1.1.1.239: 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.239
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1.1.1.239
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androgen
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estradiol
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steroidogenic
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akr1c3
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androstenedione
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prostate
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3beta-hsd
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3beta-hydroxysteroid
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estrone
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aromatase
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steroidogenesis
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5alpha-reductase
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dehydroepiandrosterone
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leydig
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3alpha-hsds
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3alpha-hydroxysteroid
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p450scc
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5alpha-dihydrotestosterone
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cochliobolus
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4-dione
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androsterone
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lunatus
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delta5-3beta-hsd
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intracrine
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coumestrol
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5alpha-dht
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pseudohermaphroditism
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p450arom
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4-androstene-3,17-dione
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medicine
- 1.1.1.239
- androgen
- estradiol
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steroidogenic
- akr1c3
- androstenedione
- prostate
- 3beta-hsd
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3beta-hydroxysteroid
- estrone
- aromatase
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steroidogenesis
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5alpha-reductase
- dehydroepiandrosterone
- leydig
- 3alpha-hsds
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3alpha-hydroxysteroid
- p450scc
- 5alpha-dihydrotestosterone
-
cochliobolus
-
4-dione
- androsterone
- lunatus
- delta5-3beta-hsd
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intracrine
- coumestrol
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5alpha-dht
- pseudohermaphroditism
- p450arom
- 4-androstene-3,17-dione
- medicine
Reaction
Synonyms
17-ketoreductase, 17beta-HSD, 17beta-hydroxysteroid dehydrogenase type 5, 3,17beta-HSD, 3,17beta-hydroxysteroid dehydrogenase, 3alpha(17beta)-HSD, 3alpha(17beta)-hydroxysteroid dehydrogenase, AKR1C26, AKR1C27, AKR1C28, AKR1C3, AKR1C34, aldo-keto reductase 1C3, dehydrogenase, 3alpha,17beta-hydroxy steroid, EC 1.1.1.63, More, NAD+-dependent 3alpha(17beta)-hydroxysteroid dehydrogenase, NAD+-dependent 3beta(17beta)-hydroxysteroid dehydrogenase, NAD+-linked S-tetralol dehydrogenase, PGER6, type 2 3alpha-HSD, type 2 3alpha-hxdroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 2 3alppha-hydroxysteroid dehydrogenase/type 5 17beta-hydroxysteroid dehydrogenase, type 3 17beta-hydroxysteroid dehydrogenase, type 5 17beta-HSD, type 5 17beta-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase, type 5 beta-hydroxysteroid dehydrogenase
ECTree
1.1.1.239 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)Advanced search results
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results (General Information
General Information on EC 1.1.1.239 - 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
mutation of Tyr118 and Phe310 in AKR1C27 to the corresponding residues (Phe and Ile, respectively) in AKR1C28 produces an enzyme that is similar to AKR1C28
physiological function
additional information
evolution
enzyme AKR1C34 is a member of the aldoketo reductase (AKR) 1C subfamily in the AKR superfamily
evolution
the enzyme is a member of the aldo-keto reductase (AKR) superfamily that metabolizes endogenous substrates, such as carbohydrates, prostaglandins and steroids, and xenobiotics in a NAD(P)(H)-dependent manner
evolution
the enzyme is a member of the aldoketo reductase (AKR) 1C subfamily in the AKR superfamily
physiological function
exposure of HCT-15 cells to cisplatin results in aquisition of cisplatin resistance and concomitant induction of isoform AKR1C3 and aldo-keto reductase AKR1C1 expression. The resistance lowers the sensitivity toward cellular damages evoked by oxidative stress-derived aldehydes, 4-hydroxy-2-nonenal and 4-oxo-2-nonenal that are detoxified by AKR1C1 and AKR1C3. Overexpression of AKR1C1 or AKR1C3 in the parental HCT15 cells mitigates the cytotoxicity of the aldehydes and cisplatin. Knockdown of both AKR1C1 and AKR1C3 in the resistant cells or treatment of the cells with specific inhibitors of the aldo-keto reductases increases the sensitivity to ciplatin toxicity
physiological function
in LNCaP and LNCaP-AKR1C3 cells overexpressing isoform AKR1C3, metabolism proceeds via 5alpha-reduction to form 5alpha-androstane-3,17-dione and then (epi)androsterone-3-glucuronide. LNCaP-AKR1C3 cells make significantly higher amounts of testosterone-17beta-glucuronide. When 5alpha-reductase is inhibited by finasteride, the production of testosterone-17beta-glucuronide is further elevated in LNCaP-AKR1C3 cells. When AKR1C3 activity is inhibited with indomethacin the production of testosterone-17beta-glucuronide is significantly decreased. 4-Androstene-3,17-dione treatment stimulates cell proliferation in both cell lines. LNCaP-AKR1C3 cells are resistant to the growth inhibitory properties of finasteride, consistent with the diversion of 4-androstene-3,17-dione metabolism from 5alpha-reduced androgens to increased formation of testosterone
physiological function
AKR1C3 catalyzes the conversion of the weak androgen precursors 4-androstene-3,17-dione and 5alpha-androstane-3,17-dione to the potent androgens testosterone and 5alpha-dihydrotestosterone (DHT), respectively, and is one of the most highly upregulated genes in castrate-resistant prostate cancer, CRPC
physiological function
aldo-keto reductase 1C3 (AKR1C3), also known as type 5 17beta-hydroxysteroid dehydrogenase, is a downstream steroidogenic enzyme and converts androgen precursors to the potent androgen receptor ligands testosterone and 5alpha-dihydrotestosterone. AKR1C3 is involved in the development of castration resistant prostate cancer (CRPC)
physiological function
crucial role of AKR1C3 in the acquisition of daunorubicin resistance of leukemic cells by metabolizing both daunorubicin and cytotoxic aldehydes derived from ROS-linked lipid peroxidation. Daunorubicin, at its sublethal doses, induces the expression of AKR1C1, EC 1.1.1.149, and AKR1C3, both of which reduce the daunorubicin sensitivity of the cells, AKR1C3 is more inducible than AKR1C1 by the daunorubicin treatment
physiological function
enzyme AKR1C34 oxidizes various xenobiotic alicyclic alcohols using NAD+
physiological function
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key enzyme involved in the degradation of steroid compounds
physiological function
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key enzyme involved in the degradation of steroid compounds
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additional information
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
J7M9D0
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
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Homology structure modeling of AKR1C28 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
structure analysis by homology modelling, overview
additional information
J7M9D0
structure analysis by homology modelling, overview
additional information
structure analysis by homology modelling, overview
additional information
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structure analysis by homology modelling, overview
additional information
the structure of the AKR1C3-NADP+ complex is solved by molecular replacement, overview
additional information
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
J7M9D0
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
additional information
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Tyr118 and Phe310 play key roles in ligand binding. Homology structure modeling of AKR1C27 on the basis of sequence alignment and crystal structure analysis of the AKR1C5 ternary complex, PDB ID 1Q13, overview
