critical roles in oxidative stress and susceptibility to benznidazole
R. Soc. Open Sci.
4
170773
2017
Trypanosoma cruzi (Q4E4V7), Trypanosoma cruzi CL Brener (Q4E4V7)
brenda
Dong, Z.; Zhang, N.; Mao, W.; Liu, B.; Huang, N.; Li, P.; Li, C.; Cao, J.
Kinetic effect of oestrogen on secretion of prostaglandins E2 and F2alpha in bovine oviduct epithelial cells
Reprod. Fertil. Dev.
29
482-489
2017
Bos taurus
brenda
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