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Information on EC 2.8.2.15 - steroid sulfotransferase
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EC Tree
2.8.2.15 steroid sulfotransferaseIUBMB Comments
Broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase, but also acts on estrone.
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Word Map
- 2.8.2.15
-
sulfotransferases
- dheas
- hydroxysteroids
-
sults
- pregnenolone
-
sulfatase
- oxysterols
- 3beta-hydroxysteroids
- 3'-phosphoadenosine-5'-phosphosulfate
-
reticularis
- estrone
- 3-sulfate
-
sulfurylation
-
sulfoconjugation
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
sult2b1b, sult2b1, dhea-st, hsult2a1, cholesterol sulfotransferase, sult2a, steroid sulfotransferase, dhea sulfotransferase, st2b2, sulfotransferase ii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cholesterol sulfotransferase
cytosolic sulfotransferase
hydroxysteroid sulfotransferase
phenol sulfotransferase
steroid alcohol sulfotransferase
-
-
-
-
steroid/bile acid-sulfotransferase
sulfotransferase II
SULT2A1
SULT2B1
additional information
SULT2A1
-
-
additional information
-
SULT2A1 belongs to the family of phenol sulfotransferases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate
3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate
broad specificity
-
-
-
3'-phosphoadenylyl sulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate
broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase, but also acts on estrone
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase
Broad specificity resembling EC 2.8.2.2 alcohol sulfotransferase, but also acts on estrone.
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CAS REGISTRY NUMBER
COMMENTARY
9032-76-2
-
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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
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-hydroxytibolone 3-O-sulfate
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-hydroxytibolone 3-O-sulfate
3'-phosphoadenylyl sulfate + 4'-hydroxy-2,3',4,5'-tetrachlorobiphenyl
adenosine 3',5'-bisphosphate + 4'-hydroxy-2,3',4,5'-tetrachlorobiphenyl 4'-O-sulfate
-
i.e. 4'-OH PCB 68, substrate of SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + 4-androstene-3,17-dione
adenosine 3',5'-bisphosphate + 3-O-sulfo-3,5-androstadien-3-ol-17-one
-
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxy-2',3,5-trichlorobiphenyl
adenosine 3',5'-bisphosphate + 2',3,5-trichlorobiphenyl-4-yl hydrogen sulfate
-
i.e. 4-OH PCB 34, substrate of SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + 5alpha,6alpha-epoxycholesterol
adenosine 3',5'-bisphosphate + 5alpha,6alpha-epoxycholesteryl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 5beta,6beta-epoxycholesterol
adenosine 3',5'-bisphosphate + 5beta,6beta-epoxycholesteryl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 6beta-hydroxytestosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 7-oxo-cholesterol
adenosine 3',5'-bisphosphate + 7-oxo-cholesteryl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 7alpha-hydroxycholesterol
adenosine 3',5'-bisphosphate + 7alpha-hydroxycholesteryl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 7beta-hydroxycholesterol
adenosine 3',5'-bisphosphate + 7beta-hydroxycholesteryl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + aldosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + cortisol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + cortisone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
3'-phosphoadenylyl sulfate + oxysterol
adenosine 3',5'-bisphosphate + oxysterol sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
3'-phosphoadenylyl sulfate + progesterone
adenosine 3',5'-bisphosphate + progesterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + taurolithocholate
adenosine 3',5'-bisphosphate + taurolithocholate 3-sulfate
3'-phosphoadenylyl sulfate + testosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + (22S,23S)-28-homobrassinolide
adenosine 3',5'-bisphosphate + (22S,23S)-28-homobrassinolide sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + (22S,23S)-28-homocastasterone
adenosine 3',5'-bisphosphate + (22S,23S)-28-homocastasterone sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 11-deoxycorticosterone
adenosine 3',5'-bisphosphate + 11-deoxycorticosterone sulfate
-
21-hydroxypregn-4-en-3,20-dione
pregn-4-en-3-one 21-sulfate
r
3'-phosphoadenylylsulfate + 16-hydroxy-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 17alpha-ethynylestradiol
adenosine 3',5'-bisphosphate + 17alpha-ethynylestradiol 3-sulfate
-
celecoxib switches sulfation from the 3-O-position to the 17beta-O-position
-
-
?
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol-17beta 3-sulfate
3'-phosphoadenylylsulfate + 17beta-estradiol 3-methyl ether
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-hydroxy-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 24-epibrassinolide
adenosine 3',5'-bisphosphate + 24-epibrassinolide sulfate
-
sulfonation leads to the loss of biological activity
-
-
r
3'-phosphoadenylylsulfate + 24-epicastasterone
adenosine 3',5'-bisphosphate + 24-epicastasterone 3-sulfate
3'-phosphoadenylylsulfate + 24-epicastasterone
adenosine 3',5'-bisphosphate + 24-epicastasterone sulfate
3'-phosphoadenylylsulfate + 24-epiteasterone
adenosine 3',5'-bisphosphate + 24-epiteasterone 3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 24-epiteasterone
adenosine 3',5'-bisphosphate + 24-epiteasterone sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 3,3',5-triidothyronine
adenosine 3',5'-bisphosphate + 3,3',5-triiodothyronine 4'-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
3'-phosphoadenylylsulfate + 3beta-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
3'-phosphoadenylylsulfate + 4'-hydroxy-2',3,4-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4'-hydroxy-2,3',4-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-2',3,5-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-2,4'-dichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,3',5-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,3'-dichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 5alpha-androst-16-en-3beta-ol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 6-deoxo-24-epicastasterone
adenosine 3',5'-bisphosphate + 6-deoxo-24-epicastasterone sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + allopregnanolone
adenosine 3',5'-bisphosphate + allopregnanolone sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + allopregnenolone
adenosine 3',5'-bisphosphate + allopregnenolone sulfate
3'-phosphoadenylylsulfate + androst-5-ene-3beta,17beta-diol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + androst-5-ene-3beta17alpha-diol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + androstenediol
adenosine 3',5'-bisphosphate + 17beta-hydroxy-androst-5-en-3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + androstenediol
adenosine 3',5'-bisphosphate + ?
SULT2B1 isoform
-
-
r
3'-phosphoadenylylsulfate + androsterone
adenosine 3',5'-bisphosphate + 5alpha-androstane-17-one 3-sulfate
3'-phosphoadenylylsulfate + beta-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + butylated hydroxy anisole
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + catechin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + chlorogenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol sulfate
-
sulfurylated at low rate
-
-
r
3'-phosphoadenylylsulfate + cortisol
adenosine 3',5'-bisphosphate + cortisol sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylylsulfate + diethylstilbestrol
adenosine 3',5'-bisphosphate + diethylstilbestrol sulfate
-
synthetic estrogen
-
r
3'-phosphoadenylylsulfate + epigallocatechin gallate
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + epitestosterone
adenosine 3',5'-bisphosphate + epitestosterone sulfate
-
17alpha-hydroxyandrost-4-en-3-one
androst-4-en-3-one 17-sulfate
r
3'-phosphoadenylylsulfate + estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + etiocholanone
adenosine 3',5'-bisphosphate + etiocholanone sulfate
3'-phosphoadenylylsulfate + kaempferol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + myricetin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + n-propyl gallate
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregn-5-en-20-one 3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
3'-phosphoadenylylsulfate + thyroxine
adenosyl 3',5'-bisphosphate + O-[3,5-diiodo-4-(sulfooxy)phenyl]-3,5-diiodotyrosine
-
-
-
?
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 + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-hydroxytibolone 3-O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-hydroxytibolone 3-O-sulfate
-
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 + 3beta-hydroxytibolone 3-O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-hydroxytibolone 3-O-sulfate
-
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
-
-
-
-
?
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-O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
preferred substrate
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
variant haplotypes in tissues possessing alterations in activity or stability may alter the plasma levels of dehydroepiandrosterone and dehydroepiandrosterone sulfate thereby altering the conversion of dehydroepiandrosterone in tissues, overview
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
i.e. DHEA, substrate of SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + taurolithocholate
adenosine 3',5'-bisphosphate + taurolithocholate 3-sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + taurolithocholate
adenosine 3',5'-bisphosphate + taurolithocholate 3-sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 17alpha-estradiol
adenosine 3',5'-bisphosphate + ?
