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Information on EC 1.1.1.148 - estradiol 17alpha-dehydrogenase
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EC Tree
1.1.1.148 estradiol 17alpha-dehydrogenaseSpecify your search results
Word Map
- 1.1.1.148
- testosterone
- epitestosterone
-
aldo-keto
- 3alpha-hsd
-
steroid-binding
- dehydrogenases
-
delta4
-
particularities
-
1.1.1.62
- nadp+
- deae-cellulose
- 3-glucuronide
-
nadph-enzyme
- oestrogen
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
17alpha-estradiol dehydrogenase, 17alpha-HSD, 17alpha-hydroxy steroid dehydrogenase, 17alpha-hydroxy steroid oxidoreductase, 17alpha-hydroxysteroid dehydrogenase, 17alpha-hydroxysteroid oxidoreductase, estradiol 17alpha-oxidoreductase, More, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
17alpha-estradiol dehydrogenase
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17alpha-hydroxy steroid dehydrogenase
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-
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17alpha-hydroxy steroid oxidoreductase
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17alpha-hydroxysteroid dehydrogenase
17alpha-hydroxysteroid oxidoreductase
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-
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estradiol 17alpha-oxidoreductase
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additional information
additional information
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N-terminal sequence comparison of several enzymes: 17alpha-hydroxysteroid dehydrogenase belongs to the disulfide oxidoreductase family, subfamily dihydrolipoamide dehydrogenases
additional information
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N-terminal sequence comparison of several enzymes: 17alpha-hydroxysteroid dehydrogenase belongs to the disulfide oxidoreductase family, subfamily dihydrolipoamide dehydrogenases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
estradiol-17alpha + NAD(P)+ = estrone + NAD(P)H + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
17alpha-hydroxysteroid:NAD(P)+ 17-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
9044-91-1
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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
17beta-hydroxy-4-androsten-3-one + NADP+
4-androsten-3,17-dione + NADPH
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testosterone
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-
?
5alpha-androstan-3beta,17alpha-diol + NADP+
3beta-hydroxy-5alpha-androstan-17-one + NADPH
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-
-
-
?
5alpha-dihydrotestosterone + NADPH
5alpha-androstane-3alpha,17alpha-diol + NADP+
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-
-
?
5alpha-pregnane-3,20-dione + NADPH + H+
3alpha,5alpha-3-hydroxypregnan-20-one + NADP+
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-
-
?
androstanedione + NADPH
5alpha-androstane-3-one-17alpha-ol + NADP+
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-
-
?
androsterone + NADPH
5alpha-androstane-3alpha,17alpha-diol + NADP+
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?
dehydroepiandrosterone + NADPH
5-androstene-3alpha,17alpha-diol + NADP+
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-
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?
estradiol-17alpha 3-galacturonide + NADP+
estrone 3-galacturonide + NADPH
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?
estradiol-17alpha 3-glucoside + NADP+
estrone 3-glucoside + NADPH
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-
-
-
?
17alpha-hydroxy-4-androsten-3-one + NADP+
4-androsten-3,17-dione + NADPH
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epitestosterone
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-
r
17alpha-hydroxy-4-androsten-3-one + NADP+
4-androsten-3,17-dione + NADPH
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epitestosterone
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-
r
17alpha-hydroxy-4-androsten-3-one + NADP+
4-androsten-3,17-dione + NADPH
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epitestosterone
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r
17alpha-hydroxy-4-androsten-3-one + NADP+
4-androsten-3,17-dione + NADPH
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epitestosterone
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r
estradiol-17alpha 3-glucuronide + NADP+
estrone 3-glucuronide + NADPH
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?
estradiol-17alpha 3-glucuronide + NADP+
estrone 3-glucuronide + NADPH
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isoform IC is more specific for this substrate than for 17alpha-estradiol
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?
additional information
?
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the enzyme is involved in the biosynthesis of epitestosterone, the 17alpha-epimer of testosterone
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?
additional information
?
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the enzyme is involved in the biosynthesis of epitestosterone, the 17alpha-epimer of testosterone
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?
additional information
?
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substrate specificity of the recombinant enzyme, overview
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?
additional information
?
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substrate specificity of the recombinant enzyme, overview
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-
?
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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
additional information
?
-
the enzyme is involved in the biosynthesis of epitestosterone, the 17alpha-epimer of testosterone
-
-
?
additional information
?
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the enzyme is involved in the biosynthesis of epitestosterone, the 17alpha-epimer of testosterone
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Epitestosterone
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substrate inhibition for all isoforms at concentration above 0.003 mM, not observed with other substrates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.003 - 0.009
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isoform IA, IB, IID, III, 17alpha-estradiol 3-glucuronide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9 - 9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
inducible by growth on androstenedione and cholic acid, not deoxycholic acid
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
enzyme tissue distribution in male and female mice, overview
brenda
additional information
-
enzyme tissue distribution in male and female mice, overview
brenda
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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). AK1CL_MOUSE
323
0
36877
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
8 forms, six of them purified to homogenity: IA, IB, IC, IIC, IID, III
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recombinant GST-fusion enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloning, subcloning in Escherichia coli, expression as GST-fusion protein in Escherichia coli strain BL21(DE3), stable expression in HEK-293 cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
LaRhee, L.H.; Warren, J.C.
Purification and characterization of epimeric estradiol dehydrogenases (17alpha and 17beta) from equine placenta
Biochemistry
23
486-491
1984
Equus caballus
brenda
Johnston, J.; Renwick, A.G.C.
Oestradiol-17alpha dehydrogenase from chicken liver
Biochem. J.
222
761-768
1984
Gallus gallus
brenda
Hasnain, S.; Williamson, D.G.
Properties of the multiple forms of the soluble 17alpha-hydroxy steroid dehydrogenase of rabbit liver
Biochem. J.
161
279-283
1977
Oryctolagus cuniculus
brenda
Hasnain, S.; Williamson, D.G.
Purification of multiple forms of the soluble 17alpha-hydroxy steroid dehydrogenase or rabbit liver
Biochem. J.
147
457-461
1975
Oryctolagus cuniculus
brenda
Renwick, A.G.C.; Engel, L.L.
The partial purification of 17alpha- and 17beta-estradiol dehydrogenase activities from chicken liver
Biochim. Biophys. Acta
146
336-348
1967
Gallus gallus
brenda
Hasnain, S.; Williamson, D.G.
The separation and partial purification of the soluble 17alpha- and 17beta-hydroxysteroid dehydrogenases of rabbit liver
Can. J. Biochem.
52
120-125
1974
Oryctolagus cuniculus
brenda
De Prada, P.; Setchell, K.D.R.; Hylemon, P.B.
Purification and characterization of a novel 17alpha-hydroxysteroid dehydrogenase from an intestinal Eubacterium sp. VPI 12708
J. Lipid Res.
35
922-929
1994
Eubacterium sp., Eubacterium sp. VPI 12708
brenda
Bellemare, V.; Faucher, F.; Breton, R.; Luu-The, V.
Characterization of 17alpha-hydroxysteroid dehydrogenase activity (17alpha-HSD) and its involvement in the biosynthesis of epitestosterone
BMC Biochem.
6
12
2005
Mus musculus (Q91WR5), Mus musculus
brenda
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