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Information on EC 2.8.2.4 - estrone sulfotransferase
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EC Tree
2.8.2.4 estrone sulfotransferaseSpecify your search results
Word Map
- 2.8.2.4
- steroid
-
sulfotransferases
- hydroxysteroid
- medicine
-
sulfatase
- 3'-phosphoadenosine
- pharmacology
- analysis
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
hsult1e1, oestrogen sulphotransferase, estrogen sulphotransferase, estrone sulfotransferase, sulfotransferase 1e1, oestrogen sulfotransferase, estrogen sult, estradiol sulfotransferase, rest-6, sult1e, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3'-phosphoadenylyl sulfate-estrone 3-sulfotransferase
-
-
-
-
3'-phosphoadenylyl sulfate:oestrone sulfotransferase
-
-
-
-
cytosolic sulfotransferase
EST
estrogen sulfotransferase
estrogen sulphotransferase
-
-
-
-
oestrogen sulphotransferase
rSULT1E1
steroid sulfotransferase
sulfotransferase 1E1
SULT
SULT1A1
SULT1E
SULT1E1
EST
-
-
estrogen sulfotransferase
-
-
-
-
estrogen sulfotransferase
-
-
estrogen sulfotransferase
-
oestrogen sulphotransferase
-
-
-
-
SULT1E1
-
-
SULT1E1
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
a reaction transition state with substantial S-O bond fission and partial charge neutralization of the leaving group
-
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
random bi-bi mechanism catalytic mechanism of SULTs, many family members have distinct, but overlapping substrate specificities, the enzymes have a sequential catalytic mechanism that is susceptible to substrate inhibition
3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate
the proposed reaction mechanism: upon binding of PAPS, Ser137 forms an H-bond with Lys47, thus prevents its interaction with the bridging oxygenin PAPS and its further hydrolysis; His107 attracts a proton from the substrate hydroxyl (i.e. of E2 or DHEA), and enables nucleophilic attack at the sulfur atom in PAPS. In the next step, Lys47 interacts with the 5' phosphate of PAPS, which helps in dissociation of the sulfuryl group and in its transfer to the substrate. Finally, the reaction products, PAP and E1-S, are released, which completes the catalytic cycle
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:estrone 3-sulfotransferase
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CAS REGISTRY NUMBER
COMMENTARY
9026-06-6
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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-estradiol + 3'-phosphoadenylyl sulfate
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phopshoadenylyl sulfate + resveratrol
adenosine 3',5'-bisphosphate + resveratrol 3-O-sulfate + resveratrol 4'-O-sulfate + resveratrol 3,4'-O-disulfate
-
i.e. 3,5,4'-trihydroxystilbene, a phytoestrogen with mixed estrogen agonist/antagonist properties developed as a chemopreventive agent, interaction of resveratrol with 17beta-estradiol, overview
three different sulfate products, product identification by NMR, overview
-
?
3'-phosphoadenylyl sulfate + 1,3-benzothiazol-6-ol
adenosine-3',5'-bisphosphate + 1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1,3-benzoxazol-6-ol
adenosine 3',5'-bisphosphate + 1,3-benzoxazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzofuran-5-ol
adenosine 3',5'-bisphosphate + 1-benzofuran-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzofuran-6-ol
adenosine 3',5'-bisphosphate + 1-benzofuran-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzothiophene-5-ol
adenosine 3',5'-bisphosphate + 1-benzothiophene-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzothiophene-6-ol
adenosine 3',5'-bisphosphate + 1-benzothiophene-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
3'-phosphoadenylyl sulfate + 1H-indol-6-ol
adenosine 3',5'-bisphosphate + 1H-indol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-aminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-aminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-cyanophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-cyanophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-dimethylaminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-dimethylaminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-fluorophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-fluorophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-iodophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-iodophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methoxyphenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methoxyphenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylamino-3-fluorophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methylamino-3-fluorophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylaminophenyl)-1,3-benzothiazol-5-ol
adenosine 3',5'-bisphosphate + 2-(4-methylaminophenyl)-1,3-benzothiazol-5-yl suflate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylaminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methylaminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylsulfonylphenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methylsulfonylphenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-N-acetylaminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-N-acetylaminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-nitrophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-nitrophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methyl-1,3-benzothiazol-5-ol
adenosine 3',5'-bisphosphate + 2-methyl-1,3-benzothiazol-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methyl-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-methyl-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methyl-17beta-estradiol
adenosine 3',5'-bisphosphate + 2-methyl-17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-phenyl-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-phenyl-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-[4-dimethylaminophenyl]-1,3-benzothiazol-5-ol
adenosine 3',5'-bisphosphate + 2-[4-dimethylaminophenyl]-1,3-benzothiazol-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3-cyano-7-hydroxycoumarin
adenosine 3',5'-bisphosphate + 3-cyano-7-hydroxycoumaryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + 6-hydroxy-4-methylbenzo[d]thiazole-2-carbonitrile
adenosine 3',5'-bisphosphate + ?
i.e. proluciferin substrate UGT-Glo substrate A, GSA
-
-
?
3'-phosphoadenylyl sulfate + apigenin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
3'-phosphoadenylyl sulfate + chrysin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + epicatechin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrogen
adenosine 3',5'-bisphosphate + estrogen 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + ethinyl estradiol
adenosine 3',5'-bisphosphate + ethinyl estradiol 3-sulfate
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a synthetic oral contraceptive, low activity
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + quercetin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + resveratrol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 1,3,5(10)-estratrien-3,16alpha,17beta-triol
adenosine 3',5'-bisphosphate + 1,3,5(10)-estratrien-16alpha,17beta-diol 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 1,3,5(10)-estratrien-3,17alpha-diol
adenosine 3',5'-bisphosphate + 1,3,5(10)-estratrien 17alpha-ol-3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 1,3,5(10)-estratrien-3,17beta-diol-17-monoacetate
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 1,3,5(10)-estratrien-3,17beta-diol-17-monoglucosiduronate
adenosine 3',5'-bisphosphate + ?
-
very low sulfation rate
-
-
r
3'-phosphoadenylylsulfate + 1,3,5(10)-estratrien-3,17beta-diol-17-monovalerinate
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 1,3,5(10)-estratrien-3-ol
adenosine 3',5'-bisphosphate + 1,3,5(10)-estratrien 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 11-hydroxy-1,3,5(10)-estratrien-17-one
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 16-epiestriol
adenosine 3',5'-bisphosphate + 16-epiestriol 3-sulfate
3'-phosphoadenylylsulfate + 17-deoxyestrone
adenosine 3',5'-bisphosphate + 17-deoxyestrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17-epiestriol
adenosine 3',5'-bisphosphate + 17-epiestriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17alpha ethinyl estradiol
adenosine 3',5'-bisphosphate + 17alpha ethinyl estradiol 3-sulfate
3'-phosphoadenylylsulfate + 17alpha-ethinylestradiol
adenosine 3',5'-bisphosphate + ?
-
isoform SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 17alpha-ethynyl-1,3,5(10)-estratrien-3,17beta-diol
adenosine 3',5'-bisphosphate + 17alpha-ethynyl-1,3,5(10)-estratrien-17beta-ol 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
3'-phosphoadenylylsulfate + 2-OH-1,3,7,8-tetrachlorinated dibenzo-p-dioxine
adenosine 3',5'-bisphosphate + 2-OH-1,3,7,8-tetrachlorinated dibenzo-p-dioxine sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-1,3,7,8-tetrachlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 2-OH-1,3,7,8-tetrachlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-3,7,8-trichlorinated dibenzo-p-dioxine
adenosine 3',5'-bisphosphate + 2-OH-3,7,8-trichlorinated dibenzo-p-dioxine sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-4,2',4'-trichlorodiphenyl ether
adenosine 3',5'-bisphosphate + 2-OH-4,2',4'-trichlorodiphenyl ethyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-4,5,3',2',3',4'-tetrachlorated biphenyl
adenosine 3',5'-bisphosphate + 2-OH-4,5,3',4'-tetrachlorated biphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-6,7,8-trichlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 2-OH-6,7,8-trichlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-7,8-dichlorinated dibenzo-p-dioxine
adenosine 3',5'-bisphosphate + 2-OH-7,8-dichlorinated dibenzo-p-dioxine sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-OH-7,8-dichlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 2-OH-7,8-dichlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3,16alpha-dihydroxy-1,3,5(10)-estratrien-17-one
adenosine 3',5'-bisphosphate + 16-alpha-hydroxy-1,3,5(10)-estratrien-17-one 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3,17beta-dihydroxy-1,3,5(10),9-estratetraen-12-one
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 3,17beta-dihydroxy-1,3,5(10)-estratrien-6-one
adenosine 3',5'-bisphosphate + ?
-
high sulfation rate
-
-
r
3'-phosphoadenylylsulfate + 3,5,3',5'-tetrabromo-4,4'-isopropylidendiphenol
adenosine 3',5'-bisphosphate + 3,5,3',5'-tetrabromo-4,4'-isopropylidendiphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3,5,3',5'-tetrachloro-4,4'-isopropylidendiphenol
adenosine 3',5'-bisphosphate + 3,5,3',5'- tetrachloro-4,4'-isopropylidendiphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-hydroxy-1,3,5(10),6,8-estrapentaen-17-one
adenosine 3',5'-bisphosphate + 1,3,5(10),6,8-estrapentaen-17-one 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-hydroxy-1,3,5(10),6-estratetraen-17-one
adenosine 3',5'-bisphosphate + 1,3,5(10),6-estratetraen-17-one 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-hydroxy-1,3,5(10),7-estratetraen-17-one
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-hydroxy-1,3,5(10),9-estratetraen-12,17-dione
adenosine 3',5'-bisphosphate + 1,3,5(10),9-estratetraen-12,17-dione 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-hydroxy-1,3,5(10)-estratrien-16-one
adenosine 3',5'-bisphosphate + 1,3,5(10)-estratriene-16-one 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-OH-2,4,7,8-tetrachlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 3-OH-2,4,7,8-tetrachlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-OH-2,6,7,8,9-pentachlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 3-OH-2,6,7,8,9-pentachlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-OH-2,6,7,8-tetrachlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 3-OH-2,6,7,8-tetrachlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3-OH-4,5,3',4'-tetrachlorated biphenyl
adenosine 3',5'-bisphosphate + 3-OH-4,5,3',4'-tetrachlorated biphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4,4'-(OH)2-3,5,3',5'-tetrachlorated biphenyl
adenosine 3',5'-bisphosphate + 4,4'-(OH)2-3,5,3',5'-tetrachlorated biphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-hydroxy-2,3,5,3',4'-pentachlorobiphenyl
adenosine 3',5'-bisphosphate + 4-hydroxy-2,3,5,3',4'-pentachlorobiphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-hydroxy-3,2',3',4',5'-pentachlorobiphenyl
adenosine 3',5'-bisphosphate + 4-hydroxy-3,2',3',4',5'-pentachlorobiphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-nitro-1,3,5(10)estratrien-3,17beta-diol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-OH-1,3,6,7-tetrachlorinated dibenzofuran
adenosine 3',5'-bisphosphate + 4-OH-1,3,6,7-tetrachlorinated dibenzofuranyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-OH-2',4',6'-tribromodiphenyl ether
adenosine 3',5'-bisphosphate + 4-OH-2',4',6'-tribromodiphenyl ethyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-OH-3',2',4',6'-tetrabromodiphenyl ether
adenosine 3',5'-bisphosphate + 4-OH-3',2',4',6'-tetrabromodiphenyl ethyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-OH-3',5,2',4',6'-pentabromodiphenyl ether
adenosine 3',5'-bisphosphate + 4-OH-3',5,2',4',6'- pentabromodiphenyl ethyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-OH-3,3',4'-trichlorated biphenyl
adenosine 3',5'-bisphosphate + 4-OH-3,3',4'-trichlorated biphenyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 7alpha-methyl-1,3,5(10)-estratrien-3,17beta-diol
adenosine 3',5'-bisphosphate + 7alpha-methyl-1,3,5(10)-estratrien 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 7alpha-methyl-3-hydroxy-1,3,5(10)-estratrien-17-one
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + androstenediol
adenosine 3',5'-bisphosphate + androstenediol sulfate
-
wild-type EST exhibits little ability to sulfate AD
-
r
3'-phosphoadenylylsulfate + butylated hydroxyanisole
adenosine 3',5'-bisphosphate + butylated hydroxyanisole sulfate
-
-
r
3'-phosphoadenylylsulfate + catechin hydrate
adenosine 3',5'-bisphosphate + catechin hydrate sulfate
-
-
r
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein sulfate
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylylsulfate + epicatechin
adenosine 3',5'-bisphosphate + epicatechin sulfate
-
-
r
3'-phosphoadenylylsulfate + epigallocatechin gallate
adenosine 3',5'-bisphosphate + epigallocatechin gallate sulfate
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate + genistein 4'-sulfate
-
-
r
3'-phosphoadenylylsulfate + hexestrol
adenosine 3',5'-bisphosphate + hexestrol 4-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + kaempferol
adenosine 3',5'-bisphosphate + kaempferol sulfate
-
-
r
3'-phosphoadenylylsulfate + myricetin
adenosine 3',5'-bisphosphate + myricetin sulfate
-
-
r
3'-phosphoadenylylsulfate + n-propyl gallate
adenosine 3',5'-bisphosphate + n-propyl gallate sulfate
-
-
r
3'-phosphoadenylylsulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
3'-phosphoadenylylsulfate + resveratrol
adenosine 3',5'-bisphosphate + resveratrol sulfate
-
-
-
r
3'-phosphoadenylylsulfate + stilbestrol
adenosine 3',5'-bisphosphate + stilbestrol 4-sulfate
-
-
-
r
8-bromoadenosine 3'-phosphate 5'-phosphosulfate + estrone
8-bromoadenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
-
r
adenosine 3'-phosphate 5'-phosphosulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
-
r
formycin 3'-phosphate 5'-phosphosulfate + estrone
formycin 3',5'-bisphosphate + estrone sulfate
-
-
-
-
r
tubercidin 3'-phosphate 5'-phosphosulfate + estrone
tubercidin 3',5'-bisphosphate + estrone sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
best substrate
-
-
?