-
estra-1,3,5(10)-triene-3,17alpha-diol
-
-
r
3'-phosphoadenylylsulfate + 17alpha-estradiol
adenosine 3',5'-bisphosphate + ?
-
estra-1,3,5(10)-triene-3,17alpha-diol
-
-
r
3'-phosphoadenylylsulfate + 17alpha-estradiol
adenosine 3',5'-bisphosphate + ?
-
estra-1,3,5(10)-triene-3,17alpha-diol
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
3alphaHST isoform
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
chorion enzyme catalyzes sulfation of estradiol at about double the velocity of estrone
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
estra-1,3,5(10)-triene-3,17alpha-diol
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
estra-1,3,5(10)-triene-3,17alpha-diol
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
estra-1,3,5(10)-triene-3,17alpha-diol
-
-
r
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol-17beta 3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + estradiol-17beta 3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 24-epicastasterone
adenosine 3',5'-bisphosphate + 24-epicastasterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 24-epicastasterone
adenosine 3',5'-bisphosphate + 24-epicastasterone 3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 24-epicastasterone
adenosine 3',5'-bisphosphate + 24-epicastasterone sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 24-epicastasterone
adenosine 3',5'-bisphosphate + 24-epicastasterone sulfate
-
highest affinity
-
-
r
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
3alphaHST isoform
-
r
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
androsterone
androsterone sulfate
r
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
androsterone
androsterone sulfate
r
3'-phosphoadenylylsulfate + 3alpha-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
androsterone
androsterone sulfate
r
3'-phosphoadenylylsulfate + 3beta-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
SULT2B1 isoform
-
r
3'-phosphoadenylylsulfate + 3beta-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
epiandrosterone
-
r
3'-phosphoadenylylsulfate + 3beta-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
epiandrosterone
-
r
3'-phosphoadenylylsulfate + 3beta-hydroxy-5alpha-androstan-17-one
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
epiandrosterone
-
r
3'-phosphoadenylylsulfate + allopregnenolone
adenosine 3',5'-bisphosphate + allopregnenolone sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + allopregnenolone
adenosine 3',5'-bisphosphate + allopregnenolone sulfate
-
3alphaHST isoform
-
r
3'-phosphoadenylylsulfate + androsterone
adenosine 3',5'-bisphosphate + 5alpha-androstane-17-one 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + androsterone
adenosine 3',5'-bisphosphate + 5alpha-androstane-17-one 3-sulfate
-
enzyme is an androsterone sulfotransferase as well as a dehydroepiandrosterone sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
SULT2B1b, concentration-dependent induction by Ca2+
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
SULT2B1b
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate
-
enzyme is an androsterone sulfotransferase as well as a dehydroepiandrosterone sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
3betaHST isoform
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
SULT2B1 isoform
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
3beta-hydroxyandrost-5-en-17-one
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
isoform SULT2B1 is capable of regulating the activity of adrenal androgens via their inactivation by sulfation
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
conversion of steroids to their inactive sulfated forms, plays a major role in the control of estrogen levels in target tissues
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
sulfation is an important pathway for biotransformation and inactivation of drugs, xenobiotics, monoamine and catecholamine neurotransmitters and steroid hormones
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
best substrate
-
-
?
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
-
major pathway in the metabolism of steroid hormones
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
enzymatic sulfation of steroids
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estriol
adenosine 3',5'-bisphosphate + estriol sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
estra-1,3,5(10)-trien-17-one 3-sulfate
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
estra-1,3,5(10)-trien-17-one 3-sulfate
r
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + etiocholanone
adenosine 3',5'-bisphosphate + etiocholanone sulfate
-
3alpha-hydroxy-5beta-androstan-17-one
5beta-androstan-17-one 3-sulfate
r
3'-phosphoadenylylsulfate + etiocholanone
adenosine 3',5'-bisphosphate + etiocholanone sulfate
-
3alpha-hydroxy-5beta-androstan-17-one
5beta-androstan-17-one 3-sulfate
r
3'-phosphoadenylylsulfate + etiocholanone
adenosine 3',5'-bisphosphate + etiocholanone sulfate
-
3alpha-hydroxy-5beta-androstan-17-one
5beta-androstan-17-one 3-sulfate
r
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + ?
-
-
-
r
3'-phosphoadenylylsulfate + glycolithocholate
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + glycolithocholate
adenosine 3',5'-bisphosphate + ?
-
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
3betaHST isoform
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
pregn-5-en-20-one 3-sulfate
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
pregn-5-en-20-one 3-sulfate
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
SULT2B1 isoform
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
3beta-hydroxypregn-5-en-20-one
pregn-5-en-20-one 3-sulfate
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
pregn-5-en-20-one 3-sulfate
r
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
3alphaHST isoform
only 3alpha-hydroxysteroid isoform, 3beta-hydroxysteroid isoform exhibits no TST activity
r
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
17beta-hydroxyandrost-4-en-3-one
androst-4-en-3-one 17-sulfate
r
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
17beta-hydroxyandrost-4-en-3-one
androst-4-en-3-one 17-sulfate
r
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
17beta-hydroxyandrost-4-en-3-one
androst-4-en-3-one 17-sulfate
r
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
-
-
r
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone sulfate
-
-
-
r
additional information
?
-
-
little or no activity with brassinolide, (22S,23R)-28-homobrassinolide, and 22-deoxy-24-epiteasterone
-
-
?
additional information
?
-
BNST4 is an ethanol-inducible steroid sulfotransferase
-
-
?
additional information
?
-
-
very limited sulfotransferase activity against dehydroepiandrosterone, testosterone and pregnenolone
-
-
?
additional information
?
-
-
isoform SULT2B1, no activity detected towards testosterone, dihydrotestosterone, dexamethasone, beta-estradiol, cholesterol, cortisol, androsterone, or p-nitrophenol, no antibody reaction with EST, P-PST-1, M-PST, DHEA-ST, or ST1B2 during immunoblot analysis
-
-
?
additional information
?
-
isoform SULT2B1, no activity detected towards testosterone, dihydrotestosterone, dexamethasone, beta-estradiol, cholesterol, cortisol, androsterone, or p-nitrophenol, no antibody reaction with EST, P-PST-1, M-PST, DHEA-ST, or ST1B2 during immunoblot analysis
-
-
?
additional information
?
-
isoform SULT2B1, no activity detected towards testosterone, dihydrotestosterone, dexamethasone, beta-estradiol, cholesterol, cortisol, androsterone, or p-nitrophenol, no antibody reaction with EST, P-PST-1, M-PST, DHEA-ST, or ST1B2 during immunoblot analysis
-
-
?
additional information
?
-
-
little or no activity with pregn-4-ene-11beta,21-diol-3,20-dione/cortisol and oestra-1,3,5(10)-triene-3,17beta-diol-3 methyl ether/17beta-oestradiol-3 methyl ether
-
-
?
additional information
?
-
-
specific for endogenous and xenobiotic estrogens
-
-
?
additional information
?
-
-
no activity towards p-nitrophenol or dopamine
-
-
?
additional information
?
-
-
presence of SULT2b1b suggests a role in the regulation of local steroid hormone synthesis and metabolism
-
-
?
additional information
?
-
-
sulfotransferase 2B1b is selective for the sulfation of 3beta-hydroxysteroids such as dehydroepiandrosterone, pregnenolone and cholesterol
-
-
?
additional information
?
-
-
the SULT2B1 isoforms are highly selective for the sulfation of 3-hydroxysteroids
-
-
?
additional information
?
-
-
hydroxylated polychlorinated biphenyls may compete with other xenobiotic substrates as well as endogenous substrates for SULT2A1
-
-
?
additional information
?
-
-
SULT2A1 is a liver- and intestine-specific sulfo-conjugating enzyme that converts the alcoholic OH of neutral steroids, bile acids, and drugs to water-soluble sulfated metabolites, regulation, overview
-
-
?
additional information
?
-
-
SULT2A1 plays a very important role in formation of steroid sulfate esters, and sulfates both 3alpha- and 3beta-hydroxysteroids, estrogens, testosterone, and aliphatic hydroxyl-containing drugs and xenobiotics
-
-
?
additional information
?
