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Information on EC 1.1.1.231 - 15-hydroxyprostaglandin-I dehydrogenase (NADP+) for references in articles please use BRENDA:EC1.1.1.231
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
dehydrogenase, prostacyclin, NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase, NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase, PG I2 dehydrogenase, prostacyclin dehydrogenase,
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dehydrogenase, prostacyclin
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NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase
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NADP-linked 15-hydroxyprostaglandin (prostacyclin) dehydrogenase
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PG I2 dehydrogenase
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prostacyclin dehydrogenase
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H+
(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H+
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH + H+
random mechanism or ordered mechanism with NADP+ binding first
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate:NADP+ 15-oxidoreductase
Specific for prostaglandin I2.
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH
4-benzoylpyridine + NADP+
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recombinant forms CHCR1, CHCR2
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4-nitrobenzaldehyde + NADP+
4-nitrobenzoate + NADPH
6-keto-prostaglandin F1alpha + NADP+
6,15-diketoprostaglandin F2alpha + NADPH
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at 1.8% the reaction rate of prostaglandin I2
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menadione + NADP+
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more rapid reaction than with prostacyclin
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phenanthrene quinone + NADP+
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more rapid reaction than with prostacyclin
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prostaglandin B1 + NADP+
15-ketoprostaglandin B1 + NADPH + H+
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at 8% the reaction rate of prostaglandin I2
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prostaglandin E2 + NADP+
15-ketoprostaglandin E2 + NADPH + H+
prostaglandin F2alpha + NAD+
15-ketoprostaglandin F2alpha + NADH + H+
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prostaglandin F2alpha + NADP+
15-ketoprostaglandin F2alpha + NADPH + H+
pyridine-4-carboxaldehyde + NADP+
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recombinant forms CHCR1, CHCR2
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additional information
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH
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i.e. prostaglandin I2, prostacyclin
the product is not stable and not available for analysis of the reverse reaction
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH
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i.e. prostaglandin I2, prostacyclin
i.e. 15-keto prostaglandin I2
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4-nitrobenzaldehyde + NADP+
4-nitrobenzoate + NADPH
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recombinant forms CHCR1, CHCR2
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4-nitrobenzaldehyde + NADP+
4-nitrobenzoate + NADPH
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more rapid reaction than with prostacyclin
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prostaglandin E2 + NADP+
15-ketoprostaglandin E2 + NADPH + H+
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prostaglandin E2 + NADP+
15-ketoprostaglandin E2 + NADPH + H+
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at 4% the reaction rate of prostaglandin I2
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prostaglandin F2alpha + NADP+
15-ketoprostaglandin F2alpha + NADPH + H+
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prostaglandin F2alpha + NADP+
15-ketoprostaglandin F2alpha + NADPH + H+
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at 2.2% the reaction rate of prostaglandin I2
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additional information
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comparison of 3 15-hydroxyproastaglandin dehydrogenases with varying amounts of 9-ketoprostaglandin reductase activity
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additional information
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enzyme catalyzes reduction of 9-keto group in prostaglandin E2 at less than 1% the rate of prostaglandin I2 oxidation
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(5Z,13E)-(15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate + NADP+
(5Z,13E)-6,9alpha-epoxy-11alpha-hydroxy-15-oxoprosta-5,13-dienoate + NADPH
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additional information
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no activity with NAD+
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additional information
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not a flavoprotein
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0.0667
4-nitrobenzaldehyde
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0.0005
Phenanthrene quinone
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0.278 - 0.364
prostaglandin I2
0.00538
NADP+
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0.278
prostaglandin I2
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0.364
prostaglandin I2
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1.217
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recombinant enzyme, latanoprost + NADP+
2.17
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recombinant enzyme, acid form of latanoprost + NADP+
24.3
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recombinant enzyme, prostaglandin F2alpha + NADP+
6.08
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recombinant enzyme, prostaglandin F2alpha + NAD+
9.8
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recombinant enzyme, prostaglandin E2 + NADP+
additional information
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chinese hamster
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brenda
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brenda
monkey
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brenda
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brenda
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brenda
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brenda
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brenda
additional information
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tissue distribution of m-RNA
brenda
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28000
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2 * 28000, rabbit, SDS-PAGE
31000
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SDs-PAGE of recombinant enzyme
34000
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SDS-PAGE of recombinant forms CHCR1, CHCR2 including His-tag
56000
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SDS-PAGE of amidinated enzyme
additional information
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relationship to NAD+-dependent 15-hydroxyprostaglandin dehydrogenase; three-dimensional model
additional information
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three-dimensional model
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dimer
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computer modelling
dimer
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2 * 28000, rabbit, SDS-PAGE
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freezing and thawing: repeatedly, slow loss of activity
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stable for months when frozen
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2 forms differing due to posttranslational modification at pos. 238
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2 enzyme forms CHCR1, CHCR2
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Krook, M.; Ghosh, D.; Duax, W.; Jörnvall, H.
Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase)
FEBS Lett.
322
139-142
1993
Homo sapiens
brenda
Korff, J.M.; Jarabak, J.
Isolation and properties of an NADP+-dependent PGI2-specific 15-hydroxyprostaglandin dehydrogenase from rabbit kidney
Methods Enzymol.
86
152-155
1982
Oryctolagus cuniculus
brenda
Korff, J.M.; Jarabak, J.
The purification and characterization of a prostacyclin dehydrogenase from rabbit kidney
J. Biol. Chem.
257
2177-2181
1982
Oryctolagus cuniculus
brenda
Fujimori, K.; Okada, T.; Urade, Y.
Expression of NADP(+)-Dependent 15-Hydroxyprostaglandin Dehydrogenase mRNA in Monkey Ocular Tissues and Characterization of Its Recombinant Enzyme
J. Biochem.
131
383-389
2002
Macaca fascicularis
brenda
Terada, T.; Sugihara, Y.; Nakamura, K.; Sato, R.; Sakuma, S.; Fujimoto, Y.; Fujita, T.; Inazu, N.; Maeda, M.
Characterization of multiple Chinese hamster carbonyl reductases
Chem. Biol. Interact.
130-132
847-861
2001
Cricetulus griseus
brenda
Jarabak, J.; Luncsford, A.; Berkowitz, D.
Substrate specificity of three prostaglandin dehydrogenases
Prostaglandins
26
849-868
1983
Homo sapiens
brenda
Krook, M.; Ghosh, D.; Stromberg, R.; Carlquist, M.; Jornvall, H.
Carboxyethyllysine in a protein: Native carbonyl reductase/NADP+-dependent prostaglandin dehydrogenase
Proc. Natl. Acad. Sci. USA
90
502-506
1993
Homo sapiens
brenda
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1.1.1.231 15-hydroxyprostaglandin-I dehydrogenase (NADP+)
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