3'-phosphoadenylyl sulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
17beta-estradiol regulates growth and differentiation in normal and malignant bone, it is inactivated to 17beta-estradiol-sulfate through SULT1E1
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
hSULT1E1 catalyzes the sulfation of estrogens and regulates estrogen bioactivities
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
the active site of hSULT1E1 contains Cys residues. Cys83 is critical for the redox regulation of hSULT1E1
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
SULT1E1 has a high affinity and catalytic efficiency for estradiol as substrate
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
inactivation
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
inactivation, increased 17beta-estradiol sulfation affects the GH signaling pathway and E2-regulated gene expression, enhanced SULT1E1 activity plays a role in inhibiting GH-stimulated STAT5b phosphorylation and IGF-1 synthesis via the sulfation and inactivation of 17beta-estradiol, regulation, overview
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + ?
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + ?
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
reaction of phenol sulfonyltransferase, EC 2.8.2.1, determination of reaction equilibrium in the forward direction at 70% of conversion of 4-nitrophenol
-
-
r
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
best substrate
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
SULT1E1 is involved in estrogen inactivation
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
high activity by SULT1E1, low activity by SULT1A1, EC 2.8.2.1
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
isozyme SULT1E1 is specific for estradiol sulfonation, interaction of resveratrol with 17beta-estradiol, overview
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
EST expression and regulation in invasive breast cancer and ductal carcinoma in situ, overview
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
estradiol sulfate is biologically inactive, the conversion of estradiol to its sulfate prevents it from binding to and thereby activating the estrogen receptor
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
SULT1E1 acts at nanomolar concentration of estradiol. SULT1A1 is active at micromolar concentration of estradiol and has an affinity 300fold lower than SULT1E1
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
SULT1E1 is involved in estrogen inactivation
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
high activity by SULT1E1, low activity by phenol sulfotransferase SULT1A1, EC 2.8.2.1
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
estrone sulfate is biologically inactive, the conversion of estradiol to its sulfate prevents it from binding to and thereby activating the estrogen receptor
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
hSULT1E1 catalyzes the sulfation of estrogens and regulates estrogen bioactivities
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
the active site of hSULT1E1 contains Cys residues. Cys83 is critical for the redox regulation of hSULT1E1
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + tamoxifen
adenosine 3',5'-bisphosphate + tamoxifen sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + tamoxifen
adenosine 3',5'-bisphosphate + tamoxifen sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + tamoxifen
adenosine 3',5'-bisphosphate + tamoxifen sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 16-epiestriol
adenosine 3',5'-bisphosphate + 16-epiestriol 3-sulfate
-
1,3,5(10)estratiene-3,16beta,17beta-triol
-
r
3'-phosphoadenylylsulfate + 16-epiestriol
adenosine 3',5'-bisphosphate + 16-epiestriol 3-sulfate
-
1,3,5(10)estratiene-3,16beta,17beta-triol
-
-
r
3'-phosphoadenylylsulfate + 17alpha ethinyl estradiol
adenosine 3',5'-bisphosphate + 17alpha ethinyl estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17alpha ethinyl estradiol
adenosine 3',5'-bisphosphate + 17alpha ethinyl estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17alpha ethinyl estradiol
adenosine 3',5'-bisphosphate + 17alpha ethinyl estradiol 3-sulfate
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
isoform rEST-6
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
best substrate
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
enzyme does not distinguish between estradiol and estrone, both appear to be natural substrates
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrogen
adenosine 3',5'-bisphosphate + estrogen sulfate
-
-
-
?
3'-phosphoadenylylsulfate + estrogen
adenosine 3',5'-bisphosphate + estrogen sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
steroid metabolism
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
also involved in the regulation of 17beta-estradiol levels in target tissue cells
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
isoform rEST-6
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
?
3'-phosphoadenylylsulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
-
-
-
r
3'-phosphoadenylylsulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
-
-
-
r
3'-phosphoadenylylsulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
-
model substrate, sulfonated by SULT1E1
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin sulfate
-
-
-
r
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin sulfate
-
-
r
additional information
?
-
-
dehydroepiandrosterone, etiocholanolone, 11-deoxycorticosterone, 17beta-oestradiol-3-methyl ether, testosterone, pregnenolone, beta-naphthylamine and p-nitrophenol are no substrates
-
-
?
additional information
?
-
-
enzyme does not sulfate an OH in position 2 or 4 of estrogens but sulfates, with decreased efficiency, the phenolic-OH on 6-benzoyl-naphthol, anthraquinone, fluorenes, diphenyl and tetraline, almost no sulfation of 4-hydroxybenzoic acid esters
-
-
?
additional information
?
-
-
simple phenols or steroid alcohols are no substrates
-
-
?
additional information
?
-
-
simple phenols, 2-naphthylamine and 3beta-hydroxysteroids are not sulfated, dienestrol is no substrate, dehydroepiandrosterone, phenol, p-nitrophenol, alpha-naphthol, beta-naphthol, beta-naphthylamine and 17 beta-estradiol-3-methyl ether fail to act as substrates
-
-
?
additional information
?
-
excess SULT1E1 is the reason for perturbed low ratio of active to inactive estrogens and the resulting hormonal imbalance contributing to the lack of overt signs of readiness for partirition in cows pregnant with clones
-
-
?
additional information
?
-
-
estrogen levels in healthy canine mammary gland and in canine inflammatory mammary carcinoma in relation to expression levels of enzymes involved in the estrogen metabolism, overview
-
-
?
additional information
?
-
-
p-nitrophenol and several neutral steroids are no substrates
-
-
?
additional information
?
-
-
activity toward dehydroepiandrosterone and testosterone is minimal or undetectable
-
-
?
additional information
?
-
caffeic acid, chlorogenic acid, BHT, and gallic acid are no substrates
-
-
?
additional information
?
-
-
1-hydroxy-2,4,7,8-tetrachlorodibenzofuran is no substrate
-
-
?
additional information
?
-
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression, estrogen levels play a role in development of cystic fibrosis
-
-
?
additional information
?
-
-
local production of estrogens in human peripheral tissues and/or breast carcinoma, overview
-
-
?
additional information
?
-
-
local regulation of estradiol and EST in ductal carcinoma, DCIS, correlation between aromatase and EST expression and grade of malignancy in ductal carcinoma, overview
-
-
?
additional information
?
-
-
phytoestrogens can potentially alter the homeostasis of estrogen levels
-
-
?
additional information
?
-
-
progestins, which activate the enzyme decrease cell proliferation of breast cancer cell lines, overview
-
-
?
additional information
?
-
-
SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals. This reaction increases the water solubility of the molecule, which may affect its cellular distribution and biological activity, and alter estrogen signaling to the estrogen receptor in human estrogen receptor-positive cells
-
-
?
additional information
?
-
SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals. This reaction increases the water solubility of the molecule, which may affect its cellular distribution and biological activity, and alter estrogen signaling to the estrogen receptor in human estrogen receptor-positive cells
-
-
?
additional information
?
-
SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview
-
-
?
additional information
?
-
role for 3'-phosphoadenylyl sulfate in priming the conformation of substrate binding loops, overview, substrate specificity and binding structure of SULT1E1, overview
-
-
?
additional information
?
-
-
the reaction is also performed by the phenol sulfotranferase, EC 2.8.2.1, but with lower activity
-
-
?
additional information
?
-
-
chronic topical application of parabens may lead to prolonged estrogenic effects in skin as a result of inhibition of estrogen sulfotransferase activity, overview. The skin anti-aging benefits of many topical cosmetics and pharmaceuticals could be derived, in part, from the estrogenicity of parabens
-
-
?
additional information
?
-
-
concerted action of catechol-O-methyltransferase and the cytosolic sulfotransferase, SULT, enzyme(s) in the metabolism of catecholestrogens with production of sulfated 2-methoxy-estrone or sulfated 2- or 4-methoxy-estradiol, overview
-
-
?
additional information
?
-
-
cytosolic sulfotransferase SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals
-
-
?
additional information
?
-
cytosolic sulfotransferase SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals
-
-
?
additional information
?
-
-
EST catalyzes the transfer of a sulfuryl group to estrogens and might be involved in endometriosis, an estrogen-dependent gynecological disease, characterized by implantation and invasive growth of endometrial tissue outside the uterine cavity, causing pelvic pain and infertility. Impaired estrogen metabolism plays a pivotal role in the pathogenesis of the disease, overview
-
-
?
additional information
?
-
-
estrogen exposure is a risk factor for gallstone disease, cholelithiasis, which often leads to chronic inflammation, cholecystitis. SULT1E1 is a key enzymes involved in the inactivation of estrogens. Estrogen concentrations in human gallbladder are regulated by a network of activating STS and inactivating SULT1E1, and estrogen receptors alpha and beta, localization in tissue, overview
-
-
?
additional information
?
-
-
SULT1E1 and ID2 genes are candidates for inherited predisposition to breast and ovarian cancer in Jewish women
-
-
?
additional information
?
-
-
SULT1E1 catalyzes the sulfate conjugation of estrone, estradiol, catecholestrogens, and 2-methyl-estradiol. SULT1E1 polymorphisms, together with other SULT enzyme polymorphisms, are risk factors for endometrial cancer susceptibility
-
-
?
additional information
?
-
-
SULT1E1 has a major role in estrogen conjugation. Important role for SULT isozymes and their pharmacogenetics in polyphenol disposition
-
-
?
additional information
?
-
SULT1E1 has a major role in estrogen conjugation. Important role for SULT isozymes and their pharmacogenetics in polyphenol disposition
-
-
?
additional information
?
-
-
SULT1E1 is involved in breast cancer cell proloferation, overview
-
-
?
additional information
?
-
-
SULT1E1 or EST is an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor. ectopic expression of SULT1E1 in MCF-7 cells suppresses the estrogen response. SULT1E1 is a transcriptional target of the glucocorticoid receptor, molecular mechanism, overview
-
-
?
additional information
?
-
-
SULT1E1 plays a regulatory role in estrogen signaling activities in human reproductive cells, including the prostate cells. SULT1E1 may function as a transcriptional mediator in transfected human prostate cancer CA-HPV-10 cells, molecular mechanism, overview
-
-
?
additional information
?
-
-
the endocrinological status of women bearing polycystic ovarian syndrome, PCOS, affects the endometrial in situ steroid metabolism, which involves EST, overview
-
-
?
additional information
?
-
-
the enzyme responsible for the formation of the biologically inactive estrogen sulfates
-
-
?
additional information
?
-
-
the redox regulation of hSULT1E1 may interrupt the regulation and function of estrogens under various physiological and pathological conditions
-
-
?
additional information
?
-
-
differential sulfating activities of the human SULTs toward catecholestrogens and nethoxyestrogens, overview
-
-
?
additional information
?
-
SULT1E1 catalyzes the sulfation of estradiol and other phenolic steroids
-
-
-
additional information
?
-
EST has a particularly high affinity for estrogens as substrates including estradiol (17beta-estradiol), estrone, and a variety of synthetic estrogens, like diethylstilbestrol and tamoxifen. EST also exhibits a low affinity for thyroid hormones, testosterones, or glucocorticoids
-
-
-
additional information
?
-
human estrogen sulfotransferase and its related fluorescently labeled decapeptides with a YKDG sequence specifically interact with oxidized low-density lipoprotein. Interaction between human SULT1E1 (hSULT1E1), which has a YKEG sequence (residues 61-64) unlike other human SULTs, and Ox-LDL. hSULT1E1 specifically binds to Ox-LDL and its major lipid component (lysophosphatidylcholine, LPC), and platelet-activating factor (PAF), which bear a marked resemblance to LPC in terms of structure and activity. An N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK, FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 also specifically binds to Ox-LDL, LPC, and PAF
-
-
-
additional information
?
-
-
human estrogen sulfotransferase and its related fluorescently labeled decapeptides with a YKDG sequence specifically interact with oxidized low-density lipoprotein. Interaction between human SULT1E1 (hSULT1E1), which has a YKEG sequence (residues 61-64) unlike other human SULTs, and Ox-LDL. hSULT1E1 specifically binds to Ox-LDL and its major lipid component (lysophosphatidylcholine, LPC), and platelet-activating factor (PAF), which bear a marked resemblance to LPC in terms of structure and activity. An N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK, FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 also specifically binds to Ox-LDL, LPC, and PAF
-
-
-
additional information
?
-
-
dehydroepiandrosterone and pregnenolone are no substrates
-
-
?
additional information
?
-
-
very little reactivity toward hydroxysteroids such as dehydroepiandrosterone
-
-
?
additional information
?
-
-
the role of the enzyme is most probably to protect male tissues against estronic action
-
-
?
additional information
?
-
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression, estrogen levels play a role in development of cystic fibrosis
-
-
?
additional information
?
-
-
SULT1E1 or EST is an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor. Ectopic expression of SULT1E1 in MCF-7 cells suppresses the estrogen response. Dexamethasone inhibits mouse uterine estrogen responses in a Sult1E1/EST-dependent manner. SULT1E1 is a transcriptional target of the glucocorticoid receptor, molecular mechanism, overview
-
-
?
additional information
?
-
-
the enzyme inactivates estrogen through sulfoconjugation
-
-
?
additional information
?
-
EST has a particularly high affinity for estrogens as substrates including estradiol (17beta-estradiol), estrone, and a variety of synthetic estrogens, like diethylstilbestrol and tamoxifen. EST also exhibits a low affinity for thyroid hormones, testosterones, or glucocorticoids
-
-
-
additional information
?
-
EST has a particularly high affinity for estrogens as substrates including estradiol (17beta-estradiol), estrone, and a variety of synthetic estrogens, like diethylstilbestrol and tamoxifen. EST also exhibits a low affinity for thyroid hormones, testosterones, or glucocorticoids
-
-
-
additional information
?
-
-
isoform rEST-6 selectively expressed in male rats sulfates estrogens, but dehydroepiandrosterone, pregnenolone, cortisol or testosterone are no substrates
-
-
?