-
-
SULT2A1 plays a very important role in sulfating endogenous hydroxysteroids and exogenousxenobiotics
-
-
?
additional information
?
-
-
the enzyme promotes phase II metabolism through its sulfonating action on certain endobiotics, including steroids and bile acids, and on diverse xenobiotics, including therapeutics drugs, regulation of enzyme expression involving HNF4alpha, overview
-
-
?
additional information
?
-
-
the nuclear receptors constitutive androstane receptor CAR and retinoid X receptor alpha RXRalpha are involved in regulation of SULT2A1 enzyme expression, regulation mechanism, overview
-
-
?
additional information
?
-
-
SULT2B1b catalyzes the sulfation of 3beta-hydroxysteroids and functions as a selective cholesterol and oxysterol sulfotransferase
-
-
?
additional information
?
-
the enzyme shows selectivity for sulfation of 3beta-hydroxysteroids and demonstrates little activity with 3alpha-hydroxysteroids and estrogens
-
-
?
additional information
?
-
-
the enzyme shows selectivity for sulfation of 3beta-hydroxysteroids and demonstrates little activity with 3alpha-hydroxysteroids and estrogens
-
-
?
additional information
?
-
enzyme SULT2A1 sulfates the 3alpha- or 3beta-hydroxyl group of hydroxysteroids, as well as the 17-hydroxyl group of testosterone. SULT2A1 can also sulfate 24-hydroxyl group of hydroxycholesterol, and mediate the N-sulfoconjugation of quinolones and other amine drugs in human liver
-
-
-
additional information
?
-
product identification by mass spectrometry analysis. No activity with 1,4-androstadiene-3,17-dione, which contains an additional 1,2-double bond in the A ring in contrast to 4-androstene-3,17-dione. Substrate specificity with DELTA4-3-keto steroids , overview. Cortisone, cortisol, aldosterone, testosterone, and 6beta-hydroxytestosterone contain both a hydroxyl group as well as a 3-carbonyl group. Whether the 3-carbonyl group in these compounds, in addition to the 3beta-hydroxyl group, can also be sulfated by SULT2A1 remains to be clarified
-
-
-
additional information
?
-
-
Sult2a is involved in 3alpha-sulfation of bile acids, e.g. of litocholic acid, required for enhanced faecal excretion of bile acid in hydroxysteroid sulfotransferase-mediated protection against lithocholic acid-induced liver toxicity, overview
-
-
?
additional information
?
-
-
Sult2A1 converts bile acids, steroids and a number of drugs to the corresponding sulfated metabolites, which are readily eliminated from the body due to increased water solubility, deviant expression of steroid- and xenobiotic-metabolizing enzymes due to metabolic stress causes severe health problems including accelerated aging, and increased expression of these enzymes is associated with extended longevity, overview, xenobiotic-activated nuclear receptors pregnane X receptor PXR, constitutive androstane receptor CAR, and the vitamin D3-activated nuclear receptor VDR regulating steroid and xenobiotic metabolism by inducing the phase I cytochrome P450 monooxygenases, phase II conjugating transferases, and the phase III transporters, are involved in enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes bile acid sulfation and plays an essential role in protection against lithocholic acid-induced liver toxicity mediated by the farnesoid X receptor FXR, overview
-
-
?
additional information
?
-
-
the proline/serine-rich C-terminal tail is not required for the catalytic activity of SULT2B1b
-
-
?
additional information
?
-
-
also sulfates estrogens and glucocorticoids to lesser extents
-
-
?
additional information
?
-
-
oestrone 3-sulfate is no substrate, no taurolithocholate sulfotransferase activity
-
-
?
additional information
?
-
-
activity for bile acids and phenolic steroids
-
-
?
additional information
?
-
-
also sulfates estrogens and glucocorticoids to lesser extents
-
-
?
additional information
?
-
-
oestrone 3-sulfate is no substrate, no taurolithocholate sulfotransferase activity
-
-
?
additional information
?
-
-
activity for bile acids and phenolic steroids
-
-
?
additional information
?
-
-
the enzyme is responsible for the sulfoconjugation of the 16-androstene steroids. Hydroxysteroid sulfotransferase may play a significant role in determining the levels of sulfated 16-androstene steroids present in plasma. Sulfoconjugation may serve to regulate the quantity of unconjugated 5alpha-androstenone present in the circulation and thus available for accumulation. Animals with a decreased ability to sulfoconjugate 5alpha-androstenone would have a subsequent increase in the levels of unconjugated 5alpha-androstenone in circulation, allowing for the accumulation of high levels in fat and thereby potentially leading to the development of boar taint
-
-
?
additional information
?
-
SULT2A1 is a key enzyme in the testicular and hepatic metabolism of 5alpha-androstenone, which is a major component of the off-odor and off-flavor in pork known as boar taint, role of testicular and hepatic SULT2A1 activity on plasma 5alpha-androstenone sulfate levels, the accumulation of 5alpha-androstenone in adipose tissue, regulatory control of SULT2A1, SULT2A1 activity is negatively correlated with 5alpha-androstenone concentrations in fat, identification of nuclear receptors involved in regulating SULT2A1, overview
-
-
?
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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 + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-hydroxytibolone 3-O-sulfate
-
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 + 3beta-hydroxytibolone 3-O-sulfate
-
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-androstene-3,17-dione
adenosine 3',5'-bisphosphate + 3-O-sulfo-3,5-androstadien-3-ol-17-one
-
-
-
?
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 + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4'-hydroxy-2',3,4-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4'-hydroxy-2,3',4-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-2',3,5-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-2,4'-dichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,3',5-trichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,3'-dichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + androsterone
adenosine 3',5'-bisphosphate + 5alpha-androstane-17-one 3-sulfate
-
enzyme is an androsterone sulfotransferase as well as a dehydroepiandrosterone sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate
-
enzyme is an androsterone sulfotransferase as well as a dehydroepiandrosterone sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylylsulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-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
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
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 + 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-O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
variant haplotypes in tissues possessing alterations in activity or stability may alter the plasma levels of dehydroepiandrosterone and dehydroepiandrosterone sulfate thereby altering the conversion of dehydroepiandrosterone in tissues, overview
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
SULT2B1b, concentration-dependent induction by Ca2+
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
3beta-hydroxyandrost-5-en-17-one
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
isoform SULT2B1 is capable of regulating the activity of adrenal androgens via their inactivation by sulfation
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
conversion of steroids to their inactive sulfated forms, plays a major role in the control of estrogen levels in target tissues
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
sulfation is an important pathway for biotransformation and inactivation of drugs, xenobiotics, monoamine and catecholamine neurotransmitters and steroid hormones
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
best substrate
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
major pathway in the metabolism of steroid hormones
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
enzymatic sulfation of steroids
-
r
additional information
?
-
BNST4 is an ethanol-inducible steroid sulfotransferase
-
-
?
additional information
?
-
-
presence of SULT2b1b suggests a role in the regulation of local steroid hormone synthesis and metabolism
-
-
?
additional information
?
-
-
hydroxylated polychlorinated biphenyls may compete with other xenobiotic substrates as well as endogenous substrates for SULT2A1
-
-
?
additional information
?
-
-
SULT2A1 is a liver- and intestine-specific sulfo-conjugating enzyme that converts the alcoholic OH of neutral steroids, bile acids, and drugs to water-soluble sulfated metabolites, regulation, overview
-
-
?
additional information
?
-
-
SULT2A1 plays a very important role in formation of steroid sulfate esters, and sulfates both 3alpha- and 3beta-hydroxysteroids, estrogens, testosterone, and aliphatic hydroxyl-containing drugs and xenobiotics
-
-
?
additional information
?
-
-
SULT2A1 plays a very important role in sulfating endogenous hydroxysteroids and exogenousxenobiotics
-
-
?
additional information
?
-
-
the enzyme promotes phase II metabolism through its sulfonating action on certain endobiotics, including steroids and bile acids, and on diverse xenobiotics, including therapeutics drugs, regulation of enzyme expression involving HNF4alpha, overview
-
-
?
additional information
?
-
-
the nuclear receptors constitutive androstane receptor CAR and retinoid X receptor alpha RXRalpha are involved in regulation of SULT2A1 enzyme expression, regulation mechanism, overview
-
-
?
additional information
?
