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Information on EC 1.1.1.270 - 3beta-hydroxysteroid 3-dehydrogenase and Organism(s) Homo sapiens and UniProt Accession Q04828
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1.1.1.270 3beta-hydroxysteroid 3-dehydrogenaseIUBMB Comments
The enzyme acts on multiple 3beta-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17beta-estradiol 17-dehydrogenase .
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Word Map
- 1.1.1.270
-
steroidogenic
- testosterone
- androgen
- progesterone
-
steroidogenesis
- adrenal
- leydig
- star
- cyp11a1
- testicular
- p450scc
- aromatase
- lutein
- lh
- pregnenolone
- androstenedione
- dehydroepiandrosterone
- akr1c1
-
granulosa
- trilostane
- 17alpha-hydroxylase
- 3betahsd
- hsd3b2
- dheas
- dihydrotestosterone
-
lhcgr
- srd5a1
- p450arom
-
5alpha-reductase
- 21-hydroxylase
- 3-ketosteroids
-
scarb1
- hsd11b1
-
22r-hydroxycholesterol
- 5alpha-dihydrotestosterone
-
neurosteroids
-
20alpha-hydroxysteroid
-
11beta-hydroxylase
- cyp21
- 3alpha-hsds
- insl3
-
intratesticular
-
lh-stimulated
-
adrenarche
- 17-hydroxypregnenolone
- medicine
- 17alpha-hydroxyprogesterone
-
delta5
-
pre-receptor
- synthesis
- analysis
- 20alpha-hsd
- 17alpha-hydroxylase/17,20-lyase
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
3beta-hydroxysteroid dehydrogenase, hsd3b1, akr1c2, hsd17b7, erg27, 3beta-hsd1, 3-ketosteroid reductase, 3beta-hsd2, 3-ketoreductase, erg27p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-keto reducing enzyme
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-
-
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3-keto reductase
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-
-
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3-ketoreductase
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-
-
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3-ketosteroid reductase
3-KSR
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-
-
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3-oxo steroid reductase
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-
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3-oxosteroid reductase
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-
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3beta-HSD1
3beta-hydroxysteroid dehydrogenase type 1
HSD17B7
reductase, 3-oxo steroid
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-
-
-
steroid-3-ketoreductase
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-
-
-
sterone-reducing enzyme
-
-
-
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3-ketosteroid reductase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH + H+
residues Leu/Val54, Tyr55, His117, Val128, Ile129, His222, and Trp227 are involved in substrate binding, Tyr55, Asp50, Lys84, and His117 form the catalytic tetrad, Tyr55 and His117 together with NADP+ form an oxyanion hole through hydrogen bond networks, molecular docking simulations, detailed overview
a 3beta-hydroxysteroid + NADP+ = a 3-oxosteroid + NADPH + H+
stereoselectivity : #1,4,5# catalyzes reduction of the 3-keto group to a 3beta-hydroxyl group <5,6,7>
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
3beta-hydroxysteroid:NADP+ 3-oxidoreductase
The enzyme acts on multiple 3beta-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17beta-estradiol 17-dehydrogenase [4].
CAS REGISTRY NUMBER
COMMENTARY
42616-29-5
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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
2 17beta-hydroxy-5alpha-androstan-3-one + 2 NADPH + 2 H+
5alpha-androstane-3beta,17beta-diol + 5alpha-androstane-3alpha,17beta-diol + 2 NADP+
3alpha-androstanediol + NAD+
? + NADH
AKR1C2 and AKR1C4 act as 3alpha-hydroxysteroid oxidase, AKR1C3 predominantly acts as 17beta-hydroxysteroid oxidase catalyzing the conversion of 3alpha-diol to androsterone, negligible activity with the 3beta-androstanediol
-
-
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
i.e. DHT, reductive 3alpha-HSD activity of AKR1C1 yielding the 3alpha,17-diol, low activity
-
-
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3beta,17beta-diol + NADP+
i.e. DHT, reductive 3beta-HSD activity of AKR1C1 yielding the 3beta,17-diol, preferred reaction
-
-
?
progesterone + NADPH
pregn-4-ene-20alpha-ol-3-one + NADP+
i.e. pregn-4-ene-3,20-dione
-
-
?
[7alpha,17alpha]-17-hydroxy-7-methyl-19-norpregn-5(10)-en-20-yn-3-one + NADPH
[7alpha,17alpha]-17-hydroxy-7-methyl-19-norpregn-5(10)-en-20-yn-3-ol + NADP+
i.e. tibolone, a synthetic hormone
-
-
?
17alpha-hydroxypregnenolone + NADH + H+
17alpha-hydroxyprogesterone + NAD+
-
-
-
-
?