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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
3'-phosphoadenylyl sulfate + 1,3-benzothiazol-6-ol
adenosine-3',5'-bisphosphate + 1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1,3-benzoxazol-6-ol
adenosine 3',5'-bisphosphate + 1,3-benzoxazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzofuran-5-ol
adenosine 3',5'-bisphosphate + 1-benzofuran-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzofuran-6-ol
adenosine 3',5'-bisphosphate + 1-benzofuran-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzothiophene-5-ol
adenosine 3',5'-bisphosphate + 1-benzothiophene-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-benzothiophene-6-ol
adenosine 3',5'-bisphosphate + 1-benzothiophene-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
3'-phosphoadenylyl sulfate + 1H-indol-6-ol
adenosine 3',5'-bisphosphate + 1H-indol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-aminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-aminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-cyanophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-cyanophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-dimethylaminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-dimethylaminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-fluorophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-fluorophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-iodophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-iodophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methoxyphenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methoxyphenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylamino-3-fluorophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methylamino-3-fluorophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylaminophenyl)-1,3-benzothiazol-5-ol
adenosine 3',5'-bisphosphate + 2-(4-methylaminophenyl)-1,3-benzothiazol-5-yl suflate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylaminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methylaminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-methylsulfonylphenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-methylsulfonylphenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-N-acetylaminophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-N-acetylaminophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-(4-nitrophenyl)-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-(4-nitrophenyl)-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methyl-1,3-benzothiazol-5-ol
adenosine 3',5'-bisphosphate + 2-methyl-1,3-benzothiazol-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methyl-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-methyl-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methyl-17beta-estradiol
adenosine 3',5'-bisphosphate + 2-methyl-17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-phenyl-1,3-benzothiazol-6-ol
adenosine 3',5'-bisphosphate + 2-phenyl-1,3-benzothiazol-6-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-[4-dimethylaminophenyl]-1,3-benzothiazol-5-ol
adenosine 3',5'-bisphosphate + 2-[4-dimethylaminophenyl]-1,3-benzothiazol-5-yl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + ?
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + ?
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrogen
adenosine 3',5'-bisphosphate + estrogen 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
best substrate
-
-
?
3'-phosphoadenylyl sulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
17beta-estradiol regulates growth and differentiation in normal and malignant bone, it is inactivated to 17beta-estradiol-sulfate through SULT1E1
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
hSULT1E1 catalyzes the sulfation of estrogens and regulates estrogen bioactivities
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
inactivation, increased 17beta-estradiol sulfation affects the GH signaling pathway and E2-regulated gene expression, enhanced SULT1E1 activity plays a role in inhibiting GH-stimulated STAT5b phosphorylation and IGF-1 synthesis via the sulfation and inactivation of 17beta-estradiol, regulation, overview
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + 17beta-estradiol sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
SULT1E1 is involved in estrogen inactivation
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
EST expression and regulation in invasive breast cancer and ductal carcinoma in situ, overview
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
estradiol sulfate is biologically inactive, the conversion of estradiol to its sulfate prevents it from binding to and thereby activating the estrogen receptor
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
SULT1E1 is involved in estrogen inactivation
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
estrone sulfate is biologically inactive, the conversion of estradiol to its sulfate prevents it from binding to and thereby activating the estrogen receptor
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
hSULT1E1 catalyzes the sulfation of estrogens and regulates estrogen bioactivities
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + tamoxifen
adenosine 3',5'-bisphosphate + tamoxifen sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + tamoxifen
adenosine 3',5'-bisphosphate + tamoxifen sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + tamoxifen
adenosine 3',5'-bisphosphate + tamoxifen sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
-
-
?
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
best substrate
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol 3-sulfate
-
enzyme does not distinguish between estradiol and estrone, both appear to be natural substrates
-
-
r
3'-phosphoadenylylsulfate + estrogen
adenosine 3',5'-bisphosphate + estrogen sulfate
-
-
-
?
3'-phosphoadenylylsulfate + estrogen
adenosine 3',5'-bisphosphate + estrogen sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
steroid metabolism
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
also involved in the regulation of 17beta-estradiol levels in target tissue cells
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
?
additional information
?
-
excess SULT1E1 is the reason for perturbed low ratio of active to inactive estrogens and the resulting hormonal imbalance contributing to the lack of overt signs of readiness for partirition in cows pregnant with clones
-
-
?
additional information
?
-
-
estrogen levels in healthy canine mammary gland and in canine inflammatory mammary carcinoma in relation to expression levels of enzymes involved in the estrogen metabolism, overview
-
-
?
additional information
?
-
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression, estrogen levels play a role in development of cystic fibrosis
-
-
?
additional information
?
-
-
local production of estrogens in human peripheral tissues and/or breast carcinoma, overview
-
-
?
additional information
?
-
-
local regulation of estradiol and EST in ductal carcinoma, DCIS, correlation between aromatase and EST expression and grade of malignancy in ductal carcinoma, overview
-
-
?
additional information
?
-
-
phytoestrogens can potentially alter the homeostasis of estrogen levels
-
-
?
additional information
?
-
-
progestins, which activate the enzyme decrease cell proliferation of breast cancer cell lines, overview
-
-
?
additional information
?
-
-
SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals. This reaction increases the water solubility of the molecule, which may affect its cellular distribution and biological activity, and alter estrogen signaling to the estrogen receptor in human estrogen receptor-positive cells
-
-
?
additional information
?
-
SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals. This reaction increases the water solubility of the molecule, which may affect its cellular distribution and biological activity, and alter estrogen signaling to the estrogen receptor in human estrogen receptor-positive cells
-
-
?
additional information
?
-
SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview
-
-
?
additional information
?
-
-
chronic topical application of parabens may lead to prolonged estrogenic effects in skin as a result of inhibition of estrogen sulfotransferase activity, overview. The skin anti-aging benefits of many topical cosmetics and pharmaceuticals could be derived, in part, from the estrogenicity of parabens
-
-
?
additional information
?
-
-
concerted action of catechol-O-methyltransferase and the cytosolic sulfotransferase, SULT, enzyme(s) in the metabolism of catecholestrogens with production of sulfated 2-methoxy-estrone or sulfated 2- or 4-methoxy-estradiol, overview
-
-
?
additional information
?
-
-
cytosolic sulfotransferase SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals
-
-
?
additional information
?
-
cytosolic sulfotransferase SULT1E1 catalyzes the sulfation of endogenous estrogens as well as xenobiotic estrogen-like chemicals
-
-
?
additional information
?
-
-
EST catalyzes the transfer of a sulfuryl group to estrogens and might be involved in endometriosis, an estrogen-dependent gynecological disease, characterized by implantation and invasive growth of endometrial tissue outside the uterine cavity, causing pelvic pain and infertility. Impaired estrogen metabolism plays a pivotal role in the pathogenesis of the disease, overview
-
-
?
additional information
?
-
-
estrogen exposure is a risk factor for gallstone disease, cholelithiasis, which often leads to chronic inflammation, cholecystitis. SULT1E1 is a key enzymes involved in the inactivation of estrogens. Estrogen concentrations in human gallbladder are regulated by a network of activating STS and inactivating SULT1E1, and estrogen receptors alpha and beta, localization in tissue, overview
-
-
?
additional information
?
-
-
SULT1E1 and ID2 genes are candidates for inherited predisposition to breast and ovarian cancer in Jewish women
-
-
?
additional information
?
-
-
SULT1E1 catalyzes the sulfate conjugation of estrone, estradiol, catecholestrogens, and 2-methyl-estradiol. SULT1E1 polymorphisms, together with other SULT enzyme polymorphisms, are risk factors for endometrial cancer susceptibility
-
-
?
additional information
?
-
-
SULT1E1 has a major role in estrogen conjugation. Important role for SULT isozymes and their pharmacogenetics in polyphenol disposition
-
-
?
additional information
?
-
SULT1E1 has a major role in estrogen conjugation. Important role for SULT isozymes and their pharmacogenetics in polyphenol disposition
-
-
?
additional information
?
-
-
SULT1E1 is involved in breast cancer cell proloferation, overview
-
-
?
additional information
?
-
-
SULT1E1 or EST is an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor. ectopic expression of SULT1E1 in MCF-7 cells suppresses the estrogen response. SULT1E1 is a transcriptional target of the glucocorticoid receptor, molecular mechanism, overview
-
-
?
additional information
?
-
-
SULT1E1 plays a regulatory role in estrogen signaling activities in human reproductive cells, including the prostate cells. SULT1E1 may function as a transcriptional mediator in transfected human prostate cancer CA-HPV-10 cells, molecular mechanism, overview
-
-
?
additional information
?
-
-
the endocrinological status of women bearing polycystic ovarian syndrome, PCOS, affects the endometrial in situ steroid metabolism, which involves EST, overview
-
-
?
additional information
?
-
-
the enzyme responsible for the formation of the biologically inactive estrogen sulfates
-
-
?
additional information
?
-
-
the redox regulation of hSULT1E1 may interrupt the regulation and function of estrogens under various physiological and pathological conditions
-
-
?
additional information
?
-
SULT1E1 catalyzes the sulfation of estradiol and other phenolic steroids
-
-
-
additional information
?
-
-
the role of the enzyme is most probably to protect male tissues against estronic action
-
-
?
additional information
?
-
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression, estrogen levels play a role in development of cystic fibrosis
-
-
?
additional information
?
-
-
SULT1E1 or EST is an enzyme important for the metabolic deactivation of estrogens, because sulfonated estrogens fail to activate the estrogen receptor. Ectopic expression of SULT1E1 in MCF-7 cells suppresses the estrogen response. Dexamethasone inhibits mouse uterine estrogen responses in a Sult1E1/EST-dependent manner. SULT1E1 is a transcriptional target of the glucocorticoid receptor, molecular mechanism, overview
-
-
?
additional information
?
-
-
the enzyme inactivates estrogen through sulfoconjugation
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
additional information
-
varying the Mg2+ concentration from 0-10 mM in the beta-estradiol sulfation reaction does not affect the sulfation activity of isoform rEST-6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-6,9:15,16-diepoxy-9alpha-hydroxy-8,9-seco-13(16),14-labdadiene-7-one
-
(7-amino-3(beta-D-ribofuranosyl)-pyrazolo-[4,3-d]pyrimidine) 3',5'-diphosphate
-
-
1-[2-(p-[3,4-dihydro-6-methoxy-2-phenyl-1-naphthyl]phenoxy)ethyl]-pyrrolidine hydrochloride
-
-
2,3',4-trichloro-4'-hydroxybiphenyl
the inhibitor has been identified as a metabolite in human plasma with an estimated half-life of 6.5 years
-
3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide
DBHM
3,5-dibromo-4-hydroxybenzoic acid (6,8-dichloro-4-oxo-4H-chromen-3-ylmethylene) hydrazide
DBHD
3alpha-tibolone
-
activates SULT1E1 in MCF-7 cells by 50% and 37% at low concentrations of 50 nM and 500 nM, respectively, inhibits at 0.05 mM by 63%
3beta-tibolone
-
activates SULT1E1 in MCF-7 cells by 101% and 74% at low concentrations of 50 nM and 500 nM, respectively, inhibits at 0.05 mM by 54%
4-hydroxybenzoate esters
-
i.e.parabens, structure-activity relationship, overview
abiraterone
antiandrogen drug, metabolite abiraterone, not the parent drug abiraterone acetate, is responsible for the inhibition
Acetylsalicylate
binds near enough to the substrate site to prevent catalysis but not affect dissociation of the substrate-enzyme complex
adenosine 5'-(beta,gamma-imido) triphosphate
i.e. AMP-PNP, a non-hydrolysable ATP analogue
buthionine sulfoxamine
-
a GSH depletor, decreases SULT1E1 activity, but fails to affect the enzyme amount in Hep-G2 cells
butylparaben
-
50% inhibition at 0.021 mM, complete inhibition at 1 mM; strong inhibition, which is threefold higher in vivo than in vitro
gavestinel
i.e. 4,6-dichloro-3-[(1E)-3-oxo-3-(phenylamino)-1-propenyl]-1H-indole-2-carboxylic acid sodium salt
GSSG
-
oxidized glutathione, inactivation and kinetics, adenosine 3'-phosphate 5'-phosphosulfate protects
ICI 182,720
-
produces a marked decrease (over 50%) of EST activity with respect to untreated control cell cultures at 24 h
L689,560
i.e. trans-2-carboxy-5,7-dichloro-4-phenylaminocarboxylamino-1,2,3,4-tetrahydroquinoline
meclofenamate
binds near enough to the substrate site to prevent catalysis but not affect dissociation of the substrate-enzyme complex
medrogestone
-
biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, overview
nimesulide
binds near enough to the substrate site to prevent catalysis but not affect dissociation of the substrate-enzyme complex
OrgOD14
-
active substance in Livial (r), above 0.05 mM decreases significantly biosynthesis of estrone by 50-60%, no effect in MDA-MB-231 cells
Promegestone
-
activates SULT1E1 by 26% at low concentrations of 500 nM, inhibits at 0.05 mM by 41%, leads to increased and decreased expression levels, respetively; biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, overview
tibolone
-
activates SULT1E1 in MCF-7 cells by 63% and 44% at low concentrations of 50 nM and 500 nM, respectively, inhibits at 0.05 mM by 64%
trans-resveratrol
-
0.1 mM resveratrol significantly decreases the SULT1E1-mediated beta-estradiol sulfation
17beta-estradiol
-
17beta-estradiol is a partial kcat-inhibitor (saturation with inhibitor decreases kcat about 7fold without altering Km for PAPS)
resveratrol
-
inhibits estradiol sulfonation, phytoestrogen with mixed estrogen agonist/antagonist properties developed as a chemopreventive agent, interaction of resveratrol with 17beta-estradiol
triclosan
-
triclosan directly inhibits and indirectly induces certain phase II UDP-glucuronosyltransferase (UGT) and PAPS-sulfotransferase (SULT) enzymes. It is an especially potent competitive inhibitor of ovine placental estrogen sulfotransferase
additional information
-
only moderately sensitive to SH-blocking agents, no inhibition with EDTA up to 20 mM
-
additional information
-
5alpha-androstanes are weak competitive inhibitors, the product estrone sulfate is not inhibitory, no inhibition with 1,3,5(10)estatriene, 1,3,5,(10)estatriene-3,17beta-diol 3,17beta-disulfate, MER-25, 1-[p-2-diethylaminoethoxyphenyl]-1-phenyl-2-p-methoxyphenyl ethanol and 5-androstene
-
additional information
-
native liver enzyme is less potently inhibited than recombinant SULT1E1
-
additional information
-
low SULT1E1 and/or high steroid sulfatase expression in breast tumor tissue correlates with a poor prognosis for disease progression. Concentrations of isoflavonoids that may be achieved in individuals consuming a high-soy diet may inhibit SULT1E1 activity while exerting no effect on steroid sulfatase
-
additional information
-
no inhibition by hydroxybenzoic acid, while butylparaben blocks the skin cytosol sulfation of estradiol and estrone, but not the androgen dehydroepiandrosterone. Structure-activity-relationship of parabens as inhibitors of estrogen sulfation, potency of SULT inhibition increases as the paraben ester chain length increases, overview
-
additional information
not inhibited by isoleoheterin, (-)-8n-acetoxy-15,16-epoxy-8,9-seco-13(16),14-labdadiene-7,9-dione, (-) hispanolone, (+)-leoheterin, (+)-galeopsin, and (+)-sibiricinone B
-
additional information
hydroxylated and sulfated metabolites of commonly occurring airborne polychlorinated biphenyls inhibit human steroid sulfotransferases SULT1E1 and SULT2A1 (EC 2.8.2.2). No inhibition by 4-chloro-4'-hydroxybiphenylsulfate, 2,4'-dichloro-4-hydroxybiphenylsulfate, 3,3'-dichloro-4-hydroxybiphenylsulfate, and 2,2',5,5'-tetrachloro-4-hydroxybiphenylsulfate at up to 0.01 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3alpha-hydroxy-tibolone
-
biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, in MCF-7 and T4-7D cells, overview
3alpha-tibolone
-
activates SULT1E1 in MCF-7 cells by 50% and 37% at low concentrations of 50 nM and 500 nM, respectively, inhibits at 0.05 mM by 63%
3beta-hydroxy-tibolone
-
biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, in MCF-7 and T4-7D cells, overview
3beta-tibolone
-
activates SULT1E1 in MCF-7 cells by 101% and 74% at low concentrations of 50 nM and 500 nM, respectively, inhibits at 0.05 mM by 54%
Melatonin
-
the level of EST mRNA steady-state of cells treated with melatonin is three times higher than that in control cells
N-acetylcysteine
-
a GSH inducer, increases SULT1E1 activity, but fails to affect the enzyme amount in Hep-G2 cells
NaCl
-
activity of liver EST transiently expressed in COS-1 cells increases 86% in presence of 150 mM
progesterone
-
specific induction by 0.01 mM, 7fold increase in sulfation of beta-estradiol, Ishikawa endometrial adenocarcinoma cells
17-hydroxy-19-nor-7-methyl-17-pregn-5(10)-en-20-yn-3-one
-
Org OD14, active substance in Livial (R), 0.0005-0.00005 mM stimulates the formation of estrone by 40-60%, no effect in MDA-MB-231 cells
medrogestone
-
biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, overview
monothiolglycerol
-
stimulates uterine and chorion enzymes by 5fold and 15fold
nomegestrol acetate
-
activates SULT1E1 maximally at 500 nM by 83% in MCF-7 cells and by 69% in T-47D cells
nomegestrol acetate
-
stimulates at low concentrations, but has no effect at high concentrations, overview
Promegestone
-
activates SULT1E1 by 26% at low concentrations of 500 nM, inhibits at 0.05 mM by 41%, leads to increased and decreased expression levels, respetively
Promegestone
-
biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, overview
tibolone
-
activates SULT1E1 in MCF-7 cells by 63% and 44% at low concentrations of 50 nM and 500 nM, respectively, inhibits at 0.05 mM by 64%
tibolone
-
biphasic effect, inhibits at high concentrations, but stimulates at low concentrations, in MCF-7 and T4-7D cells, overview
additional information
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression
-
additional information
-
activation of the glucocorticoid receptor by dexamethasone induces the expression and activity of estrogen sulfotransferase SULT1E1
-
additional information
-
SULT1E1 expression is 3-4fold increased in inflamed gallbladder epithelium along with an increased in estrogen receptors, overview
-
additional information
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression
-
additional information
-
activation of the glucocorticoid receptor by dexamethasone induces the expression and activity of estrogen sulfotransferase SULT1E1, which is suppressed by the coadministration of RU486, a glucocorticoid receptor antagonist. The pregnane X receptor PXR agonist PCN fails to increase Sult1E1 mRNA level in wild-type mice
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Atherosclerosis
Human estrogen sulfotransferase and its related fluorescently labeled decapeptides specifically interact with oxidized low-density lipoprotein.