-
-
SULT2B1b catalyzes the sulfation of 3beta-hydroxysteroids and functions as a selective cholesterol and oxysterol sulfotransferase
-
-
?
additional information
?
-
enzyme SULT2A1 sulfates the 3alpha- or 3beta-hydroxyl group of hydroxysteroids, as well as the 17-hydroxyl group of testosterone. SULT2A1 can also sulfate 24-hydroxyl group of hydroxycholesterol, and mediate the N-sulfoconjugation of quinolones and other amine drugs in human liver
-
-
-
additional information
?
-
-
Sult2a is involved in 3alpha-sulfation of bile acids, e.g. of litocholic acid, required for enhanced faecal excretion of bile acid in hydroxysteroid sulfotransferase-mediated protection against lithocholic acid-induced liver toxicity, overview
-
-
?
additional information
?
-
-
Sult2A1 converts bile acids, steroids and a number of drugs to the corresponding sulfated metabolites, which are readily eliminated from the body due to increased water solubility, deviant expression of steroid- and xenobiotic-metabolizing enzymes due to metabolic stress causes severe health problems including accelerated aging, and increased expression of these enzymes is associated with extended longevity, overview, xenobiotic-activated nuclear receptors pregnane X receptor PXR, constitutive androstane receptor CAR, and the vitamin D3-activated nuclear receptor VDR regulating steroid and xenobiotic metabolism by inducing the phase I cytochrome P450 monooxygenases, phase II conjugating transferases, and the phase III transporters, are involved in enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes bile acid sulfation and plays an essential role in protection against lithocholic acid-induced liver toxicity mediated by the farnesoid X receptor FXR, overview
-
-
?
additional information
?
-
-
the proline/serine-rich C-terminal tail is not required for the catalytic activity of SULT2B1b
-
-
?
additional information
?
-
-
the enzyme is responsible for the sulfoconjugation of the 16-androstene steroids. Hydroxysteroid sulfotransferase may play a significant role in determining the levels of sulfated 16-androstene steroids present in plasma. Sulfoconjugation may serve to regulate the quantity of unconjugated 5alpha-androstenone present in the circulation and thus available for accumulation. Animals with a decreased ability to sulfoconjugate 5alpha-androstenone would have a subsequent increase in the levels of unconjugated 5alpha-androstenone in circulation, allowing for the accumulation of high levels in fat and thereby potentially leading to the development of boar taint
-
-
?
additional information
?
-
SULT2A1 is a key enzyme in the testicular and hepatic metabolism of 5alpha-androstenone, which is a major component of the off-odor and off-flavor in pork known as boar taint, role of testicular and hepatic SULT2A1 activity on plasma 5alpha-androstenone sulfate levels, the accumulation of 5alpha-androstenone in adipose tissue, regulatory control of SULT2A1, SULT2A1 activity is negatively correlated with 5alpha-androstenone concentrations in fat, identification of nuclear receptors involved in regulating SULT2A1, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
androsterone
-
stronger substrate inhibition than dehydroepiandrosterone adenosine
celecoxib
-
heterotrophic modulator, 3-O-sulfation is inhibited by celecoxib to the same extent, independent of the concentration of 17alpha-ethynylestradiol, switches sulfation from the 3-O-position to the 17beta-O-position
corticosterone
-
competitive inhibitor, inhibits cortisol sulfotransferase activity
deoxycorticosterone
-
competitive inhibitor, inhibits cortisol sulfotransferase activity
endoxifen
i.e. 4-hydroxy-N-desmethyltamoxifen, potent noncompetitive inhibition
estradiol-17beta
-
competitive inhibitor, inhibits cortisol sulfotransferase activity
progesterone
-
competitive inhibitor, inhibits cortisol sulfotransferase activity
testosterone
-
competitive inhibitor, inhibits cortisol sulfotransferase activity
4-hydroxy-2',3,5-trichlorobiphenyl
-
i.e. 4-OH PCB 34, substrate inhibition of SULT1A2
dehydroepiandrosterone
-
competitive inhibitor, inhibits cortisol sulfotransferase activity
gavestinel
-
i.e. 4,6-dichloro-3-[(1E)-3-oxo-3-(phenylamino)-1-propenyl]-1H-indole-2-carboxylic acid sodium salt
gavestinel
-
i.e. 4,6-dichloro-3-[(1E)-3-oxo-3-(phenylamino)-1-propenyl]-1H-indole-2-carboxylic acid sodium salt
Kynurenic acid
-
exhibits selective inhibitory effects on Sult1b1-mediated sulfation of various compounds with IC50 values in the low micromolar range
L689,560
-
i.e. trans-2-carboxy-5,7-dichloro-4-phenylaminocarboxylamino-1,2,3,4-tetrahydroquinoline
L689,560
-
i.e. trans-2-carboxy-5,7-dichloro-4-phenylaminocarboxylamino-1,2,3,4-tetrahydroquinoline
additional information
-
human pregnane X receptor, PXR, downregulates SULT2A1 gene expression, overview, CAR inhibites VDR-mediated vitamin D3 induction of SULT2A1 but notmethotrexate induction of SULT2A1
-
additional information
-
expression of SULT1A1 is reduced in Hep-G2 cells by farnesoid X receptor FXR agonists chenodeoxycholic acid and GW4064, chenodeoxycholic acid also decreases SULT2A expression in wild-type mice
-
additional information
-
unaffected by 8 mM ADP, ATP, and AMP, diethylstilbestrol, cortisone and cholesterol are no inhibitors for the purified enzyme
-
additional information
SULT2A1 activity is negatively correlated with 5alpha-androstenone concentrations in fat, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
celecoxib
-
heterotrophic modulator, switches sulfation from the 3-O-position to the 17beta-O-position and activates such that the total sulfated product exceed product formation by the native enzyme, 3fold to 4fold at 0.25 mM celecoxib
additional information
-
enzyme induction by 1alpha,25-dihydroxyvitamin D3 via the vitamin D responsive element C/ERB-alpha, but not C/ERB-beta, coactivators p300, steroid receptor coactivator 1 and 2, SRC-1 and SRC-2, but not SRC-3, are also required, overview
-
additional information
-
methotrexate induces SULT2A1 expression via nuclear receptor interactions, molecular mechanism, overview, the constitutive active receptor, CAR, mediates the methotrexate induction of SULT2A1 in both Caco-2 and Hep G2 cells, vitamin D receptor, VDR, also upregulates SULT2A1 gene expression, CAR inhibits VDR-mediated vitaminD3 induction of SULT2A1 but notmethotrexate induction of SULT2A1, overview
-
additional information
-
SULT2A1 is a target gene for metabolic regulation/induction by thyroid hormone T3, T3 overexpressing cell s show increased SULT2A1 expression, indirect regulation mechanism via the transcription factor steroidogenic factor 1, SF1, overview
-
additional information
-
the enzyme promoter contains composite elements inducible by nuclear receptors pregnane X receptor and constitutive androstane receptor, synergizing effects by HNF4alpha binding at a site near the promoter, overview
-
additional information
-
induction of SULT2A1 expression by xenobiotic-activated nuclear receptors pregnane X receptor PXR, constitutive androstane receptor CAR, and the vitamin D3-activated nuclear receptor VDR, aging has no effect on the activity of an IR0 enhancer in the Sult2A1 chromatin to recruit VDR, RXR-alpha, and PXR in mice injected with D3 or PCN
-
additional information
-
lithocholic acid induces SULT2A in wild-type and farnesoid X receptor-null mice, chenodeoxycholic acid induces the enzyme only in farnesoid X receptor-null mice, not in wild-type mice, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
3alpha(or 20beta)-hydroxysteroid dehydrogenase deficiency
Premature adrenarche: novel lessons from early onset androgen excess.
Adenocarcinoma
Cholesterol Sulfonation Enzyme, SULT2B1b, Modulates AR and Cell Growth Properties in Prostate Cancer.
Adenocarcinoma
Cloning and expression of cDNA encoding human placental estrogen sulfotransferase.
Adenocarcinoma
Inhibition of SULT2B1b expression alters effects of 3beta-hydroxysteroids on cell proliferation and steroid hormone receptor expression in human LNCaP prostate cancer cells.
Adenocarcinoma
Sulfotransferase 2B1b in human breast: differences in subcellular localization in African American and Caucasian women.