[7alpha,17alpha]-17-hydroxy-7-methyl-19-norpregn-5(10)-en-20-yn-3-one + NADPH
[7alpha,17alpha]-17-hydroxy-7-methyl-19-norpregn-5(10)-en-20-yn-3-ol + NADP+
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i.e. tibolone, a synthetic hormone
reaction product determination and analysis
-
?
2 17beta-hydroxy-5alpha-androstan-3-one + 2 NADPH + 2 H+
5alpha-androstane-3beta,17beta-diol + 5alpha-androstane-3alpha,17beta-diol + 2 NADP+
-
the rates of 3alpha-diol versus 3beta-diol formation varies significantly among the isoforms. AKR1C1 predominantly catalyzes the formation of 3beta-diol, whereas AKR1C2 and AKR1C4 predominantly catalyze the formation of 3alpha-diol. AKR1C3 shows relatively low reductive activity towards 17beta-hydroxy-5alpha-androstan-3-one, in which 3alpha-diol and 3beta-diol is formed in almost equal amounts
-
?
2 17beta-hydroxy-5alpha-androstan-3-one + 2 NADPH + 2 H+
5alpha-androstane-3beta,17beta-diol + 5alpha-androstane-3alpha,17beta-diol + 2 NADP+
AKR1cs are a source of beta-tetrahydrosteroids. This is of physiological significance because the formation of 3beta-diol in contrast to 3alpha-diol is virtually irreversible, the 3beta-diol is a pro-apoptotic ligand for estrogen receptor beta, and 3beta-tetrahydrosteroids act as gamma-aminobutyric acid type A receptor antagonists
-
-
?
(4-methyl)zymosterone + NADPH + H+
(4-methyl)zymosterol + NADP+
cholesterol pathway
-
-
?
5alpha-androstane-3,17-dione + NADPH
epi-androsterone + NADP+
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3-ketosteroid reductase activity of the human 3(alpha-beta)-hydroxysteroid epimerase, stereoselective reduction
epi-ADT
?
5alpha-androstane-3,17-dione + NADPH
epi-androsterone + NADP+
-
5alpha-dione
epi-ADT
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
-
-
-
-
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
-
in prostate cells AKR1C2 acts as a 3-ketosteroid reductase to eliminate 5alpha-dihydrotestosterone and prevents activation of androgen receptor. AKR1C2 does not act as an oxidase due to either potent product inhibition by NADPH or because it cannot surmount the oxidative 17beta-hydroxysteroid dehydrogenase present. AKR1C2 is not a source of 5alpha-dihydrotestosterone in PC-3 cells
-
-
?
dihydrotestosterone + NADPH + H+
5alpha-androstane-3beta,17beta-diol + NADP+
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-
-
?
dihydrotestosterone + NADPH + H+
5alpha-androstane-3beta,17beta-diol + NADP+
steroid hormone pathway
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-
?
progesterone + NADPH + H+
4-pregnen-3beta-ol-20-one + NADP+
steroid hormone pathway
-
-
?
additional information
?
-
AKR1C1 is a cytosolic hydroxysteroid dehydrogenase, that reduces 3-ketosteroids and 20-ketosteroids, overview, molecular docking simulations with generation of docking targets, overview
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-
?
additional information
?
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-
AKR1C1 is a cytosolic hydroxysteroid dehydrogenase, that reduces 3-ketosteroids and 20-ketosteroids, overview, molecular docking simulations with generation of docking targets, overview
-
-
?
additional information
?
-
-
3-ketosteroid reductase activity of the human 3(alpha-beta)-hydroxysteroid epimerase catalyzes reduction of 3-ketosteroids to form 3beta-hydroxysteroids
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-
?
additional information
?
-
-
HSD17B7 participates in postsqualene cholesterol biosynthesis, HSD17B7 is a novel candidate for inborn errors of cholesterol metabolism
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-
?
additional information
?
-
-
tibolone is used to treat climacteric symptoms and prevent osteoporosis, it exerts tissue-selective effects via site-specific metabolism into 3alpha- and 3beta-hydroxymetabolites and a DELTA4-isomer, In Hep-G2 cell cytosol and intact cells tibolone is exclusively reduced to 3beta-hydroxytibolone, tibolone metabolism in human liver is catalyzed by 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily, overview
-
-
?
additional information
?
-
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comparison of substrate specificity and enantioselectivity of AKR1C isozymes, overview
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-
?
additional information
?