Atherosclerosis
Interaction of Native- and Oxidized-Low-Density Lipoprotein with Human Estrogen Sulfotransferase.
Breast Neoplasms
A correlation between estrogen sulfotransferase levels and estrogen receptor status in human primary breast carcinoma.
Breast Neoplasms
Effect of Org OD14 (LIVIAL) and its metabolites on human estrogen sulphotransferase activity in the hormone-dependent MCF-7 and T-47D, and the hormone-independent MDA-MB-231, breast cancer cell lines.
Breast Neoplasms
Enzymic synthesis of steroid sulphates. XVII. On the structure of bovine estrogen sulphotransferase.
Breast Neoplasms
Estrone sulfatase versus estrone sulfotransferase in human breast cancer: potential clinical applications.
Breast Neoplasms
Expression of Estrogen Sulfotransferase 1E1 and Steroid Sulfatase in Breast Cancer: A Immunohistochemical Study.
Breast Neoplasms
Expression of hydroxysteroid sulphotransferase is related to estrogen receptor status in human mammary cancer.
Breast Neoplasms
Oestrogen sulfotransferase: isolation of a high specific activity species from bovine placenta.
Breast Neoplasms
Steroid sulphotransferase activity in human hormone-independent MDA-MB-468 mammary cancer cells.
Carcinoma
Steroid sulphatase and oestrogen sulphotransferase in human non-small-cell lung carcinoma.
Carcinoma, Non-Small-Cell Lung
Steroid sulphatase and oestrogen sulphotransferase in human non-small-cell lung carcinoma.
Colonic Neoplasms
Inhibitory effects of various beverages on the sulfoconjugation of 17beta-estradiol in human colon carcinoma Caco-2 cells.
Cystic Fibrosis
Increased SULT1E1 activity in HepG2 hepatocytes decreases growth hormone stimulation of STAT5b phosphorylation.
Endometriosis
Expression of aromatase and estrogen sulfotransferase in eutopic and ectopic endometrium: evidence for unbalanced estradiol production in endometriosis.
Neoplasms
Effect of hormone manipulation on oxidation, reduction and sulphurylation of dehydroepiandrosterone and oestrone in DMBA-induced rat mammary tumours.
Neoplasms
Properties of estrogen and hydroxysteroid sulphotransferases in human mammary cancer.
Neoplasms
Steroid sulphotransferase activity in human hormone-independent MDA-MB-468 mammary cancer cells.
Neoplasms
The steroid alcohol and estrogen sulfotransferases in rodent and human mammary tumors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00211
2-(4-aminophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00025
2-(4-cyanophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00142
2-(4-dimethylaminophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00056
2-(4-fluorophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00052
2-(4-iodophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.0009
2-(4-methoxyphenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.001
2-(4-methylamino-3-fluorophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00077
2-(4-methylaminophenyl)-1,3-benzothiazol-5-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00142
2-(4-methylaminophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00132
2-(4-methylsulfonylphenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00236
2-(4-N-acetylaminophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00012
2-(4-nitrophenyl)-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00099
2-phenyl-1,3-benzothiazol-6-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.00043
2-[4-dimethylaminophenyl]-1,3-benzothiazol-5-ol
-
in 50 mM Tris-HCl, pH 7.4, at 37°C
0.000005
3'-phosphoadenylyl sulfate
-
pH and temperature not specified in the publication
0.00033
beta-estradiol
isoform SULT1E1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C
0.000029
17beta-estradiol
SULT1E1, pH and temperature not specified in the publication
0.00011
estrone
SULT1E1, pH and temperature not specified in the publication
additional information
additional information
kinetics of SULT1E1, overview
-
additional information
additional information
-
transition state and kinetic isotope effects, detailed overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00011
3-cyano-7-hydroxycoumarin
mutant enzyme K85E/A135T/F138Y/G182S/L251V, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.065
3-cyano-7-hydroxycoumarin
mutant enzyme E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.179
3-cyano-7-hydroxycoumarin
mutant enzyme D65N/K85E/E86K/F138Y, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.694
3-cyano-7-hydroxycoumarin
wild type enzyme, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.0009
4-nitrophenol
mutant enzyme K85E/A135T/F138Y/G182S/L251V, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.01
4-nitrophenol
mutant enzyme E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.059
4-nitrophenol
mutant enzyme D65N/K85E/E86K/F138Y, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
0.151
4-nitrophenol
wild type enzyme, 7 mM MgCl2, 1.5 mM dithiothreitol, and 20 mM HEPES (pH 7.5), temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
(7-amino-3(beta-D-ribofuranosyl)-pyrazolo-[4,3-d]pyrimidine) 3,5''-diphosphate
-
pH 7.5, 37°C
0.074
1-[2-(p-[3,4-dihydro-6-methoxy-2-phenyl-1-naphthyl]phenoxy)ethyl]-pyrrolidine hydrochloride
-
pH 8.1, 37°C
0.0017
8-bromoadenosine 3'-phosphate 5'-phosphosulfate
-
pH 7.5, 37°C, competitive inhibition
0.043
formycin 3'-phosphate 5'-phosphosulfate
-
pH 7.5, 37°C, noncompetitive inhibition
0.068
nebularine(9-beta-D-ribofuranosylpurine)adenosine 3',5'-diphosphate
-
pH 7.5, 37°C
0.0006
tubercidin 3'-phosphate 5'-phosphosulfate
-
pH 7.5, 37°C, competitive inhibition
0.0006
resveratrol
-
pH 7.4, jejunum extract, inhibition of estradiol sulfonation
0.0023
resveratrol
-
pH 7.4, recombinant SULT1E1, inhibition of estradiol sulfonation
additional information
additional information
-
inactivation kinetics with oxidized glutathione
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0313
(+)-6beta-hydroxy-15,16-epoxylabda-8,13(16),14-trien-7-one
Homo sapiens
at pH 6.0 and 37°C
0.0405
(-)-6,9:15,16-diepoxy-9alpha-hydroxy-8,9-seco-13(16),14-labdadiene-7-one
Homo sapiens
at pH 6.0 and 37°C
0.000019
2,2',5,5'-tetrachloro-4-hydroxybiphenyl
Homo sapiens
recombinant SULT1E1, pH 7.4, 37°C
-
0.00044
2,3',4-trichloro-4'-biphenylsulfate
Homo sapiens
recombinant SULT1E1, pH 7.4, 37°C
-
0.0000073
2,3',4-trichloro-4'-hydroxybiphenyl
Homo sapiens
recombinant SULT1E1, pH 7.4, 37°C
-
0.000018
2,4'-dichloro-4-hydroxybiphenyl
Homo sapiens
recombinant SULT1E1, pH 7.4, 37°C
-
0.0000072
3,3'-dichloro-4-hydroxybiphenyl
Homo sapiens
recombinant SULT1E1, pH 7.4, 37°C
-
0.012
butylparaben
Homo sapiens
-
pH 7.4, 37°C, inhibition of estradiol sulfation, NHEK cells
0.021
butylparaben
Homo sapiens
-
pH 7.4, 37°C, inhibition of estradiol sulfation, liver cytosol
0.037
butylparaben
Homo sapiens
-
pH 7.4, 37°C, inhibition of estradiol sulfation, skin cytosol
0.062
butylparaben
Homo sapiens
-
pH 7.4, 37°C, inhibition of estrone sulfation, skin cytosol
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity in healthy and hyperplasic endometrium with or without polycystic ovary syndrome, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
5.5
5.8
6.1
-
2 forms of the enzyme, FPLC chromatofocusing in a pH gradient of 4.0-7.1
6.4
5.5
-
2 forms of the enzyme, FPLC chromatofocusing in a pH gradient of 4.0-7.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
guinea pig
-
-
brenda
-
676931, 677219, 690848, 691170, 691194, 691580, 691624, 691630, 692042, 692263, 693848, 693892, 701709, 701710, 701711
-
-
brenda
-
738296, 738894, 738929, 739055, 739089, 739665, 760317, 761001, 761169, 761725, 761874, 761875, 762067
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
benign, and primary and secondary malignant bone tumors, from patients undergoing routine surgery for skeletal tumors
brenda
-
recombinant SULT1E1 expressed in insect Sf9 cells
brenda
determination of the levels of SULT1E1, STS and estrogen receptor alpha (ERalpha) protein in paraffin-embedded specimens from 206 patients with Federation of Gynecology and Obstetrics stage II-IV EOC treated with debulking surgery and standard platinum-based adjuvant chemotherapy. Significantly higher SULT1E1 levels are observed in better differentiated EOC tumors compared to grade 3 EOC tumors. STS and SULT1E1 levels are positively associated with ERalpha abundance
brenda
high level in males. Castration of male mice abolishes EST expression in the epididymal fat, whereas testosterone supplementation restores it, suggesting that EST expression in male WAT is testosterone-dependent
brenda
-
from from 14 patients operated for symptomatic cholelithiais
brenda
-
an osteosarcoma cell line, increased expression compared to healthy cells
brenda
-
a Ewings sarcoma cell line, expression level of SULT1E1 is slightly reduced comapred to heathy cells
brenda
additional information
EST is predominantly expressed in stromal vascular cells (pre-adipocytes). Consistent with the pre-adipocyte pattern of expression, the expression of EST is dramatically reduced in differentiated 3T3-L1 cells or mature primary adipocytes
brenda
-
EST is predominantly expressed in stromal vascular cells (pre-adipocytes). Consistent with the pre-adipocyte pattern of expression, the expression of EST is dramatically reduced in differentiated 3T3-L1 cells or mature primary adipocytes
-
brenda
EST expression is detectable in the subcutaneous adipose tissue in both obese women and men. The expression of EST in the abdominal subcutaneous fat of obese and nonobese female human subjects and in primary adipose-derived stem cells (ASCs) isolated from female subjects is low, but the expression of EST increases with the onset of differentiation. EST is detectable in the subcutaneous adipose tissue in both obese women and men, especially in the abdominal area
brenda
-
-
brenda
-
the majority of the SULT1E1 activity is observed in the frontal cortical area, superior cortical areas, subcortical areas, and brain stem
brenda
reduced SULT1E1 expression in MCF-7 cells, but elevated SULT1E1 expression in breast tumour tissue, which also exhibits elevated E2 concentrations and increased Nrf2 expression as compared to the surrounding. Nrf2 is an oxidative stress responsive transcription protein, in situ expression analysis, overview
brenda
-
hormone-dependent MCF-7 and T47D, hormone-independent MDA-MB-231
brenda
-
EST is localized all along the excurrent duct with a higher signal in the caput and corpus epididymis
brenda
high level in males. Castration of male mice abolishes EST expression in the epididymal fat, whereas testosterone supplementation restores it, suggesting that EST expression in male WAT is testosterone-dependent
brenda
-
high level in males. Castration of male mice abolishes EST expression in the epididymal fat, whereas testosterone supplementation restores it, suggesting that EST expression in male WAT is testosterone-dependent
-
brenda
-
not expressed in a host of breast cancer cell lines such as MCF-7 cells
brenda
-
-
brenda
-
knockout of the cystic fibrosis transmembrane conductance regulator, CFTR, leads to increased SULT1E1 expression
brenda
liver has a low basal expression of Est, but the hepatic expression of Est is highly induced in the ob/ob, db/db, and HFD-induced obese mice
brenda
-
liver has a low basal expression of Est, but the hepatic expression of Est is highly induced in the ob/ob, db/db, and HFD-induced obese mice
-
brenda
-
estrogen sulfotransferase is significantly more active in the normal breast cell than in the cancer cell
brenda
-
estrogen sulfotransferase is significantly more active in the normal breast cell than in the cancer cell
brenda
reduced SULT1E1 expression in MCF-7 cells, but elevated SULT1E1 expression in breast tumour tissue, which also exhibits elevated E2 concentrations and increased Nrf2 expression as compared to the surrounding. Nrf2 is an oxidative stress responsive transcription protein
brenda
-
EST is expressed in the granulosa and cumulus cells of the large antral follicles and is absent in both the theca cells and oocytes
brenda
WAT, high level in females. EST expression in male WAT is testosterone-dependent. Although the basal expression of Est in the female mouse WAT is low, it can be induced in the parametrial fat by testosterone treatment. The induction of EST expression by testosterone in female mice is WAT specific, because testosterone treatment fails to induce the expression of EST in the liver
brenda
-
WAT, high level in females. EST expression in male WAT is testosterone-dependent. Although the basal expression of Est in the female mouse WAT is low, it can be induced in the parametrial fat by testosterone treatment. The induction of EST expression by testosterone in female mice is WAT specific, because testosterone treatment fails to induce the expression of EST in the liver
-
brenda
additional information
-
analysis of tissue specific expression of the enzyme, overview
brenda
additional information
-
expression analysis of the enzyme in healthy and preinvasive and invasive tumor breast tissue, no stromal expression
brenda
additional information
-
SULT1E1 bone expression levels show no correlation to age
brenda
additional information
-
no SULT1E1 expression is detectable in MMNK-1 cells
brenda
additional information
-
the enzyme is not detected in non-neoplastic prostate tissues
brenda
additional information
STS is upregulated in patients with chronic inflammatory liver diseases. Tissue distribution and the transcriptional regulation of EST and STS exhibit obvious sex and species specificity
brenda
additional information
quantitative real-time RT-PCR enzyme expression analysis in female and male tissue samples, tissue distribution and expression pattern, overview
brenda
additional information
-
not detected in brain, intestine, liver, ovary, uterus, and stomach
brenda
additional information
in mice, the expression of EST shows sex specificity. Male, but not female, mice express a high basal level of EST in the white adipose tissue (WAT). The expression of EST in the male epididymal fat pad is particularly highly. The expression of EST is also detected at a lower level in several other white adipose depots, but not in the brown adipose tissue
brenda
additional information
the expression of Est exhibits both tissue and sex specificity. In male mice, the expression of Est is high in the white adipose tissue (WAT) and testis
brenda
additional information
-
in mice, the expression of EST shows sex specificity. Male, but not female, mice express a high basal level of EST in the white adipose tissue (WAT). The expression of EST in the male epididymal fat pad is particularly highly. The expression of EST is also detected at a lower level in several other white adipose depots, but not in the brown adipose tissue
-
brenda
additional information
-
the expression of Est exhibits both tissue and sex specificity. In male mice, the expression of Est is high in the white adipose tissue (WAT) and testis
-
brenda
additional information
-
determination of SULT1E1 expression during the estrous cycle, ovaries from sexually mature, cycling female Wistar rats, no expression in ovarial theca cells and oocytes, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
-