Adenoma
Immunolocalization of dehydroepiandrosterone sulfotransferase in normal and pathologic human adrenal gland.
Adrenocortical Adenoma
Immunolocalization of dehydroepiandrosterone sulfotransferase in normal and pathologic human adrenal gland.
Adrenocortical Carcinoma
Immunolocalization of dehydroepiandrosterone sulfotransferase in normal and pathologic human adrenal gland.
Atherosclerosis
Reduced SULT2B1b expression alleviates ox-LDL-induced inflammation by upregulating miR-148-3P via inhibiting the IKK?/NF-?B pathway in macrophages.
Breast Neoplasms
Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate.
Breast Neoplasms
Endocrine steroid sulfotransferases: steroid alcohol sulfotransferase from human breast carcinoma cell line MCF-7.
Breast Neoplasms
Enzymatic Inactivation of Oxysterols in Breast Tumor Cells Constraints Metastasis Formation by Reprogramming the Metastatic Lung Microenvironment.
Breast Neoplasms
Genetics of androgen metabolism in women with infertility and hypoandrogenism.
Breast Neoplasms
High metabolization of catecholestrogens by type 1 estrogen sulfotransferase (hEST1).
Breast Neoplasms
Relationship between intratumoral expression of genes coding for xenobiotic-metabolizing enzymes and benefit from adjuvant tamoxifen in estrogen receptor alpha-positive postmenopausal breast carcinoma.
Breast Neoplasms
The steroid alcohol and estrogen sulfotransferases in rodent and human mammary tumors.
Carcinogenesis
Hydroxysteroid sulfotransferase 2B1 affects gastric epithelial function and carcinogenesis induced by a carcinogenic agent.
Carcinoma
Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate.
Carcinoma
Immunolocalization of dehydroepiandrosterone sulfotransferase in normal and pathologic human adrenal gland.
Carcinoma
Overexpression of steroid sulfotransferase genes is associated with worsened prognosis and with immune exclusion in clear cell-renal cell carcinoma.
Carcinoma, Hepatocellular
Down-regulation of dehydroepiandrosterone sulfotransferase gene in human hepatocellular carcinoma.
Carcinoma, Hepatocellular
Hydroxysteroid sulfotransferase SULT2B1b promotes hepatocellular carcinoma cells proliferation in vitro and in vivo.
Carcinoma, Hepatocellular
Overexpression of SULT2B1b Promotes Angiogenesis in Human Gastric Cancer.
Cholangiocarcinoma
Progenitor-derived hepatocyte-like (B-13/H) cells metabolise 1'-hydroxyestragole to a genotoxic species via a SULT2B1-dependent mechanism.
Choriocarcinoma
Characterization of Proline-Serine-Rich Carboxyl Terminus in Human Sulfotransferase 2B1b: Immunogenicity, Subcellular Localization, Kinetic Properties, and Phosphorylation.
Choriocarcinoma
Human cytosolic sulfotransferase 2B1: isoform expression, tissue specificity and subcellular localization.
Colorectal Neoplasms
Association study of genetic variants in estrogen metabolic pathway genes and colorectal cancer risk and survival.
Colorectal Neoplasms
Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma.
Communicable Diseases
Influenza A virus infection activates cholesterol sulfotransferase (SULT2B1b) in the lung of female C57BL/6 mice.
COVID-19
Relationships between hyperinsulinaemia, magnesium, vitamin D, thrombosis and COVID-19: rationale for clinical management.
Cushing Syndrome
Serum levels of dehydroepiandrosterone sulfate in patients with asymptomatic cortisol producing adrenal adenoma: comparison with adrenal Cushing's syndrome and non-functional adrenal tumor.
Endometrial Neoplasms
Disturbed expression of phase I and phase II estrogen-metabolizing enzymes in endometrial cancer: Lower levels of CYP1B1 and increased expression of S-COMT.
Fatty Liver
Inhibition of LXR signaling by SULT2B1b promotes liver regeneration after partial hepatectomy in mouse models of nonalcoholic fatty liver disease.
Glioblastoma
Hydroxysteroid sulfotransferase 2B1b expression and localization in normal human brain.
Glioma
Regulation of SULT2B1a (pregnenolone sulfotransferase) expression in rat C6 glioma cells: relevance of AMPA receptor-mediated NO signaling.
Hepatitis, Chronic
17Beta-hydroxysteroid dehydrogenase type 2 and dehydroepiandrosterone sulfotransferase in the human liver.
Herpes Zoster
Age-dependent increases in adrenal cytochrome b5 and serum 5-androstenediol-3-sulfate.
Herpes Zoster
Dehydroepiandrosterone and dehydroepiandrosterone sulfate production in the human adrenal during development and aging.
Herpes Zoster
Developmental changes in steroidogenic enzymes in human postnatal adrenal cortex: immunohistochemical studies.
Herpes Zoster
Genetic and Histopathologic Inter-Tumor Heterogeneity in Primary Aldosteronism.
Herpes Zoster
Human dehydroepiandrosterone sulfotransferase. Purification, molecular cloning, and characterization.
Herpes Zoster
Immunolocalization of dehydroepiandrosterone sulfotransferase in normal and pathologic human adrenal gland.
Hyperlipidemias
Oxysterol sulfation by cytosolic sulfotransferase suppresses liver X receptor/sterol regulatory element binding protein-1c signaling pathway and reduces serum and hepatic lipids in mouse models of nonalcoholic fatty liver disease.
Hyperthyroidism
Serum dehydroepiandrosterone, dehydroepiandrosterone sulfate, and pregnenolone sulfate concentrations in patients with hyperthyroidism and hypothyroidism.
Ichthyosis
Novel Homozygous Mutations in the Genes TGM1, SULT2B1, SPINK5 and FLG in Four Families Underlying Congenital Ichthyosis.
Infections
Oxysterol sulfation by cytosolic sulfotransferase suppresses liver X receptor/sterol regulatory element binding protein-1c signaling pathway and reduces serum and hepatic lipids in mouse models of nonalcoholic fatty liver disease.
Influenza, Human
Influenza A virus infection activates cholesterol sulfotransferase (SULT2B1b) in the lung of female C57BL/6 mice.
Intellectual Disability
Genetics of androgen metabolism in women with infertility and hypoandrogenism.
Liver Diseases
Inhibition of LXR signaling by SULT2B1b promotes liver regeneration after partial hepatectomy in mouse models of nonalcoholic fatty liver disease.
Lymphatic Metastasis
Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma.
Neoplasm Metastasis
Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma.
Neoplasms
Association study of genetic variants in estrogen metabolic pathway genes and colorectal cancer risk and survival.
Neoplasms
Cholesterol Sulfonation Enzyme, SULT2B1b, Modulates AR and Cell Growth Properties in Prostate Cancer.
Neoplasms
Dehydroepiandrosterone sulfotransferase as a possible shunt for the control of steroid metabolism in human mammary carcinoma.
Neoplasms
Hydroxysteroid sulfotransferase SULT2B1b promotes hepatocellular carcinoma cells proliferation in vitro and in vivo.
Neoplasms
Intratumoral heterogeneity of the tumor cells based on in situ cortisol excess in cortisol-producing adenomas; ?An association among morphometry, genotype and cellular senescence?.
Neoplasms
Involvement of prostaglandin E2 in the tumor promoter phorbol ester-caused increase in epidermal cholesterol sulfotransferase activity.
Neoplasms
Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma.
Neoplasms
Quantitative Secretomic Analysis Identifies Extracellular Protein Factors That Modulate the Metastatic Phenotype of Non-Small Cell Lung Cancer.
Neoplasms
The steroid alcohol and estrogen sulfotransferases in rodent and human mammary tumors.
Neoplasms
Tumor Necrosis Factor-Alpha-Nuclear Factor-Kappa B-Signaling Enhances St2b2 Expression during 12-O-Tetradecanoylphorbol-13-acetate-Induced Epidermal Hyperplasia.
Neoplasms
Tumor-mediated liver X receptor-alpha activation inhibits CC chemokine receptor-7 expression on dendritic cells and dampens antitumor responses.
Non-alcoholic Fatty Liver Disease
Inhibition of LXR signaling by SULT2B1b promotes liver regeneration after partial hepatectomy in mouse models of nonalcoholic fatty liver disease.