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-
both isoforms of the enzyme catalyze the conversion of 3beta-hydroxy-5-ene-steroids (dehydroepiandrosterone, 17alpha-hydroxypregnenolone, pregnenolone) to 3-oxo-4-ene-steroids (androstenedione, 17alpha-hydroxyprogestrone, progesterone) on a single, dimeric protein containing both enzyme activities
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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
2 17beta-hydroxy-5alpha-androstan-3-one + 2 NADPH + 2 H+
5alpha-androstane-3beta,17beta-diol + 5alpha-androstane-3alpha,17beta-diol + 2 NADP+
AKR1cs are a source of beta-tetrahydrosteroids. This is of physiological significance because the formation of 3beta-diol in contrast to 3alpha-diol is virtually irreversible, the 3beta-diol is a pro-apoptotic ligand for estrogen receptor beta, and 3beta-tetrahydrosteroids act as gamma-aminobutyric acid type A receptor antagonists
-
-
?
(4-methyl)zymosterone + NADPH + H+
(4-methyl)zymosterol + NADP+
cholesterol pathway
-
-
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
-
in prostate cells AKR1C2 acts as a 3-ketosteroid reductase to eliminate 5alpha-dihydrotestosterone and prevents activation of androgen receptor. AKR1C2 does not act as an oxidase due to either potent product inhibition by NADPH or because it cannot surmount the oxidative 17beta-hydroxysteroid dehydrogenase present. AKR1C2 is not a source of 5alpha-dihydrotestosterone in PC-3 cells
-
-
?
dihydrotestosterone + NADPH + H+
5alpha-androstane-3beta,17beta-diol + NADP+
steroid hormone pathway
-
-
?
progesterone + NADPH + H+
4-pregnen-3beta-ol-20-one + NADP+
steroid hormone pathway
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-
?
additional information
?
-
-
HSD17B7 participates in postsqualene cholesterol biosynthesis, HSD17B7 is a novel candidate for inborn errors of cholesterol metabolism
-
-
?
additional information
?
-
-
tibolone is used to treat climacteric symptoms and prevent osteoporosis, it exerts tissue-selective effects via site-specific metabolism into 3alpha- and 3beta-hydroxymetabolites and a DELTA4-isomer, In Hep-G2 cell cytosol and intact cells tibolone is exclusively reduced to 3beta-hydroxytibolone, tibolone metabolism in human liver is catalyzed by 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily, overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
potent inhibition of hydroxysteroid oxidase activity by low micromolar concentrations
2,16-dicyano-4,5-epoxy-androstane-3,17-dione
competitively inhibits 3beta-HSD1
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NADPH
-
the NAD+:NADPH ratio in cell will determinewhether AKR1C2 makes 5alpha-dihydrotestosterone
additional information
NADPH-dependent 3-ketosteroid reductase activity is not inhibited by NAD+
-
additional information
-
NADPH-dependent 3-ketosteroid reductase activity is not inhibited by NAD+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0043
17beta-hydroxy-5alpha-androstan-3-one
pH 7.0, 37°C, spectrophotometric analysis, formation of 3beta-androstanediol or 3alpha-androstanediol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
17beta-hydroxy-5alpha-androstan-3-one
pH 7.0, 37°C, radiometric analysis, formation of 3beta-androstanediol
0.0493
17beta-hydroxy-5alpha-androstan-3-one
pH 7.0, 37°C, radiometric analysis, formation of 3alpha-androstanediol
0.052
17beta-hydroxy-5alpha-androstan-3-one
pH 7.0, 37°C, spectrophotometric analysis, formation of 3beta-androstanediol or 3alpha-androstanediol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0047
2,16-dicyano-4,5-epoxy-androstane-3,17-dione
pH 7.4, 27°C, wild-type enzyme
-
0.0295
2,16-dicyano-4,5-epoxy-androstane-3,17-dione
pH 7.4, 27°C, chimeric S194G-1 mutant
-
0.0415
2,16-dicyano-4,5-epoxy-androstane-3,17-dione
pH 7.4, 27°C, chimeric 195P-1 mutant
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0039
with substrate 5alpha-dihydrotestosterone, formation of the 3alpha-hydroxysteroid
0.0161
with substrate 5alpha-dihydrotestosterone, formation of the 3beta-hydroxysteroid
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
HepG2 cells which lack 3-ketohydroxysteroid reductase/DELTA5-4ketosteroid isomerase mRNA expression, but express AKR1C1-AKR1C3 are able to convert 17beta-hydroxy-5alpha-androstan-3-one to 3beta-androstanediol and 3alpha-androstanediol
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primary, time-dependent reduction of tibolone into 3beta- and 3alpha-hydroxytibolone was observed again in a 4:1 ratio
-
in primary cultures of epithelial cells, high levels of AKR1C2 transcripts are detected in prostate cancer, but not in cell from normal prostate. In prostate cells AKR1C2 acts as a 3-ketosteroid reductase to eliminate 5alpha-dihydrotestosterone and prevents activation of androgen receptor
-
in primary cultures of epithelial cells, high levels of AKR1C2 transcripts are detected in prostate cancer, but not in cell from normal prostate
additional information
-
isozymes 3beta-HSD1 and 3beta-HSD2 are encoded by two distinct genes which are expressed in a tissue-specific pattern
17beta-HSD7 is amplified in primary and progressive breast cancer
3beta-HSD1 is selectively expressed in human placenta, mammary glands and breast tumors in women