-
675086, 677219, 690848, 691170, 691194, 691624, 692042, 693884, 693892, 701711, 706922, 716213, 725965
brenda
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
gene structure and genomic organization of each cynomolgus SULTs are similar to those of the human orthologues. SULT1B1 and SULT1E1 form a gene cluster
evolution
the estrogen sulfotransferase (EST or SULT1E1) is a member of the sulfotransferase family. It shares high amino acid homology with other sulfotransferase isoforms. But EST is believed to have unique functions due to its distinct substrates and specific tissue distribution and sex-regulated expression. The effect of EST on adipogenesis seems to be species specific. The anti-adipogenic activity of EST in mice is opposite to the pro-adipogenic effect of the same enzyme in human adipocytes
evolution
the estrogen sulfotransferase (EST or SULT1E1) is a member of the sulfotransferase family. It shares high amino acid homology with other sulfotransferase isoforms. But EST is believed to have unique functions due to its distinct substrates and specific tissue distribution and sex-regulated expression. The effect of EST on adipogenesis seems to be species specific. The anti-adipogenic activity of EST in mice is opposite to the pro-adipogenic effect of the same enzyme in human adipocytes
evolution
-
the estrogen sulfotransferase (EST or SULT1E1) is a member of the sulfotransferase family. It shares high amino acid homology with other sulfotransferase isoforms. But EST is believed to have unique functions due to its distinct substrates and specific tissue distribution and sex-regulated expression. The effect of EST on adipogenesis seems to be species specific. The anti-adipogenic activity of EST in mice is opposite to the pro-adipogenic effect of the same enzyme in human adipocytes
-
malfunction
-
loss of EST may result in altered estrogen metabolism in hormone-dependent breast cancer cells
malfunction
-
ablation of the enzyme accelerates the differentiation of primary preadipocytes
malfunction
knock-down of the enzyme in HUVEC cells results in regulation of genes involved in inflammation and lipid metabolism
malfunction
-
inhibition of Eenzyme activity produces placental thrombosis and spontaneous abortion
malfunction
inhibition of Eenzyme activity produces placental thrombosis and spontaneous abortion
malfunction
-
administration of low dose triclosan to pregnant ewes results in placental uptake and reduced estradiol sulfotransferase activity in fetal liver and placenta, effects of triclosan exposure (administered to late gestation fetal sheep for two days either by direct infusion into the fetal circulation or infusion into the maternal blood) of pregnant ewes on placental and hepatic sulfotransferase activity, overview. Placenta contained higher concentrations of triclosan than liver in each individual sheep in both treatment groups
malfunction
EST ablation produces completely opposite metabolic phenotype in female and male obese mice. Male Est-/- mice develop age-dependent Leydig cell hypertrophy/hyperplasia and impaired steroidogenesis, have reduced total and forward sperm motility, and produce smaller litters compared with age-matched wild-type males. In female mice, ablation of the mouse Sult1e1 gene causes placental thrombosis and spontaneous fetal loss, which is associated with elevated free estrogen levels in the circulation and the amniotic fluid. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). The activation of GR can lead to hyperglycemia in genetically obese viable yellow (Avy) female mice due to an aberrant shift in hepatic androgen/ estrogen balance. Castration of male mice abolishes EST expression in the epididymal fat, whereas testosterone supplementation restores it. Although EST expression can be induced in the parametrial fat of female mice, whole body ablation of EST does not cause any differences in fat indices (fat weight normalized to body weight) between female WT and EST-/- mice. EST-/- male mice have their epididymal and inguinal fat indices significantly higher than those of the wild-type mice. Adipocyte size in EST-/- male mice is markedly larger than that of wild-type mice, but under chow diet, these changes are not accompanied by obvious metabolic abnormalities. EST loss in obese males worsens metabolic phenotype. Female obe mice exhibit completely opposite metabolic phenotypes. Whole body loss of EST expression in the ob/ob background decreases hepatic gluconeogenesis and lipogenesis, improves body composition and insulin sensitivity, and increases energy expenditure. Ablation of EST in female ob/ob mice does not affect WAT inflammation
malfunction
impairment in the hepatic estrogen sulfotransferase (SULT1E1) protein expression are noticed with interfered hepatic free-thiols only in a N-ethyl-N-nitrosourea (ENU) and a xenograft-estradiol (E2) group compared to the arsenic group. Impairment of SULT1E1 expression and E2 regulations through oxidant-stress signalling. Oxidative stress has a vital role in E2 regulation and can structurally modify or alter the expression level of E2 metabolizing proteins. As such, estrogen receptors lose their DNA binding ability and thus impairing transcription. The estradiol binding site gets blocked in estrogen sulfotransferase under oxidative stress
malfunction
loss of Est in male ob/ob mice, but not in female ob/ob mice, exacerbates the diabetic phenotype. Transgenic reconstitution of Est in the adipose tissue, but not in the liver, attenuates diabetic phenotype in Est-deficient ob/ob mice (obe mice). Mechanistically, adipose reconstitution of Est in obe mice (oae mice) results in reduced local and systemic inflammation, improved insulin sensitivity, and increased energy expenditure. At the molecular level, adipose induction of lipocalin-2 (Lcn2) in oae males may have contributed to the inhibition of inflammation because the level of Lcn2 is negatively associated with tumor necrosis factor (TNF) alpha expression, and treatment of differentiated adipocytes with Lcn2 antagonizes TNFalpha-responsive inhibition of insulin signaling. The metabolic benefit of adipose reconstitution of Est is sex specific, because adipose reconstitution of Est in obe females has little effect. Interestingly, despite their improved metabolic functions, obe male mice with reconstituted Est in their adipose tissue fail to ameliorate the impairment of the structure and function of the pancreatic islets
malfunction
oxidative stress has a vital role in E2 regulation and can structurally modify or alter the expression level of E2 metabolizing proteins. As such, estrogen receptors lose their DNA binding ability and thus impairing transcription. The estradiol binding site gets blocked in estrogen sulfotransferase under oxidative stress
malfunction
reduced SULT1E1 expression is observed in MCF-7 cells, breast tumour tissue also exhibits elevated E2 concentrations as compared to the surrounding
malfunction
the expression of Est is markedly induced in the liver but not in the lung of female mice subject to Hemorrhagic shock (HS), a potential life-threatening condition that may lead to injury to multiple organs, including the lung, and resuscitation. Genetic ablation or pharmacological inhibition of Est effectively protects female mice from HS-induced acute lung injury (ALI), including interstitial edema, neutrophil mobilization and infiltration, and inflammation. The pulmonoprotective effect of Est ablation or inhibition is sex-specific, because the HS-induced ALI is not affected in male Est-/- mice. Mechanistically, the pulmonoprotective phenotype in female Est-/- mice is accompanied by increased lung and circulating levels of estrogens, attenuated pulmonary inflammation, and inhibition of neutrophil (PMN) mobilization from the bone marrow and neutrophil infiltration to the lung, whereas the pulmonoprotective effect is abolished upon ovariectomy, the protection is estrogen-dependent. The pulmonoprotective effect of Est ablation was also tissue specific, as loss of Est had little effect on HS-induced liver injury. Transgenic reconstitution of human EST in the liver of global Est-/- mice abolishes the pulmonoprotective effect, suggesting that it is the EST in the liver that sensitizes mice to HS-induced ALI. The enzyme inhibitor triclosan can trigger colonic inflammation in mice, so it is possible triclosan may have also induced mild inflammation in the lung and and have caused a mild induction of the total BALF protein level in the sham group
malfunction
-
the expression of Est is markedly induced in the liver but not in the lung of female mice subject to Hemorrhagic shock (HS), a potential life-threatening condition that may lead to injury to multiple organs, including the lung, and resuscitation. Genetic ablation or pharmacological inhibition of Est effectively protects female mice from HS-induced acute lung injury (ALI), including interstitial edema, neutrophil mobilization and infiltration, and inflammation. The pulmonoprotective effect of Est ablation or inhibition is sex-specific, because the HS-induced ALI is not affected in male Est-/- mice. Mechanistically, the pulmonoprotective phenotype in female Est-/- mice is accompanied by increased lung and circulating levels of estrogens, attenuated pulmonary inflammation, and inhibition of neutrophil (PMN) mobilization from the bone marrow and neutrophil infiltration to the lung, whereas the pulmonoprotective effect is abolished upon ovariectomy, the protection is estrogen-dependent. The pulmonoprotective effect of Est ablation was also tissue specific, as loss of Est had little effect on HS-induced liver injury. Transgenic reconstitution of human EST in the liver of global Est-/- mice abolishes the pulmonoprotective effect, suggesting that it is the EST in the liver that sensitizes mice to HS-induced ALI. The enzyme inhibitor triclosan can trigger colonic inflammation in mice, so it is possible triclosan may have also induced mild inflammation in the lung and and have caused a mild induction of the total BALF protein level in the sham group
-
malfunction
-
impairment in the hepatic estrogen sulfotransferase (SULT1E1) protein expression are noticed with interfered hepatic free-thiols only in a N-ethyl-N-nitrosourea (ENU) and a xenograft-estradiol (E2) group compared to the arsenic group. Impairment of SULT1E1 expression and E2 regulations through oxidant-stress signalling. Oxidative stress has a vital role in E2 regulation and can structurally modify or alter the expression level of E2 metabolizing proteins. As such, estrogen receptors lose their DNA binding ability and thus impairing transcription. The estradiol binding site gets blocked in estrogen sulfotransferase under oxidative stress
-
malfunction
-
EST ablation produces completely opposite metabolic phenotype in female and male obese mice. Male Est-/- mice develop age-dependent Leydig cell hypertrophy/hyperplasia and impaired steroidogenesis, have reduced total and forward sperm motility, and produce smaller litters compared with age-matched wild-type males. In female mice, ablation of the mouse Sult1e1 gene causes placental thrombosis and spontaneous fetal loss, which is associated with elevated free estrogen levels in the circulation and the amniotic fluid. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). The activation of GR can lead to hyperglycemia in genetically obese viable yellow (Avy) female mice due to an aberrant shift in hepatic androgen/ estrogen balance. Castration of male mice abolishes EST expression in the epididymal fat, whereas testosterone supplementation restores it. Although EST expression can be induced in the parametrial fat of female mice, whole body ablation of EST does not cause any differences in fat indices (fat weight normalized to body weight) between female WT and EST-/- mice. EST-/- male mice have their epididymal and inguinal fat indices significantly higher than those of the wild-type mice. Adipocyte size in EST-/- male mice is markedly larger than that of wild-type mice, but under chow diet, these changes are not accompanied by obvious metabolic abnormalities. EST loss in obese males worsens metabolic phenotype. Female obe mice exhibit completely opposite metabolic phenotypes. Whole body loss of EST expression in the ob/ob background decreases hepatic gluconeogenesis and lipogenesis, improves body composition and insulin sensitivity, and increases energy expenditure. Ablation of EST in female ob/ob mice does not affect WAT inflammation
-
malfunction
-
loss of Est in male ob/ob mice, but not in female ob/ob mice, exacerbates the diabetic phenotype. Transgenic reconstitution of Est in the adipose tissue, but not in the liver, attenuates diabetic phenotype in Est-deficient ob/ob mice (obe mice). Mechanistically, adipose reconstitution of Est in obe mice (oae mice) results in reduced local and systemic inflammation, improved insulin sensitivity, and increased energy expenditure. At the molecular level, adipose induction of lipocalin-2 (Lcn2) in oae males may have contributed to the inhibition of inflammation because the level of Lcn2 is negatively associated with tumor necrosis factor (TNF) alpha expression, and treatment of differentiated adipocytes with Lcn2 antagonizes TNFalpha-responsive inhibition of insulin signaling. The metabolic benefit of adipose reconstitution of Est is sex specific, because adipose reconstitution of Est in obe females has little effect. Interestingly, despite their improved metabolic functions, obe male mice with reconstituted Est in their adipose tissue fail to ameliorate the impairment of the structure and function of the pancreatic islets
-
metabolism
estrogen sulfotransferase SULT1E1 regulates inflammatory response and lipid metabolism of human endothelial cells via proliferator-activated receptor gamma
metabolism
both SULT1E1 and SULT2A1 can play important roles in steroid signaling through regulation of the active forms of the hormones
metabolism
in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Further activation of estrone to the most potent estrogen, estradiol, is catalyzed by 17-ketosteroid reductases, while estradiol can also be formed from dehydroepiandrosterone by the sequential actions of 3beta-hydroxysteroid dehydrogenase-DELTA4-isomerase, aromatase, and 17-ketosteroid reductase. Roles of the STS and SULT enzymes in local estrogen biosynthesis, overview
metabolism
interdependence between estrogen sulfotransferase (SULT1E1) and nuclear transcription factor Nrf-2, Nrf2 an oxidative stress responsive transcription protein, regulations via oxidative stress in breast cancer. Human estrogen sulfotransferase (SULT1E1) and nuclear factor erythroid 2-related factor 2 (Nrf-2) expressions influence each other in advanced human breast carcinogenesis. The difference in the metabolism of estradiol (E2) in pre- and postmenopausal women is connected with post-menopausal breast cancer. A synergism between reactive oxygen species (ROS) production and E2 generation is demonstrated. ROS dependent regulation of Nrf-2 is one of the most important determinants of E2 regulation by altering SULT1E1 expression. Oxidative stress is the link between SULT1E1 and Nrf2 expression