Obesity
Cholesterol sulfate and cholesterol sulfotransferase inhibit gluconeogenesis by targeting hepatocyte nuclear factor 4?.
Prostatic Intraepithelial Neoplasia
Cholesterol Sulfonation Enzyme, SULT2B1b, Modulates AR and Cell Growth Properties in Prostate Cancer.
Prostatic Neoplasms
Cholesterol Sulfonation Enzyme, SULT2B1b, Modulates AR and Cell Growth Properties in Prostate Cancer.
Prostatic Neoplasms
Cholesterol Sulfotransferase SULT2B1b Modulates Sensitivity to Death Receptor Ligand TNF? in Castration-Resistant Prostate Cancer.
Prostatic Neoplasms
Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate.
Prostatic Neoplasms
Inhibition of SULT2B1b expression alters effects of 3beta-hydroxysteroids on cell proliferation and steroid hormone receptor expression in human LNCaP prostate cancer cells.
Prostatic Neoplasms
Inhibitory Interplay of SULT2B1b Sulfotransferase with AKR1C3 Aldo-keto Reductase in Prostate Cancer.
Prostatic Neoplasms
SULT2B1b sulfotransferase: induction by vitamin D receptor and reduced expression in prostate cancer.
Sepsis
Dissociation of serum dehydroepiandrosterone and dehydroepiandrosterone sulfate in septic shock.
Squamous Cell Carcinoma of Head and Neck
Inhibition of growth and squamous-cell differentiation markers in cultured human head and neck squamous carcinoma cells by beta-all-trans retinoic acid.
steroid sulfotransferase deficiency
Premature adrenarche: novel lessons from early onset androgen excess.
Stomach Neoplasms
Overexpression of SULT2B1b Promotes Angiogenesis in Human Gastric Cancer.
Uterine Cervical Neoplasms
Verteporfin Promotes the Apoptosis and Inhibits the Proliferation, Migration, and Invasion of Cervical Cancer Cells by Downregulating SULT2B1 Expression.
Viremia
Genetic variations in humans associated with differences in the course of hepatitis C.
Virus Diseases
Influenza A virus infection activates cholesterol sulfotransferase (SULT2B1b) in the lung of female C57BL/6 mice.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
1-naphthol
-
isoform SULT1B1, 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
0.0209
3,4-dihydroxyphenylacetic acid
-
isoform Sult1d1, 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
0.238
3-(10,11-dihydro-5H-dibenzo[b,f]azepin-5-yl)-N-methylpropan-1-amine
-
isoform Sult2a1, in 50 mM Tris/HCl buffer, pH 10.0, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C
0.0262
4'-hydroxy-2',3,4-trichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0086
4'-hydroxy-2,3',4-trichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0568
4-hydroxy-2,4'-dichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0136
4-hydroxy-3,3',5-trichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0366
4-hydroxy-3,3'-dichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0085
4-hydroxy-3,5-dichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0399
4-nitrophenol
-
isoform SULT1B1, 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
0.145
L-triiodothyronine
-
isoform SULT1B1, 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
0.0003
3'-phosphoadenylylsulfate
pH 7.4, 37°C, isoenzyme His-SULT2B1a
0.0006
3'-phosphoadenylylsulfate
pH 7.4, 37°C, isoenzyme His-SULT2B1b
0.0019
3beta-hydroxyandrost-5-ene-17-one
pH 7.4, 37°C, isoenzyme DHEA-ST
0.0044
3beta-hydroxyandrost-5-ene-17-one
pH 7.4, 37°C, isoenzyme His-SULT2B1a
0.0093
3beta-hydroxyandrost-5-ene-17-one
pH 7.4, 37°C, isoenzyme SULT2B1a
0.0109
3beta-hydroxyandrost-5-ene-17-one
pH 7.4, 37°C, isoenzyme His-SULT2B1b
0.0185
3beta-hydroxyandrost-5-ene-17-one
pH 7.4, 37°C, isoenzyme SULT2B1b
0.0081
4-hydroxy-2',3,5-trichlorobiphenyl
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0006
dehydroepiandrosterone
-
truncated isoform SULT2B1b, in 50 mM Tris-HCl, pH 7.5, 10 mM MgCl2, at 37°C
0.0008
dehydroepiandrosterone
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0008
dehydroepiandrosterone
-
in 0.25 M potassium phosphate buffer (pH 7.0), at 37°C
0.0038
dehydroepiandrosterone
-
full-length isoform SULT2B1b, in 50 mM Tris-HCl, pH 7.5, 10 mM MgCl2, at 37°C
0.0051
dehydroepiandrosterone
-
isoform SULT2A1, 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
0.0063
xanthurenic acid
-
isoform SULT1B1, 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
0.015
xanthurenic acid
-
isoform Sult1d1, 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
0.206
xanthurenic acid
-
isoform SULT1C2, 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
additional information
additional information
-
for 4'-OH PCB 68, the limit of solubility makes the determination of kinetic constants difficult, the highest rate of sulfation is observed at the limit of solubility at about 0.05 mM
-
additional information
additional information
-
the proline- and serine-rich carboxyl end is an important site in the immunogenicity, nuclear translocation, kinetic activity, and thermostability of SULT2B1b
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0127
4-hydroxytamoxifen
with pregnenolone as substrate, at pH 7.4 and 37°C
0.0194
4-hydroxytamoxifen
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.008
dehydroepiandrosterone
-
in 0.25 M potassium phosphate buffer (pH 7.0), at 37°C
0.0028
endoxifen
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.0098
N-demethyltamoxifen
with pregnenolone as substrate, at pH 7.4 and 37°C
0.0172
N-demethyltamoxifen
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.0096
tamoxifen N-oxide
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.0169
tamoxifen N-oxide
with pregnenolone as substrate, at pH 7.4 and 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
3',4'-dihydroxy-2,3-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.096
3',4'-dihydroxy-4-monochlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0025
4'-hydroxy-2',3,4-trichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0008
4'-hydroxy-2,3',4,5'-tetrachlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0044
4'-hydroxy-2,3',4-trichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0098
4'-hydroxy-2,3'-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.016
4'-hydroxy-3,4-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.028
4'-hydroxy-4-monochlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0006
4-hydroxy-2',3,5-trichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.01
4-hydroxy-2,4'-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0044
4-hydroxy-3,3',5-trichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.014
4-hydroxy-3,3'-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.013
4-hydroxy-3,5-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.016
6'-hydroxy-3,3'-4-trichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.0342
2,6-Dichloro-4-nitrophenol
Homo sapiens
-
isoform SULT1B1, using xanthurenic acid as substrate, 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
24
2,6-Dichloro-4-nitrophenol
Homo sapiens
-
isoform SULT1B1, using L-triiodothyronine as substrate, 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
0.0075
4'-hydroxy-2,5-dichlorobiphenyl
Homo sapiens
-
in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C
0.01
4-hydroxytamoxifen
Homo sapiens
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.0167
4-hydroxytamoxifen
Homo sapiens
with pregnenolone as substrate, at pH 7.4 and 37°C
0.1642
5,7-dichlorokynurenic acid
Homo sapiens
-
isoform SULT1B1, using L-triiodothyronine as substrate, 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
0.2536
5,7-dichlorokynurenic acid
Homo sapiens
-
isoform SULT1B1, using xanthurenic acid as substrate, 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
0.0017
endoxifen
Homo sapiens
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.0012
gavestinel
Homo sapiens
-
isoform SULT1B1, using L-triiodothyronine as substrate, 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
0.0017
gavestinel
Homo sapiens
-
isoform SULT1B1, using xanthurenic acid as substrate, 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
0.0337
Kynurenic acid
Homo sapiens
-
isoform SULT1B1, using xanthurenic acid as substrate, 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
9
Kynurenic acid
Homo sapiens
-
isoform SULT1B1, using L-triiodothyronine as substrate, 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
0.0473
L689,560
Homo sapiens
-
isoform SULT1B1, using xanthurenic acid as substrate, 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
0.0536
L689,560
Homo sapiens
-
isoform SULT1B1, using L-triiodothyronine as substrate, 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
0.005
Mefenamic acid
Homo sapiens
-
IC50 above 0.005 mM, isoform SULT1B1, using L-triiodothyronine as substrate, 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
0.005
Mefenamic acid
Homo sapiens
-
IC50 above 0.005 mM, isoform SULT1B1, using xanthurenic acid as substrate, 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
0.0083
N-demethyltamoxifen
Homo sapiens
