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1.1.1.188: prostaglandin-F synthase

This is an abbreviated version!
For detailed information about prostaglandin-F synthase, go to the full flat file.

Word Map on EC 1.1.1.188

Reaction

(5Z,13E)-(15S)-9alpha,11alpha,15-trihydroxyprosta-5,13-dienoate
+
NADP+
=
(5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
 +
NADPH
 +
H+

Synonyms

17beta-hydroxysteroid dehydrogenase type 5, 17betaHSD5, 20alpha-HSD/PGFS, 20alpha-hydroxysteroid dehydrogenase/prostaglandin F-synthase, 9,11-endoperoxidase reductase, AKR1B1, AKR1B3, AKR1B7, AKR1C3, Akr1cl, aldo-keto reductase, aldo-keto reductase 1C3, aldo-ketoreductase 1B1, ALDR1, ALR2, DD1, dihydrodiol dehydrogenase 1, LBRM2904_31.2170, LemaA.00019.a.B1, m-PGFS, More, NADPH-dependent prostaglandin D2 11-keto reductase, P100/11E, PG endoperoxide reductase, PGD 11-ketoreductase, PGD2 11-ketoreductase, PGF, PGF synthase, PGF synthase I, PGF synthase II, PGF2alpha synthase, PGF2alpha-synthase, PGF2alpha-synthetic activity, PGF2S, PGFS, PGFS I, PGFS-I, PGFS-II, PGFSI, PGFSII, PGH 9-,11-endoperoxide reductase, PGH2 9,11-endoperoxidase, PGH2 9,11-endoperoxide reductase, PGH2 9-,11-endoperoxide reductase, prostaglandin 11-keto reductase, prostaglandin 11-ketoreductase, prostaglandin D2 11-ketoreductase, prostaglandin D2-ketoreductase, prostaglandin F synthase, prostaglandin F synthase I, prostaglandin F synthase II, prostaglandin F synthetase, prostaglandin F2alpha synthase, prostaglandin F2alpha-synthase, prostaglandin-D2 11-reductase, prostaglandin-F2alpha synthase, 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, type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase, vas deferens protein

ECTree

     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

Crystallization

Crystallization on EC 1.1.1.188 - prostaglandin-F synthase

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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
AKR1C3 in complex with NADP+ and indomethacin
homology modeling of enzyme in complex with inhibitor indomethacin
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