metabolism
sulfonation and desulfation are two opposing processes that represent an important layer of regulation of estrogenic activity via ligand supplies. Enzymatic activities of families of enzymes, known as sulfotransferases and sulfatases, lead to structural and functional changes of the steroids, thyroids, xenobiotics, and neurotransmitters. Estrogen sulfotransferase (EST) and steroid sulfatase (STS, EC 3.1.6.2) represent negative and positive regulation of the estrogen activity, respectively. This is because EST-mediated sulfation deactivates estrogens, whereas STS-mediated desulfation converts the inactive estrogen sulfates to active estrogens. Sex-dependent role of estrogen sulfotransferase and steroid sulfatase in metabolic homeostasis
metabolism
sulfonation and desulfation are two opposing processes that represent an important layer of regulation of estrogenic activity via ligand supplies. Enzymatic activities of families of enzymes, known as sulfotransferases and sulfatases, lead to structural and functional changes of the steroids, thyroids, xenobiotics, and neurotransmitters. Estrogen sulfotransferase (EST) and steroid sulfatase (STSEC 3.1.6.2) represent negative and positive regulation of the estrogen activity, respectively. This is because EST-mediated sulfation deactivates estrogens, whereas STS-mediated desulfation converts the inactive estrogen sulfates to active estrogens. Sex-dependent role of estrogen sulfotransferase and steroid sulfatase in metabolic homeostasis
metabolism
-
sulfonation and desulfation are two opposing processes that represent an important layer of regulation of estrogenic activity via ligand supplies. Enzymatic activities of families of enzymes, known as sulfotransferases and sulfatases, lead to structural and functional changes of the steroids, thyroids, xenobiotics, and neurotransmitters. Estrogen sulfotransferase (EST) and steroid sulfatase (STS, EC 3.1.6.2) represent negative and positive regulation of the estrogen activity, respectively. This is because EST-mediated sulfation deactivates estrogens, whereas STS-mediated desulfation converts the inactive estrogen sulfates to active estrogens. Sex-dependent role of estrogen sulfotransferase and steroid sulfatase in metabolic homeostasis
-
physiological function
-
EST plays an important role in the regulation of in situ estrogen production in human breast cancer
physiological function
-
SULT1E1 is responsible for the inactivation of beta-estradiol at physiological concentrations via conjugation with sulfonate
physiological function
17beta-estradiol sulfation catalyzed by SULT1E1 plays an important role in modulating endothelial cell function
physiological function
-
estrogen sulfotransferase activity inhibits adipocyte differentiation. Enzyme overexpression in the adipose tissue of female transgenic mice results in smaller adipocyte size. Enzyme overexpression results in a sustained activation of ERK1/2 (p42/p44) MAPK and attenuates the insulin-signaling pathway
physiological function
-
estrogen sulfotransferase regulates body fat and glucose homeostasis in female mice. Enzyme overexpression decreases the differentiation of primary adipocytes, and this is associated with reductions in the expression of peroxisome proliferator-activated receptor-gamma, fatty acid synthase, hormone-sensitive lipase, lipoprotein lipase, and leptin
physiological function
transgenic overexpression of the enzyme promotes estrogen deactivation and sensitizes mice to cecal ligation and puncture-induced inflammatory response
physiological function
17beta-estradiol (E2) can contribute to the progression of epithelial ovarian cancer (EOC). Although the majority of patients with EOC are postmenopausal woman, when de novo estrogen production in the ovary has ceased, ovarian cancer cells remain exposed to estrogens synthesized locally in the cancer cells from inactive sulfonated steroid hormone precurxadsors, such as estrone sulfate taken up from the circulation via the sulfatase pathway. An abundance of the estrogen-modixadfying enzymes, including estrogen-activating steroid sulfatase (STS, EC 3.1.6.2) and estrogen-inactivating estrogen-sulfotransferase (SULT1E1), is important for providing active estrogen to EOC cells. In advanced stage high-grade serous EOC, the most frequent and lethal type of ovarian cancer, SULT1E1 expression is significantly associated with a better overall survival rate. Importance of SULT1E1-mediated estrogen inactivation in EOC, particularly high-grade serous EOC (HGSOC). Therefore, targeting the sulfatase pathway is a potenxadtial endocrine therapeutic intervention for certain patients with estrogen-responsive EOC
physiological function
estrogen sulfotransferase (EST) mediates sulfation and deactivation of estrogens. Consistent with the function of EST in estrogen sulfation and deactivation, EST plays an important role in protecting the reproductive tissue in both sexes. EST plays a role in inhibiting the estrogen-dependent growth of breast cancer cells both in vitro and in vivo through its activity in deactivating estrogens. Overexpression of EST in 3T3-L1 cells or transgenic expression of EST in the white adipose tissue (WAT) of female mice results in decreased differentiation of primary adipocytes and smaller adipocyte size, suggesting that conditional EST expression/activity in WAT has a profound effect on female adiposity, inhibitory effect of EST on adipogenesis probably resulting from the activation of ERK1/2 MAPK and inhibition of insulin signaling, which explains a blunted glucose uptake in parametrial adipose tissue during the hyperinsulinemic-euglycemic clamp in EST transgenic female mice. Although EST expression can be induced in the parametrial fat of female mice, whole body ablation of EST does not cause any differences in fat indices (fat weight normalized to body weight) between female wild-type and EST-/- mice. The obese males that have higher fasting glucose level and worse glucose tolerance performance also show impaired glucose-stimulated insulin secretion. Transgenic expression of EST in female WAT does not significantly change the mRNA expression levels of proinflammatory genes such as MCP1 and IL-beta
physiological function
estrogen sulfotransferase (EST) mediates sulfation and deactivation of estrogens. Consistent with the function of EST in estrogen sulfation and deactivation, EST plays an important role in protecting the reproductive tissue in both sexes. EST plays a role in inhibiting the estrogen-dependent growth of breast cancer cells both in vitro and in vivo through its activity in deactivating estrogens. The pro-adipogenic effect resulting from EST overexpression in primary adipose-derived stem cells (ASCs) can be mimicked by using an estrogen receptor (ER) antagonist or ER knockdown, suggesting that EST promotes adipogenesis by deactivating estrogens. Although the expression of EST can be positively associated with general adiposity or BMI scores, it does not correlate with the circulating levels of estradiol or testosterone in both men and women. EST through controlling the local availability of the estrogens has a profound effect on adipocyte metabolism and growth. Elevated EST expression in white adipose tissue (WAT) in obese men and women is significantly associated with the expression of tumor necrosis factor alpha (TNF-alpha) and suppressor of cytokine signaling-3 (SOCS3), a downstream target of TNF-alpha and a marker of inflammation. Potential inflammatory regulation of the enzyme, at least in human adipose tissues
physiological function
estrogen sulfotransferase (SULT1E) mainly catalyzes the sulfation of estrogens, which are known to prevent the pathogenesis of atherosclerosis. Human estrogen sulfotransferase and its related fluorescently labeled decapeptides specifically interact with oxidized low-density lipoprotein, peptides with a YKDG sequence specifically bind to oxidized low-density lipoprotein (Ox-LDL), which plays a major role in the pathogenesis of atherosclerosis. Ox-LDL is abundant in atherosclerotic plaques and is associated with plaque instability. Ox-LDL is believed to cause cell formation in macrophages through Ox-LDL uptake via scavenger receptors in atherosclerotic lesions
physiological function
estrogen sulfotransferase (SULT1E1) is a phase-2 drug metabolizing enzyme, it sulfonates estrogen and produces estradiol sulfate (E2S) or estrone sulfate (E1S), which are biologically inactive and unable to bind to estrogen receptor (ER)alpha or ERbeta, important role of rSULT1E1 in the regulation of estradiol (E2) metabolism, overview
physiological function
estrogen sulfotransferase (SULT1E1) is a phase-2 drug metabolizing enzyme, it sulfonates estrogen and produces estradiol sulfate (E2S) or estrone sulfate (E1S), which are biologically inactive and unable to bind to estrogen receptor (ER)alpha or ERbeta, important role of rSULT1E1 in the regulation of estradiol (E2) metabolism, overview
physiological function
Estrogen sulfotransferase catalyzes the sulfoconjugation and deactivation of estrogens. plays an important role in regulating the tissue and systemic estrogen activity. Sulfoconjugation inactivates estrogens because the sulfonated estrogens cannot bind to the estrogen receptors and they are more susceptible to urinary excretion. Sex- and tissue-specific role of estrogen sulfotransferase in energy homeostasis and insulin sensitivity. The WATexpression of Est ensures a sufficient deactivation of estrogens in males, whereas the testicular expression of Est protects the male reproductive system from estrogen toxicity. The Est expression in the adipose tissue, but not in the liver, is essential to protect mice from systemic and local inflammation and metabolic syndrome in a male-specific manner. Adipose reconstitution of Est fails to rescue the pancreatic beta cell damage in Est-deficient ob/ob (obe) male mice. Liver reconstitution of Est fails to ameliorate inflammation and diabetic phenotype in obe male mice
physiological function
in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Enzyme SULT1E1 catalyzes the conjugation of estrone (E1)
physiological function
SULT1E1 deactivates estradiol and estrone by adding a sulfate group and forming estrogen sulfate which has least addiction towards the estrogen receptor
physiological function
SULT1E1 is involved in estrogenic signaling through regulation of intracellular concentrations of the active hormone
physiological function
the estrogen sulfotransferase (EST or SULT1E1) is a conjugating enzyme that sulfonates and deactivates estrogens. Sulfonated estrogens cannot bind to and activate the estrogen receptors, therefore losing their hormonal activities. Hepatic estrogen sulfotransferase distantly sensitizes mice to hemorrhagic shock-induced acute lung injury
physiological function
-
the estrogen sulfotransferase (EST or SULT1E1) is a conjugating enzyme that sulfonates and deactivates estrogens. Sulfonated estrogens cannot bind to and activate the estrogen receptors, therefore losing their hormonal activities. Hepatic estrogen sulfotransferase distantly sensitizes mice to hemorrhagic shock-induced acute lung injury
-
physiological function
-
estrogen sulfotransferase (SULT1E1) is a phase-2 drug metabolizing enzyme, it sulfonates estrogen and produces estradiol sulfate (E2S) or estrone sulfate (E1S), which are biologically inactive and unable to bind to estrogen receptor (ER)alpha or ERbeta, important role of rSULT1E1 in the regulation of estradiol (E2) metabolism, overview
-
physiological function
-
estrogen sulfotransferase (EST) mediates sulfation and deactivation of estrogens. Consistent with the function of EST in estrogen sulfation and deactivation, EST plays an important role in protecting the reproductive tissue in both sexes. EST plays a role in inhibiting the estrogen-dependent growth of breast cancer cells both in vitro and in vivo through its activity in deactivating estrogens. Overexpression of EST in 3T3-L1 cells or transgenic expression of EST in the white adipose tissue (WAT) of female mice results in decreased differentiation of primary adipocytes and smaller adipocyte size, suggesting that conditional EST expression/activity in WAT has a profound effect on female adiposity, inhibitory effect of EST on adipogenesis probably resulting from the activation of ERK1/2 MAPK and inhibition of insulin signaling, which explains a blunted glucose uptake in parametrial adipose tissue during the hyperinsulinemic-euglycemic clamp in EST transgenic female mice. Although EST expression can be induced in the parametrial fat of female mice, whole body ablation of EST does not cause any differences in fat indices (fat weight normalized to body weight) between female wild-type and EST-/- mice. The obese males that have higher fasting glucose level and worse glucose tolerance performance also show impaired glucose-stimulated insulin secretion. Transgenic expression of EST in female WAT does not significantly change the mRNA expression levels of proinflammatory genes such as MCP1 and IL-beta
-
physiological function
-
Estrogen sulfotransferase catalyzes the sulfoconjugation and deactivation of estrogens. plays an important role in regulating the tissue and systemic estrogen activity. Sulfoconjugation inactivates estrogens because the sulfonated estrogens cannot bind to the estrogen receptors and they are more susceptible to urinary excretion. Sex- and tissue-specific role of estrogen sulfotransferase in energy homeostasis and insulin sensitivity. The WATexpression of Est ensures a sufficient deactivation of estrogens in males, whereas the testicular expression of Est protects the male reproductive system from estrogen toxicity. The Est expression in the adipose tissue, but not in the liver, is essential to protect mice from systemic and local inflammation and metabolic syndrome in a male-specific manner. Adipose reconstitution of Est fails to rescue the pancreatic beta cell damage in Est-deficient ob/ob (obe) male mice. Liver reconstitution of Est fails to ameliorate inflammation and diabetic phenotype in obe male mice
-
additional information
adipogenesis is differentially regulated by EST in murine and human adipocytes
additional information
adipogenesis is differentially regulated by EST in murine and human adipocytes
additional information
analysis of tertiary structure and reaction mechanism of the human SULT1E1 enzyme using the structure of the human SULT1E1 enzyme in complex with PAP and E2 (PDB ID 4JVL), catalytic amino acid residues His107, Lys47, and Ser137 play a role in the reaction mechanism
additional information
estradiol (E2) may be responsible for carcinogenesis in the breasts
additional information
hSULT1E1 may change its charge and structure in the presence of LDL/Ox-LDL, for example, a monomer or a dimer, likely leading to the change of biological activity of hSULT1E1
additional information
-
hSULT1E1 may change its charge and structure in the presence of LDL/Ox-LDL, for example, a monomer or a dimer, likely leading to the change of biological activity of hSULT1E1