expression of 3beta-hydroxysteroid dehydrogenase type 1 (HSD3B1) in breast cancer is associated with shorter recurrence-free survival, and genetic or pharmacologic inhibition of HSD3B1 reduced colony formation and xenograft growth
3beta-HSD1 is selectively expressed in human placenta, mammary glands and breast tumors in women
3beta-HSD1 is selectively expressed in human placenta, mammary glands and breast tumors in women
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
3-keto reductase activity in both microsomal fractions and intact cells
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
-
human 3beta-hydroxysteroid dehydrogenase is a member of the short-chain dehydrogenase/reductase (SDR) family of enzymes, all of which contain the Rossmann-fold domain with a beta-alpha-beta-alpha-beta-alpha-beta-alpha-beta folding pattern that binds cofactor and substrate
malfunction
interleukin-6 treatment partially reduces the cytotoxicity augmented by the HSD3B1 knockdown
metabolism
physiological function
drug target
inhibition of 3beta-hydroxysteroid dehydrogenase type 1 suppresses interleukin-6 in breast cancer. The therapeutic potential of targeting HSD3B1 is in part mediated by IL-6 suppression
drug target
selective inhibition of 3beta-HSD1 may prevent spontaneous premature birth. Inhibition of 3beta-HSD1 decreases placental estradiol production that promotes labor. The 3beta-HSD1 inhibitor may be administered with 17alpha-hydroxyprogesterone caproate
metabolism
-
the enzyme catalyzes the first step in the conversion of dehydroepiandrosterone to estradiol
metabolism
expression of 3beta-hydroxysteroid dehydrogenase type 1 (HSD3B1) in breast cancer is associated with shorter recurrence-free survival, and genetic or pharmacologic inhibition of HSD3B1 reduced colony formation and xenograft growth
metabolism
the anti-apoptotic protein GRP78 is a key regulatory protein related to 17beta-HSD7 inhibition and effect
metabolism
the enzyme (17beta-HSD7) promotes breast cancer cell growth via dual-catalytic activity by modulating estradiol and DHT
physiological function
-
the enzyme promotes tumor growth in placenta, mammary glands, and breasts. In human adrenals, 3beta-HSD2 is required for the production of cortisol and aldosterone
physiological function
the enzyme is involved in the metabolism of steroid hormones and in the biosynthesis of cholesterol
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). PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R195P
S194G
trilostane inhibits chimeric S194G-1 mutant (Ki: 0.00067 mM) with a noncompetitive mode compared to its 6.7fold higher affinity, competitive inhibition of 3beta-HSD1. 2,16-Dicyano-4,5-epoxy-androstane-3,17-dione inhibits S194G-1 with a 6.3fold higher Ki (0.0295 mM) than measured for 3beta-HSD1 (Ki: 0.0047 mM) but with the same competitive mode for both enzyme species
additional information
R195P
2,16-dicyano-4,5-epoxy-androstane-3,17-dione competitively inhibits S194G-1
additional information
overexpression of 17beta-hydroxysteroid dehydrogenase type 7 in ERG27-deleted yeast cells. Recombinant strains grow more slowly than the control yeast ERG27-overexpressing strain on sterol-deficient media, whereas the growth rate is normal on media supplemented with a 3-ketoreductase substrate. Mammalian steroid-3-ketoreductase expressed in yeast shows full enzymatic functioanlity but is unable to support the functionality of yeast oxidosqualene cyclase as ERG27 does
additional information
-
overexpression of 17beta-hydroxysteroid dehydrogenase type 7 in ERG27-deleted yeast cells. Recombinant strains grow more slowly than the control yeast ERG27-overexpressing strain on sterol-deficient media, whereas the growth rate is normal on media supplemented with a 3-ketoreductase substrate. Mammalian steroid-3-ketoreductase expressed in yeast shows full enzymatic functioanlity but is unable to support the functionality of yeast oxidosqualene cyclase as ERG27 does
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Sf9 insect cells by ultracentrifugation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
3-ketosteroid reductase activity of the human 3(alpha-beta)-hydroxysteroid epimerase, stable expression
-
expression of HSD17B7 and truncated HSD17B7 (shortened by 127 amino acids at the C terminus) as glutathione-S-transferase fusion protein in Escherichia coli. Erg27p-deficient yeast strain complements the 3-ketosteroid reductase deficiency of the cells and restores growth on sterol-deficient medium
-
expression of wild-type and mutant enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
the cDNA that encodes the mutant 3beta-HSD1 enzymes S194G-1 and R195P-1 are generated via double-stranded, PCR-based mutagenesis and inserted into baculovirus. The recombinant baculovirus system successfully expresses the mutant S194G-1 and R195P-1 enzyme proteins in Sf9 cells with the wild-type 3beta-HSD1 as the control
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is elevated in ER+ postmenopausal breast cancer and progressive breast cancer by TNM stage (local lymph node invasion and distant metastases)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the selective inhibition of human 3beta-HSD1 in breast tumors represents a potential treatment for hormone-sensitive breast cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, X.F.; Luu-The, V.
Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha->beta)-hydroxysteroid epimerase
Biochim. Biophys. Acta
1520
124-130
2001
Homo sapiens
Rizner, T.L.; Lin, H.K.; Peehl, D.M.; Steckelbroeck, S.; Bauman, D.R.; Penning, T.M.
Human type 3 3alpha-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) and androgen metabolism in prostate cells
Endocrinology
144
2922-2932
2003
Homo sapiens
Steckelbroeck, S.; Jin, Y.; Gopishetty, S.; Oyesanmi, B.; Penning, T.M.
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3beta-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action
J. Biol. Chem.
279
10784-10795
2004
Homo sapiens (Q04828), Homo sapiens
Marijanovic, Z.; Laubner, D.; Moeller, G.; Gege, C.; Husen, B.; Adamski, J.; Breitling, R.
Closing the gap: Identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis
Mol. Endocrinol.
17
1715-1725
2003
Homo sapiens, Mus musculus
Steckelbroeck, S.; Oyesanmi, B.; Jin, Y.; Lee, S.H.; Kloosterboer, H.J.; Penning, T.M.
Tibolone metabolism in human liver is catalyzed by 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily
J. Pharmacol. Exp. Ther.
316
1300-1309
2006
Homo sapiens
Jin, Y.; Penning, T.M.
Molecular docking simulations of steroid substrates into human cytosolic hydroxysteroid dehydrogenases (AKR1C1 and AKR1C2): insights into positional and stereochemical preferences
Steroids
71
380-391
2006
Homo sapiens (Q04828), Homo sapiens
Taramino, S.; Teske, B.; Oliaro-Bosso, S.; Bard, M.; Balliano, G.
Divergent interactions involving the oxidosqualene cyclase and the steroid-3-ketoreductase in the sterol biosynthetic pathway of mammals and yeasts
Biochim. Biophys. Acta
1801
1232-1237
2010
Homo sapiens (P56937), Homo sapiens, Mus musculus (O88736), Mus musculus
Thomas, J.L.; Mack, V.L.; Sun, J.; Terrell, J.R.; Bucholtz, K.M.
The functions of key residues in the inhibitor, substrate and cofactor sites of human 3beta-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis
J. Steroid Biochem. Mol. Biol.
120
192-199
2010
Homo sapiens
Ferrante, T.; Adinolfi, S.; DArrigo, G.; Poirier, D.; Daga, M.; Lolli, M.L.; Balliano, G.; Spyrakis, F.; Oliaro-Bosso, S.
Multiple catalytic activities of human 17beta-hydroxysteroid dehydrogenase type 7 respond differently to inhibitors
Biochimie
170
106-117
2020
Homo sapiens (P56937), Homo sapiens
Wang, X.Q.; Aka, J.A.; Li, T.; Xu, D.; Doillon, C.J.; Lin, S.X.
Inhibition of 17beta-hydroxysteroid dehydrogenase type 7 modulates breast cancer protein profile and enhances apoptosis by down-regulating GRP78
J. Steroid Biochem. Mol. Biol.
172
188-197
2017
Homo sapiens (P56937)
Pham, J.H.; Will, C.M.; Mack, V.L.; Halbert, M.; Conner, E.A.; Bucholtz, K.M.; Thomas, J.L.
Structure-function relationships for the selective inhibition of human 3beta-hydroxysteroid dehydrogenase type 1 by a novel androgen analog
J. Steroid Biochem. Mol. Biol.
174
257-264
2017
Homo sapiens (P14060)
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