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
0.015
N-demethyltamoxifen
Homo sapiens
with pregnenolone as substrate, at pH 7.4 and 37°C
0.0111
tamoxifen N-oxide
Homo sapiens
with dehydroepiandrosterone as substrate, at pH 7.4 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0175
0.027
-
purified recombinant SULT1A2, substrate 4-hydroxy-2',3,5-trichlorobiphenyl
0.9599
-
full-length enzyme, using pregnenolone as substrate, at pH 7.5 and 37°C
0.9993
-
full-length enzyme, using dehydroepiandrosterone as substrate, at pH 7.5 and 37°C
0.0175
-
purified recombinant SULT1A2, substrate 4'-hydroxy-2,3',4,5'-tetrachlorobiphenyl
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 10.5
2 optima: pH 6.5 and pH 10-10.5, activity with estrone and n-propyl gallate
5.5 - 6
6.5
2 optima: pH 6.5 and pH 10-10.5, activity with estrone and n-propyl gallate
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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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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
660966, 661253, 662582, 662863, 673295, 673350, 674394, 675275, 675998, 676007, 677218, 702138, 723910, 724113, 724741, 725045, 725980, 726332, 738098
-
-
brenda
human
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
fetal, and adult adrenal reticular layer as well as adrenal cortex, SULT2A1
brenda
-
of 4-month- and 20-month-old mice, SULT2A1 expression analysis, overview
brenda
-
SULT2A levels in liver are 8fold higher in farnesoid X receptor-null micethan in wild-type mice
brenda
-
SULT2B1b, ciliated columnar or cuboid epithelial cells in terminal bronchia, not in alveolar cells
brenda
additional information
-
both 3alphaHST and 3betaHST activities are essentially undetectable in the testis
brenda
additional information
-
no SULT2B1 in liver, colon, lung, kidney, brain, or testis
brenda
additional information
no SULT2B1 in liver, colon, lung, kidney, brain, or testis
brenda
additional information
no SULT2B1 in liver, colon, lung, kidney, brain, or testis
brenda
additional information
-
variant haplotypes in tissues possessing alterations in activity or stability may alter the plasma levels of dehydroepiandrosterone and dehydroepiandrosterone sulfate thereby altering the conversion of dehydroepiandrosterone in tissues, overview
brenda
additional information
-
farnesoid X receptor FXR-null mice express a constitutively high level of SULT2A
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
epithelial cells in prostate tissue, of LNCaP prostate cancer cells
brenda
-
of ciliated columnar or cuboid epithelial cells in terminal bronchia, SULT2B1b
brenda
-
truncated mutant SULT2B1b lacking the proline- and serine-rich carboxyl end
brenda
-
of placental syncytiotrophoblasts, term human placenta. Human prostate shows only cytosolic localization of SULT2b1 in the basal and luminal prostate epithelial cells. SULT2B1b is capable of translocating to nuclei in BeWo placental cells after stable transfection and differentiation
brenda
-
full-length SULT2B1b, the proline- and serine-rich carboxyl end is an important site in the immunogenicity, nuclear translocation, kinetic activity, and thermostability of SULT2B1b
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
knockdown of SULT2B1 in Hepa1-6 cells induces cell-cycle arrest and apoptosis and suppresses tumorigenesis in vivo
metabolism
enzyme SULT1E1 cannot catalyze the sulfation of either of these two DELTA4-3-ketosteroids, whereas SULT2B1b exhibits weak activity toward only 4-androstene-3,17-dione (7.1 pmol/min/mg enzyme), but not progesterone. Thus, SULT2A1 may be the only major human SULT that is capable of sulfating DELTA4-3-ketosteroids, particularly 4-androstene-3,17-dione
physiological function
additional information
modeling of the binding of hSULT2A1 with substrate 4-androstene-3,17-dione using the crystal structure of 3-ketosteroid-DELTA4-(5alpha)-dehydrogenase from Rhodococcus jostii RHA1 in complex with 4-androstene-3,17-dione (PDB ID 4AT2) and two crystal structures of human SULT2A1 in complex with DHEA and lithocholic acid (PDB IDs 1J99 and 3F3Y) as templates. The intact steroid nucleus is important for the binding of DELTA4-3-keto steroids by SULT2A1. Proposed mechanism of DELTA4-3-ketosteroid sulfation by SULT2A1, overview. Enzyme residues W77 and H99 are likely involved in the catalysis, possibly in the deprotonation of C-6. The sulfation of 4-androstene-3,17-dione might progress through the formation of a hydroxyl group which is a typical target for sulfation, it would require the isomerization of 4-androstene-3,17-dione from a keto form to an enol form
physiological function
-
expression of St2b2 is a trigger of epidermal cell differentiation by controlling cholesterol sulfate level in the cells
physiological function
-
isoform SULT2B1b interacts with cytoskeletal proteins via a proline/serine-rich C-terminus. Such an interaction allows the enzyme to move along microfilaments such as actin filaments, and catalyze the sulfation of hydroxysteroids at specific intracellular locations
physiological function
-
SULT2B1b expression promotes proliferation of hepatocellular carcinoma cells in vitro and in vivo, which may contribute to the progression of hepatocellular carcinoma
physiological function
-
the enzyme SULT2B1b promotes hepatocyte proliferation by inactivating oxysterol/LXR signaling
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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). ST2B1_HUMAN
365
0
41308
Swiss-Prot
Mitochondrion (Reliability: 1)
Q3S3F7_PIG
285
0
33533
TrEMBL
other Location (Reliability: 4)
ST2S2_DANRE
301
0
35364
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32500
34000
35000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
-
isozyme SULT2B1b has an extension at the proline- and serine-rich carboxyl end of about 53 amino acids
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the the proline- and serine-rich carboxyl end of SULT2B1 is phosphorylated at serine residues, e.g. by casein kinase or Cdc2 protein kinase in vitro
phosphoprotein
-
the full-length enzyme is phosphorylated by casein kinase or Cdc2 protein kinase in vitro
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion technique, structure of human dehydroepiandrosterone adenosine sulfotransferase in complex with androsterone has been solved at 2.7 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A679G
-
naturally occuring polymorphisms of SULT2A1, genotyping, SULT2A1 variant allele frequencies in African-American populations, overview
G187C
-
naturally occuring polymorphisms of SULT2A1, genotyping, SULT2A1 variant allele frequencies in African-American populations, overview
G781A
-
naturally occuring polymorphisms of SULT2A1, genotyping, SULT2A1 variant allele frequencies in African-American populations, overview
H99A
site-directed mutagenesis, 50% reduced sulfating activity toward 4-androstene-3,17-dione compared to wild-type
H99S
site-directed mutagenesis, mutant H99S shows complete loss of the sulfating activity toward 4-androstene-3,17-dione
W77A
site-directed mutagenesis, 50% reduced sulfating activity toward 4-androstene-3,17-dione compared to wild-type
Y160F
site-directed mutagenesis, unaltered sulfating activity toward 4-androstene-3,17-dione compared to wild-type
Y231F
site-directed mutagenesis, unaltered sulfating activity toward 4-androstene-3,17-dione compared to wild-type
additional information
additional information
-
construction of a SULT2B1b truncation mutant lacking the proline- and serine-rich carboxyl end of about 53 amino acids, removal of the PSC extension significantly decreases the thermostability of the expressed enzyme and the rate of dehydroepiandrosterone sulfation, truncated SULT2B1b is incapable of translocation to nuclei in transfected human BeWo choriocarcinoma cells
additional information
-
construction of truncation mutants of SULT2A1 for analysis of SF1 binding sites and promoter activity, overview
additional information
-
disruption of the DR4-type motif and the IR2-type motif prevents in vitro binding of nuclear receptors pregnane X receptor and constitutive androstane receptor to their specific binding sites, overview
additional information
-
farnesoid X receptor FXR-null mice express a constitutively high level of SULT2A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
-
after 30 min, dehydroepiandrosterone sulfation activity with recombinant truncated SULT2B1b is decreased 3.5fold more than that of recombinant full-length SULT2B1b, after 45 min,the truncated SULT2B1b activity is completely eliminated, whereas full-length SULT2B1b still maintains about 70% of its original activity
42 - 45
-