additional information
-
adipogenesis is differentially regulated by EST in murine and human adipocytes
-
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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). ST1E1_HUMAN
294
0
35126
Swiss-Prot
other Location (Reliability: 1)
ST1E1_MOUSE
295
0
35590
Swiss-Prot
other Location (Reliability: 1)
ST1E1_RAT
295
0
35509
Swiss-Prot
other Location (Reliability: 1)
ST1E2_RAT
295
0
35365
Swiss-Prot
other Location (Reliability: 1)
ST1E3_RAT
295
0
35416
Swiss-Prot
other Location (Reliability: 1)
ST1E1_BOVIN
295
0
34640
Swiss-Prot
other Location (Reliability: 2)
ST1E1_CAVPO
296
0
35245
Swiss-Prot
other Location (Reliability: 1)
STE2_RAT
295
0
35303
Swiss-Prot
other Location (Reliability: 1)
A0A7R8H664_LEPSM
323
0
37355
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7R8CI10_LEPSM
213
0
25268
TrEMBL
other Location (Reliability: 4)
B7QJU7_IXOSC
506
0
59518
TrEMBL
other Location (Reliability: 2)
B7PAE3_IXOSC
298
0
34426
TrEMBL
Secretory Pathway (Reliability: 5)
B7QK94_IXOSC
176
1
20339
TrEMBL
other Location (Reliability: 2)
A0A7R8CHE7_LEPSM
314
0
37098
TrEMBL
other Location (Reliability: 1)
B7PWF9_IXOSC
306
0
35998
TrEMBL
other Location (Reliability: 3)
B7Q6M5_IXOSC
308
0
36187
TrEMBL
other Location (Reliability: 5)
B7P2E3_IXOSC
316
0
37288
TrEMBL
other Location (Reliability: 1)
A0A7R8CKW1_LEPSM
382
0
44720
TrEMBL
other Location (Reliability: 1)
B7PWE9_IXOSC
309
0
36068
TrEMBL
other Location (Reliability: 1)
A0A7R8H2F8_LEPSM
291
0
34587
TrEMBL
other Location (Reliability: 1)
B7Q7I4_IXOSC
164
0
19133
TrEMBL
other Location (Reliability: 2)
B7Q4F8_IXOSC
357
0
41181
TrEMBL
Secretory Pathway (Reliability: 3)
B7PH61_IXOSC
599
0
69827
TrEMBL
other Location (Reliability: 3)
A0A7R8D032_LEPSM
383
0
44897
TrEMBL
Mitochondrion (Reliability: 4)
A0A7R8CV05_LEPSM
142
0
16404
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34000
35000
67000
74800
-
meniscus depletion method, sucrose density gradient centrifugation, pH 7.0
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
hSULT1E1 is biologically active as a dimer. hSULT1E1 may change its charge and structure in the presence of LDL/Ox-LDL, for example, a monomer or a dimer, likely leading to the change of biological activity of hSULT1E1
additional information
detailed structural analysis and comparison of SULT family enzymes, comparison of substrate binding structures, overview, chemical library preparation and ligand binding screens
additional information
SULT1E1 is a dimer with an alpha/beta motif that consists of five parallel beta-strands surrounded by alpha-helices and a conserved alpha-helix across this structure
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D65N/K85E/E86K/F138Y
the mutant exhibits increased thermostability (heat inactivation at 43.4°C) compared to the wild type enzyme (42°C)
E12G/N29D/D65N/C83R/N87D/M98V/F138Y/G182S/L195M/H224K
the mutant exhibits increased thermostability (heat inactivation at 43.1°C) compared to the wild type enzyme (42°C)
E12G/N29D/F138Y/G182S/L251V
the mutant exhibits increased thermostability (heat inactivation at 51.8°C) compared to the wild type enzyme (42°C)
E12G/N29D/V73A/N87D/F138Y/G182S/L195M/E211G/E285G
the mutant exhibits increased thermostability (heat inactivation at 52.1°C) compared to the wild type enzyme (42°C)
F138Y/G182S/H224K/E285G
the mutant exhibits increased thermostability (heat inactivation at 54.6°C) compared to the wild type enzyme (42°C)
F138Y/G182S/L195M/E211G
the mutant exhibits increased thermostability (heat inactivation at 55.8°C) compared to the wild type enzyme (42°C)
H107A
-
site-directed mutagenesis, humSULT1E1, presence of a histidine residue at position 107 is essential for the production of a functional protein, substitution of this amino acid to alanine results in complete loss of activity towards all substrates tested
H224Q
-
naturally ocuring mutation in SULT1E1, genotyping in Jewish women of the Ashkenazi ethnic origin
K85E/A135T/F138Y/G182S/L251V
the mutant exhibits increased thermostability (heat inactivation at 46.3°C) compared to the wild type enzyme (42°C)
N29D/L195M/H224K/L251V
the mutant exhibits increased thermostability (heat inactivation at 48.3°C) compared to the wild type enzyme (42°C)
V73A/N87D/G182S/H224K/L251V/E285G
the mutant exhibits increased thermostability (heat inactivation at 52.8°C) compared to the wild type enzyme (42°C)
additional information
additional information
-
proliferative response of MCF-7 cells stably expressing SULT1E1 to polyphenols, overview
additional information
proliferative response of MCF-7 cells stably expressing SULT1E1 to polyphenols, overview
additional information
-
ectopic expression of SULT1E1 in MCF-7 cells suppresses the estrogen response
additional information
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MCF-7 cells stably expressing SULT1E1 show altered cellular proliferation upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1
additional information
MCF-7 cells stably expressing SULT1E1 show altered cellular proliferation upon treatment with chrysin, quercetin, or resveratrol, thus suggesting inactivation of these compounds by SULT1E1
additional information
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SULT1E1 and ID2 genes are candidates for inherited predisposition to breast and ovarian cancer in Jewish women, phenoytpes, overview
additional information
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SULT1E1 polymorphisms are risk factors for endometrial cancer susceptibility, genotyping and phenotyping, overview
additional information
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SULT1E1 transfection in CA-HPV-10 cells leads to decreased mRNA expression levels of TFRC, a cell membrane transferrin receptor gene, and increased TMEPAI mRNA levels, a gene encoding a steroid-dependent mRNA product. The estrogen-induced estrogen response element activation in CA-HPV-10 cells is repressed by SULT1E1 expression
additional information
elevated EST expression in white adipose tissue (WAT) in obese men and women is significantly associated with the expression of tumor necrosis factor alpha (TNF-alpha) and suppressor of cytokine signaling-3 (SOCS3), a downstream target of TNF-alpha and a marker of inflammation
additional information
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ectopic expression of SULT1E1 in MCF-7 cells suppresses the estrogen response
additional information
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IGF-1 message levels in cystic fibrosis transmembrane receptor (CFTR)-deficient mouse livers are positively correlated with body weight and negatively correlated with SULT1E1 activity, overexpression of SULT1E1 reduces STAT5b phosphorylation, pathway regulation, overview
additional information
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low expression of COX-2, reduced cumulus expansion, placental dysfunction, impaired ovulation, and reduced fertility in SULT1E1-deficient female mice, phenotype, overview
additional information
mice with adipose tissue (WAT) reconstitution of Est in Est-deficient ob/ob mice (oae mice) are generated by crossing the obe mice with the aP2-Est transgenic mice that express Est in the adipose tissue under the control of the aP2 gene promoter. The resulting oae mice bear the expression of Est in the adipose tissue in the background of obe. Est-deficient ob/ob mice with transgenic reconstitution of Est in liver (ole mice) are generated by crossing the obe mice with the Lap-Est transgenic mice that express Est in the liver under the control of the liver-enriched activator protein (Lap) gene promoter. The resulting ole mice bear the expression of Est in the liver in the background of obe. Adipose reconstitution of Est improves the metabolic function of obe mice in a male-specific manner, phenotypes, overview. The reduced WAT local and systemic inflammation in oae males may have been accounted for by the upregulation of Lcn2. The induction of Lcn2 is consistent with the notion that the expression of Lcn2 can be suppressed by estrogens, so the increased deactivation of estrogen in oae mice causes a desuppression of Lcn2 in the adipose tissue. The induction of Lcn2 is bothWAT specific and male specific because the liver expression of Lcn2 is comparable between the obe and oae males, and the aP2-Est transgene has little effect on the adipose expression of Lcn2 in oae females. In contrast to the notion that Lcn2 might be an inflammatory marker, a striking negative association between the WAT expression of Lcn2 and TNF-alpha is found, suggesting that Lcn2 might actually antagonize TNF-alpha as part of a negative feedback loop. Treatment of differentiated 3T3-L1 cells with Lcn2 attenuates the TNF-alpha-responsive suppression of insulin signaling, including the expression of insulin-responsive genes such as Srbep-1c and Fas. Adipose reconstitution of Est fails to rescue the pancreatic beta cell damage in obe males
additional information
the mRNA and protein expression of EST is highly induced in the livers of obese and diabetogenic leptin receptor deficient C57BL/KsJ-db/db mice. The db/db genotype does not change the constitutive expression of the enzyme in the testis. The leptin-deficient ob/ob mice as well as wild-type mice fed with Western style high-fat diet also show increased expression of EST specifically in the liver. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). The activation of GR can lead to hyperglycemia in genetically obese viable yellow (Avy) female mice due to an aberrant shift in hepatic androgen/ estrogen balance. Overexpression of EST in 3T3-L1 cells or transgenic expression of EST in the WAT of female mice results in decreased differentiation of primary adipocytes and smaller adipocyte size, suggesting that conditional EST expression/activity in WAT has a profound effect on female adiposity. Only tissue-specific or local changes in insulin sensitivity were shown in the female murine model of WAT-EST overexpression. Transgenic expression of EST in female WAT does not significantly change the mRNA expression levels of proinflammatory genes such as MCP1 and IL-beta
additional information
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the mRNA and protein expression of EST is highly induced in the livers of obese and diabetogenic leptin receptor deficient C57BL/KsJ-db/db mice. The db/db genotype does not change the constitutive expression of the enzyme in the testis. The leptin-deficient ob/ob mice as well as wild-type mice fed with Western style high-fat diet also show increased expression of EST specifically in the liver. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). The activation of GR can lead to hyperglycemia in genetically obese viable yellow (Avy) female mice due to an aberrant shift in hepatic androgen/ estrogen balance. Overexpression of EST in 3T3-L1 cells or transgenic expression of EST in the WAT of female mice results in decreased differentiation of primary adipocytes and smaller adipocyte size, suggesting that conditional EST expression/activity in WAT has a profound effect on female adiposity. Only tissue-specific or local changes in insulin sensitivity were shown in the female murine model of WAT-EST overexpression. Transgenic expression of EST in female WAT does not significantly change the mRNA expression levels of proinflammatory genes such as MCP1 and IL-beta
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additional information
-
mice with adipose tissue (WAT) reconstitution of Est in Est-deficient ob/ob mice (oae mice) are generated by crossing the obe mice with the aP2-Est transgenic mice that express Est in the adipose tissue under the control of the aP2 gene promoter. The resulting oae mice bear the expression of Est in the adipose tissue in the background of obe. Est-deficient ob/ob mice with transgenic reconstitution of Est in liver (ole mice) are generated by crossing the obe mice with the Lap-Est transgenic mice that express Est in the liver under the control of the liver-enriched activator protein (Lap) gene promoter. The resulting ole mice bear the expression of Est in the liver in the background of obe. Adipose reconstitution of Est improves the metabolic function of obe mice in a male-specific manner, phenotypes, overview. The reduced WAT local and systemic inflammation in oae males may have been accounted for by the upregulation of Lcn2. The induction of Lcn2 is consistent with the notion that the expression of Lcn2 can be suppressed by estrogens, so the increased deactivation of estrogen in oae mice causes a desuppression of Lcn2 in the adipose tissue. The induction of Lcn2 is bothWAT specific and male specific because the liver expression of Lcn2 is comparable between the obe and oae males, and the aP2-Est transgene has little effect on the adipose expression of Lcn2 in oae females. In contrast to the notion that Lcn2 might be an inflammatory marker, a striking negative association between the WAT expression of Lcn2 and TNF-alpha is found, suggesting that Lcn2 might actually antagonize TNF-alpha as part of a negative feedback loop. Treatment of differentiated 3T3-L1 cells with Lcn2 attenuates the TNF-alpha-responsive suppression of insulin signaling, including the expression of insulin-responsive genes such as Srbep-1c and Fas. Adipose reconstitution of Est fails to rescue the pancreatic beta cell damage in obe males
-
additional information
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low expression of COX-2, reduced cumulus expansion, placental dysfunction, impaired ovulation, and reduced fertility in SULT1E1-deficient female mice, phenotype, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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half-life 2 h, glycerol prevents detectable deterioration of activity over 3 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, freshly prepared adrenal cytosol loses no estrogen sulfotransferase activity during storage for periods of up to 5 months
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-20°C, partially purified enzyme exhibits large losses of activity within 1 week
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-20°C, partially purified enzyme may be stored for 2-3 weeks without loss of activity
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-70°C, liver cytosol, 50 mM Tris-HCl, pH 7.8, 0.25 M sucrose, 0.5 mM EDTA, 0.1 mM DTT, and 0.02 mM BHT, no loss of activity during storage
0°C, fresh cytosol retains 85% of activity after 20 days, 50% after 50 days
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0°C, partially purified A form of enzyme loses only a small percentage of its activity on standing in ice for a period of 2 weeks, B form loses 50% of its initial activity in this time
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EST cDNA cloned and expressed as fusion protein in Escherichia coli using pGEX-4T-3 and in CHO cells using eukaryotic expression vector pCDNA3
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EST cDNA inserted into the pcDNA 1 eukaryotic expression vector and transfected into COS-7 cells and expressed
