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Information on EC 1.1.1.141 - 15-hydroxyprostaglandin dehydrogenase (NAD+) and Organism(s) Rattus norvegicus
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1.1.1.141 15-hydroxyprostaglandin dehydrogenase (NAD+)IUBMB Comments
Acts on prostaglandin E2, F2alpha and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
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Word Map
- 1.1.1.141
- cox-2
- cyclooxygenase-2
- fetal
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arachidonic
- pregnancy
- chorion
- labor
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pgf2alpha
- indomethacin
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parturition
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nsaid
- trophoblast
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preterm
- myometrium
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chemoprevention
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15-keto
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eicosanoids
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thromboxane
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prostanoids
- decidua
- synthase-1
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nadp-linked
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15-keto-pge2
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clubbing
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cesarean
- osteoarthropathy
- prostacyclin
- amnion
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beta-hydroxysteroid
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lipoxins
- calcitriol
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9-ketoreductase
- medicine
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slco2a1
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6-keto-pgf1
- drug development
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
15-pgdh, 15-hydroxyprostaglandin dehydrogenase, prostaglandin dehydrogenase, 15-prostaglandin dehydrogenase, 15-hydroxy prostaglandin dehydrogenase, nad+-dependent 15-hydroxyprostaglandin dehydrogenase, 15-oh-pgdh, nad-dependent 15-hydroxyprostaglandin dehydrogenase, 15-hydroxyprostaglandin-dehydrogenase, 15-hydroxy-prostaglandin-dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
11alpha,15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase
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15-hydroxyprostanoic dehydrogenase
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15-OH-PGDH
dehydrogenase, 15-hydroxyprostaglandin
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NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (type I)
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NAD-specific 15-hydroxyprostaglandin dehydrogenase
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PGDH
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prostaglandin dehydrogenase
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15-OH-PGDH
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate:NAD+ 15-oxidoreductase
Acts on prostaglandin E2, F2alpha and B1, but not on prostaglandin D2. cf. EC 1.1.1.196 15-hydroxyprostaglandin-D dehydrogenase (NADP+) and EC 1.1.1.197 15-hydroxyprostaglandin dehydrogenase (NADP+).
CAS REGISTRY NUMBER
COMMENTARY
9030-87-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
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?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
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first step in prostaglandin catabolism
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-
?
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
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i.e. 15-hydroxyprostaglandin or (15S)-PGE2
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
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first step in prostaglandin catabolism
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-
?
(5Z,13E,15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate + NAD+
(5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-5,13-dienoate + NADH + H+
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-[[4-(ethoxycarbonyl)phenyl]azo]2-hydroxy-benzene acetic acid
CAY-10397
papaverine
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the inhibition is noncompetitive with prostaglandin E2, uncompetitive with NAD+, and reversible
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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both 15-hydroxyprostaglandin dehydrogenase mRNA and protein levels are significantly higher in kidney cortex than in papilla. Enzyme is mainly localized to the tubular epithelial cells in kidney cortex and outer medulla
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macula densa cell line, significantly lower enzyme levels than in a proximal tubule cell line. Treatment with an inhibitor of cyclooxygenase-2 increases enzyme level
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enzyme is mainly localized to the tubular epithelial cells in kidney cortex and outer medulla
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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the enzyme regulates postnatal kidney development through interaction with cyclooxygenase 2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PGDH_RAT
266
0
28939
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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expression in nontumorigenic IEC-18 cells, with and without K-RasV12 and analysis of the ability of cells to form tumors in nu/nu mice. Transformed cells show increased 15-hydroxyprostaglandin dehydrogenase activity with decreased prostaglandin E2 and prostaglandin I2 levels, cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression and proliferation rates. Xenografts of cells expressing both the enzyme and K-RasV12 exhibit delayed tumor formation with negligible cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression and significantly decreased prostaglandin E2 levels. Tumors have decreased staining of the proliferative marker, Ki-67, and a significant increase in apoptosis in the central region of the tumor
additional information
expression in nontumorigenic IEC-18 cells, with and without K-RasV12 and analysis of the ability of cells to form tumors in nu/nu mice. Transformed cells show increased 15-hydroxyprostaglandin dehydrogenase activity with decreased prostaglandin E2 and prostaglandin I2 levels, cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression and proliferation rates. Xenografts of cells expressing both the enzyme and K-RasV12 exhibit delayed tumor formation with negligible cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression and significantly decreased prostaglandin E2 levels. Tumors have decreased staining of the proliferative marker, Ki-67, and a significant increase in apoptosis in the central region of the tumor
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
expression in nontumorigenic IEC-18 cells, with and without K-RasV12 and analysis of the ability of cells to form tumors in nu/nu mice. Transformed cells show increased 15-hydroxyprostaglandin dehydrogenase activity with decreased prostaglandin E2 and prostaglandin I2 levels, cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression and proliferation rates. Xenografts of cells expressing both the enzyme and K-RasV12 exhibit delayed tumor formation with negligible cyclooxygenase-2 and microsomal prostaglandin E synthase-1 expression and significantly decreased prostaglandin E2 levels. Tumors have decreased staining of the proliferative marker, Ki-67, and a significant increase in apoptosis in the central region of the tumor
medicine
PGDH expression suppresses K-RasV12-mediated tumorigenesis in intestinal epithelial cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iijima, Y.; Ueno, T.; Sasagawa, K.; Yamazaki, M.
Inhibition of 15-hydroxyprostaglandin dehydrogenase by papaverine
Biochem. Biophys. Res. Commun.
80
484-489
1978
Canis lupus familiaris, Cavia porcellus, Gallus gallus, Rattus norvegicus, Sus scrofa
Okita, R.T.; Okita, J.R.
Prostaglandin-metabolizing enzymes during pregnancy: characterization of NAD+-dependent prostaglandin dehydrogenase, carbonyl reductase, and cytochrome P450-dependent prostaglandin omega-hydroxylase
CRC Crit. Rev. Biochem.
31
101-126
1996
Bos taurus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus, Sus scrofa
Yao, B.; Xu, J.; Harris, R.C.; Zhang, M.Z.
Renal localization and regulation of 15-hydroxyprostaglandin dehydrogenase
Am. J. Physiol. Renal Physiol.
294
F433-F439
2008
Mus musculus, Rattus norvegicus
Pham, H.; Eibl, G.; Vincenti, R.; Chong, B.; Tai, H.H.; Slice, L.W.
15-Hydroxyprostaglandin dehydrogenase suppresses K-RasV12-dependent tumor formation in Nu/Nu mice
Mol. Carcinog.
47
466-477
2008
Rattus norvegicus, Rattus norvegicus (O08699)
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Release 2023.1 (January 2023)
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