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EST cloned and expressed by CHO-K1 cells stably transfected with plasmid pcDNAI/Neo eukaryotic expression vector
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EST expression analysis in healthy and endometriosis uterine endometrium showing no significant differences
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EST expression and regulation in invasive breast cancer and ductal carcinoma in situ, overview
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expressed in Escherichia coli BL21(DE3) cells
expression analysis of EST by real-time RT-PCR in prostate cancer cell lines, overview
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expression analysis of the enzyme in healthy and preinvasive and invasive tumor breast tissue
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expression of GFP-tagged SULT1E1 in HEK-293 cell cytoplasm, subcellular localization study, RT-PCR expression analysis, overview
expression of GFP-tagged SULT1E1 in HEK-293 cells, localization in the cytoplasm
expression of SULT1E1 in prostate cancer CAHPV-10 cells leading to changes in the transcriptional expression of selected signal transduction-related genes, real-time RT-PCR expression analysis, overview
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functional overexpression of SULT1E1 in Escherichia coli strain XL-1 blue cytosol
gene SULT1E1, DNA and amino acid sequence determination and analysis, localized on chromosome 5, sequence comparisons and phylogenetic analysis, gene structure and genomic organization of each cynomolgus SULTs, recombinant expression in Escherichia coli cytosol, quantitative real-time RT-PCR enzyme expression analysis
gene SULT1E1, localized to chromosome 4 (4q13.2), different transcripts and genetic variants, overview
human placental cDNA library constructed in lambda gt11, expression vector encoding estrogen sulfotransferase transfected in human adrenal adenocarcinoma SW-13 cells
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recombinant expression of the enzyme in Escherichia coli strain BL21(DE3)
stable expression of SULT1E1 in MCF-7 cells, expression of His-tagged SULT1E1 using a baculoviral-Spodoptera frugiperda Sf9 cell system
SULT1E1 expression analysis in wild-type, CFTR-DELTAF508 mutant, and CFTR-KO mice
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SULT1E1, quantitative expression analysis in benign and in primary and secondary malignant bone tumors
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SULT1E1, tissue-specific expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a confirmed repressor of EST gene in human primary hepatocytes and hepatocellular carcinoma Huh7 cells is pregnane X receptor (PXR), when the PXR is activated by rifampicin. Aryl hydrocarbon receptor (AhR) activation has also been shown to suppress EST expression
dopamine has no significant effect on enzyme expression in both sexes
enzyme activity is significantly higher in the endometrial carcinoma than in normal endometrial tissues
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enzyme expression is dramatically reduced in differentiated 3T3-L1 cells and mature primary adipocytes
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factors HNF4alpha and Nrf2 induce the expression of enzyme SULT1E1. Factor HNF4alpha is induced by oxidative stress, and factor Nrf2 is induced by estradiol via the P13K/GSK3B pathway
hemorrhagic shock (HS) induces the hepatic expression of Est in mice. The HS-responsive induction of Est may play a pathogenic role in HS-induced acute lung injury (ALI), because genetic ablation or pharmacological inhibition of Est effectively protect female mice from HS-induced ALI, whereas hepatic reconstitution of EST re-sensitized mice to HS-induced ALI
hepatic EST is also positively regulated by the liver X receptor (LXR). The induction of EST in acute inflammation in sepsis model is nuclear factor kappa-B (NF-kappaB) dependent, and EST is an NF-kappaB target gene. Inflammation and oxidative stress induce the activation of nuclear factor 2 (Nrf2), followed by the induction of EST who is a direct transcriptional target of Nrf2
in liver SULT1E1 is repressed by xenobiotic activators of the pregnane X receptor and aryl hydrocarbon receptor peroxisome proliferator
inhibition of cystic fibrosis transmembrane receptor expression in MMNK-1 cells results in the induction SULT1E1 message and activity in Hep-G2 cells
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insulin-like growth factor-1 increases SULT1E1 mRNA and SULT1E1 protein levels
L-DOPA increases recombinant enzyme expression and activity 1.9fold only in male rat liver when administered at high dose of 125 mg/kg/day
lipopolysaccharide, lipopeptide Pam3CSK4, or TLR2 induce the expression of estrogen sulfotransferase
liver has a low basal expression of Est, but the hepatic expression of Est is highly induced in the ob/ob, db/db, and HFD-induced obese mice
liver ischemia and reperfusion induce the expression of estrogen sulfotransferase
reduced SULT1E1 expression is observed in the eutopic endometrium relative to the superficial lesions as well as during the follicular phase of the menstrual cycle
rSULT1E1 expression is reduced in the liver tissues of the N-ethyl-N-nitrosourea-administered group and in the estradiol-treated group compared to the control group
SULT expression in breast cancer cells can be stimulated by promegestone, SULT1E1 expression can be controlled by progesterone during the menstrual cycle and during early pregnancy
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SULT1E1 is epigenetically regulated, as its expression is induced by the histone deacetylase inhibitor trichostatin A in MCF10A cells. In endometrial cancer cell line Ishikawa SULT1E1 is induced by steroid drug tibolone via progesterone receptor. In liver, it is activated via peroxisome proliferator activated receptor alpha and the liver X receptor
the enzyme expression is low in preadipocytes but increases upon differentiation
the increase in SULT1E1 activity results in the alteration of estradiol-regulated protein expression in cystic fibrosis liver, SULT1E1 expression in HepG2 cells is inducible by sterol mediated liver-X-receptor activation although not by progestins that induce SULT1E1 in the endometrium
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the mRNA and protein expression of EST is highly induced in the livers of obese and diabetogenic leptin receptor deficient C57BL/KsJ-db/db mice. The leptin-deficient ob/ob mice as well as wild-type mice fed with Western style high-fat diet also show increased expression of EST specifically in the liver. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). Although the basal expression of Est in the female mouse WAT is low, it can be induced in the parametrial fat by testosterone treatment. The induction of EST expression by testosterone in female mice is WAT specific, because testosterone treatment fails to induce the expression of EST in the liver. The xenobiotic nuclear receptor, constitutive androstane receptor (CAR), induces the expression of EST in the mouse liver in response to diallyl sulfide (DAS) treatment. Environmental pollutants such as dioxin, polychlorinated biphenyl 153, or bisphenol A have also been reported to induce the hepatic expression of EST in a sex-specific manner. Another inducer of EST expression is hypoxia and oxidative stress as shown in the mouse model of liver ischemia and reperfusion (I/R) injury. Inflammation and oxidative stress induce the activation of nuclear factor 2 (Nrf2), followed by the induction of EST who is a direct transcriptional target of Nrf2
there are significantly higher mRNA levels in ectopic endometrium of deep infiltrating endometriosis, when compared to the normal endometrium. The enzyme expression is upregulated in endometrial cancer
hemorrhagic shock (HS) induces the hepatic expression of Est in mice. The HS-responsive induction of Est may play a pathogenic role in HS-induced acute lung injury (ALI), because genetic ablation or pharmacological inhibition of Est effectively protect female mice from HS-induced ALI, whereas hepatic reconstitution of EST re-sensitized mice to HS-induced ALI
hemorrhagic shock (HS) induces the hepatic expression of Est in mice. The HS-responsive induction of Est may play a pathogenic role in HS-induced acute lung injury (ALI), because genetic ablation or pharmacological inhibition of Est effectively protect female mice from HS-induced ALI, whereas hepatic reconstitution of EST re-sensitized mice to HS-induced ALI
-
-
liver has a low basal expression of Est, but the hepatic expression of Est is highly induced in the ob/ob, db/db, and HFD-induced obese mice
liver has a low basal expression of Est, but the hepatic expression of Est is highly induced in the ob/ob, db/db, and HFD-induced obese mice
-
-
rSULT1E1 expression is reduced in the liver tissues of the N-ethyl-N-nitrosourea-administered group and in the estradiol-treated group compared to the control group
rSULT1E1 expression is reduced in the liver tissues of the N-ethyl-N-nitrosourea-administered group and in the estradiol-treated group compared to the control group
-
-
the mRNA and protein expression of EST is highly induced in the livers of obese and diabetogenic leptin receptor deficient C57BL/KsJ-db/db mice. The leptin-deficient ob/ob mice as well as wild-type mice fed with Western style high-fat diet also show increased expression of EST specifically in the liver. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). Although the basal expression of Est in the female mouse WAT is low, it can be induced in the parametrial fat by testosterone treatment. The induction of EST expression by testosterone in female mice is WAT specific, because testosterone treatment fails to induce the expression of EST in the liver. The xenobiotic nuclear receptor, constitutive androstane receptor (CAR), induces the expression of EST in the mouse liver in response to diallyl sulfide (DAS) treatment. Environmental pollutants such as dioxin, polychlorinated biphenyl 153, or bisphenol A have also been reported to induce the hepatic expression of EST in a sex-specific manner. Another inducer of EST expression is hypoxia and oxidative stress as shown in the mouse model of liver ischemia and reperfusion (I/R) injury. Inflammation and oxidative stress induce the activation of nuclear factor 2 (Nrf2), followed by the induction of EST who is a direct transcriptional target of Nrf2
the mRNA and protein expression of EST is highly induced in the livers of obese and diabetogenic leptin receptor deficient C57BL/KsJ-db/db mice. The leptin-deficient ob/ob mice as well as wild-type mice fed with Western style high-fat diet also show increased expression of EST specifically in the liver. The expression of EST can also be stimulated in the liver by dexamethasone through the activation of the glucocorticoid receptor (GR). Although the basal expression of Est in the female mouse WAT is low, it can be induced in the parametrial fat by testosterone treatment. The induction of EST expression by testosterone in female mice is WAT specific, because testosterone treatment fails to induce the expression of EST in the liver. The xenobiotic nuclear receptor, constitutive androstane receptor (CAR), induces the expression of EST in the mouse liver in response to diallyl sulfide (DAS) treatment. Environmental pollutants such as dioxin, polychlorinated biphenyl 153, or bisphenol A have also been reported to induce the hepatic expression of EST in a sex-specific manner. Another inducer of EST expression is hypoxia and oxidative stress as shown in the mouse model of liver ischemia and reperfusion (I/R) injury. Inflammation and oxidative stress induce the activation of nuclear factor 2 (Nrf2), followed by the induction of EST who is a direct transcriptional target of Nrf2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
pharmacology
synthesis
generation of a complete set of recombinant fission yeast strains each expressing one of the 14 human SULT enzymes. The intracellular production of the cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) necessary for SULT activity is sufficiently high to support metabolite production
analysis
a modified variant of sulfotransferase assay employs permeabilized fission yeast cells (enzyme bags). A new and convenient SULT activity assay is based on the sulfation of a proluciferin compound, which is catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1
analysis
N-terminally fluorescein isothiocyanate (FITC)-labeled decapeptide (MIYKEGDVEK, FITC-hSULT1E1-P10) corresponding to residues 59-68 of hSULT1E1 can be used as an efficient fluorescent probe for the detection of Ox-LDL, LPC, and PAF, which could facilitate the mechanistic study, identification, diagnosis, prevention, and treatment of atherosclerosis
medicine
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diagnosis of atherosclerotic changes, enzymatic distribution and involvement in the development and pathogenesis of atherosclerosis is different between males and females
medicine
development of flavonoid, isoflavonoid and phenolic inhibitors of the bioactivation of carcinogens by the enzyme
medicine
-
formation of inactive estrogen sulfates can cause a reduction in the estrogenic environment which confers a beneficial effect to Org OD14 reducing the risk of breast tumours in long-term hormone replacement treatment
medicine
-
the steroid sulfatase/estrogen sulfotransferase status of carcinoma tissue determines intratumoral estrogen levels and can be a significant prognostic factor in colon carcinoma
medicine
-
enzyme immunoreactivity is inversely correlated with tumor size or lymph node status in the invasive breast carcinoma, and is also significantly associated with a decreased risk of recurrence or improved prognosis of the patients. Ovarian cancer patients with higher enzyme activity are significantly associated with shorter progression-free survival than those with lower enzyme activity
medicine
inhibition of estrogen sulfotransferase, at least in females, represents an effective approach to manage hepatic ischemia and reperfusion injury
medicine
there is a positive correlation between the enzyme expression and body mass index
medicine
pharmacological inhibition of EST may represent an effective approach to manage hemorrhagic shock-induced acute lung injury (ALI)
medicine
-
pharmacological inhibition of EST may represent an effective approach to manage hemorrhagic shock-induced acute lung injury (ALI)
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pharmacology
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reactivation of endogenous SULT1E1 gene expression may represent a novel therapeutic strategy to inhibit estrogen-dependent growth of breast cancer cells
pharmacology
-
reactivation of endogenous SULT1E1 gene expression may represent a novel therapeutic strategy to inhibit estrogen-dependent growth of breast cancer cells
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Release 2023.1 (January 2023)
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