truncated SULT2B1b is more sensitive to thermal inactivation than the full-length enzyme. After incubation at 42°C for 30 min, dehydroepiandrosterone sulfation activity with truncated SULT2B1b is decreased 3.5fold more than that of full-length enzyme. After 45 min of incubation at 42°C, truncated SULT2B1b activity is completely eliminated, whereas full-length SULT2B1b still maintains about 70% of its original activity
additional information
-
the proline- and serine-rich carboxyl end is an important site in the immunogenicity, nuclear translocation, kinetic activity, and thermostability of SULT2B1b
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
removal of the extension at the proline- and serine-rich carboxyl end of about 53 amino acids significantly decreases the thermostability of the expressed enzyme as well as decreasing the rate of dehydroepiandrosterone sulfation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stored in glass ampoules , 0.05 M Tris-HCl buffer, pH 7.5, 0.1 mM DTT, 2% propylene glycol, 1 mg/ml protein, no significant difference in activity observed after storage for 3.5 months
-
0°C, redialyzed againstTris/thiol buffer, stored under N2, activity retains for at least 4 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DE52 anion exchange column chromatography and hydroxyapatite column chromatography
-
Ni-NTA agarose column chromatography
partial
recombinant enzyme, expressed in Escherichia coli
recombinant His-tagged full-length SULT2B1b as well as truncated SULT2B1b without the PSC extension from Escherichia coli strain DH5alpha by nickel affinity chromatography
-
recombinant His-tagged SULT2A1 from Escherichia coli by nickel affinity chromatography, expression analysis
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of 5'-flanking region of SULT2A1 and expression of a SULT2A1-reporter construct in Caco-2 cells, transcriptional regulation mechanism analysis, co-expression of human nuclear receptors constitutive androstane receptor CAR and retinoid X receptor alpha RXRalpha which are involved in the regulation, electrophoretic mobility shift assay for interaction study, overview
-
DHEA-ST cDNA cloned and sequenced from human adrenal cDNA library, expression vectors transfected into 293 cells, gene hEST, Hugo nomenclature named it STM gene, because it also codes for monoamine-sulfating phenolsulfotransferase M-PST
-
enzyme expression induction by 1alpha,25-dihydroxyvitamin D3 via the vitamin D responsive element C/ERB-alpha, but not C/ERB-beta, coactivators p300, steroid receptor coactivator 1 and 2, SRC-1 and SRC-2, but not SRC-3, are also required, regulation of transcription and translation, overview, co-expression of SULT2A1 with C/ERB-alpha and 1alpha,25-dihydroxyvitamin D3 in murine NIH3T3 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in livers from Rattus norvegicus and Mus musculus by using a recombinant adenovirus
-
expression analysis of SULT2A1, induction of SULT2A1 expression by xenobiotic-activated nuclear receptors pregnane X receptor PXR, constitutive androstane receptor CAR, and the vitamin D3-activated nuclear receptor VDR, aging has no effect on the activity of an IR0 enhancer in the Sult2A1 chromatin to recruit VDR, RXR-alpha, and PXR in mice injected with D3 or PCN
-
expression of His-tagged full-length SULT2B1b and truncated SULT2B1b without the PSC extension in Escherichia coli strain DH5alpha and in human BeWo choriocarcinoma cells, translocation of the wild-type enzyme to nuclei, but not of the truncation mutant
-
expression of SULT2B1b eliminates the cytotoxic effect of 7-oxo-cholesterol on 293T cells, which are normally devoid of SULT2B1b
-
full-length isoform SULT2B1b as well as truncated SULT2B1b without the PS proline- and serine-rich carboxyl extension are expressed in Escherichia coli XL1-Blue cells
-
gene SULT2A1, expression and regulation analysis, the enzyme promoter contains composite elements inducible by nuclear receptors pregnane X receptor, PXR, and constitutive androstane receptor, CAR, synergizing effects by HNF4alpha binding at a site near the promoter, overview
-
gene SULT2A1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21
genomic library constructed in pTZ18R, expression of recombinant BNST3 in Escherichia coli
-
hEST1 and hEST2 cloned and overexpressed in Escherichia coli in fusion with GST
-
SULT2A1 is a target gene for metabolic regulation/induction by thyroid hormone T3, T3 overexpressing Hep-G2 cells, with co-expression of the T3-receptor-alpha, show increased SULT2A1 expression in a DNA microarray analysis, 5fold at protein level and 9fold at mRNA level, which is inhibited by cycloheximide indicating an indirect regulation mechanism via the transcription factor steroidogenic factor 1, SF1, SULT2A1 contains seven SF1 binding sites, analysis of promoter activity in wild-type and truncation mutants of the enzyme, overview
-
SULT2A1, determination of the promoter sequence, SULT2A1-reporter gene expression in Hep-G2 cells and expression analysis, the constitutive active receptor, CAR, mediates the methotrexate induction of SULT2A1 in both Caco-2 andHep G2 cells, vitamin D receptor, VDR, also upregulates SULT2A1 gene expression, while human pregnane X receptor, PXR, downregulates it
-
SULT2A1, DNA and amino acid sequence determination and analysis, relationship between SULT2A1 expression and sulfoconjugation of androstenone, quantitative expression analysis, overview, identification of nuclear receptors involved in regulating SULT2A1
SULT2B1 gene encodes 2 isoforms, SULT2B1a and SULT2B1b, generated by alternate splicing of the first exon, cloned and expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a 2 week's ethanol ingestion up-regulates hydroxysteroid sulfotransferase SULT2A1 in male rat liver and intestine
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activation of liver X receptor alpha as well as liver X receptor synthetic ligands like TO901317 and GW3965 induce the expression of isoform SULT2A1 at mRNA, protein, and enzymatic levels
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down-regulation of RORalpha and/or RORgamma by small interfering RNA inhibits the expression of endogenous SULT2A1
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estrogen-related receptor alpha upregulates SULT2A1 transcription in Caco-2 cells
highest expression level is detected in epidermis from 3-day-old mice and then decreases before maturation
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inhibition of SULT2B1b expression induces cell-cycle arrest and apoptosis in Hepa1-6 cells by upregulating the expression of FAS, downregulating the expression of cyclinB1, BCL2 and MYC in vitro and in vivo at both the transcript and protein levels. Knock-down of SULT2B1b expression significantly suppresses tumor growth in nude mouse xenografts
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retinoid-related orphan receptor (ROR)alpha and RORgamma transactivate the SULT2A1 gene promoter through their binding to a ROR response element found in the SULT2A1 gene promoter
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SULT2B1 is comparatively higher in the human hepatocarcinoma tumorous tissues than their adjacent tissues
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the amount of SULT2B1b mRNA in human endometrial tissues is significantly higher during the midluteal phase than during other phases of the menstrual cycle. Expression of SULT2B1b mRNA is induced by cAMP or phosphate in human endometrial stromal cells, whereas it is induced by cAMP or relaxin in endometrial epithelial cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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isoenzyme STS plays important roles in regulating the in situ production of estrogens in breast carcinoma tissue, immunoreactivity of the enzymes is a potent prognostic factor for cancer
medicine
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characterization of the mechanism of regulation and action of DHEA-ST should lead to a better understanding of the control of adrenal androgen production as well as a better knowledge of the role of DHEAS in the androgen-and estrogen-sensitive disorders
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Singer, S.S.; Gebhart, J.; Hess, E.
Enzymatic sulfation of steroids. V. Partial purification and some properties of sulfotransferase III, the major glucocorticoid sulfotransferase of liver cytosol from male rats
Can. J. Biochem.
56
1028-1035
1978
Rattus norvegicus
brenda
Adams, J.B.; McDonald, D.
Enzymic synthesis of steroid sulphates. XII. Isolation of dehydroepiandrosterone sulphotransferase from human adrenals by affinity chromatography
Biochim. Biophys. Acta
567
144-153
1979
Homo sapiens
brenda
Adams, J.B.; McDonald, D.
Enzymic synthesis of steroid sulphates. XIII. Isolation and properties of dehydroepiandrosterone sulphotransferase from human foetal adrenals
Biochim. Biophys. Acta
615
275-278
1980
Homo sapiens
brenda
Gower, D.B.; Cooke, G.M.; Ferguson, S.E.
Sulphoconjugation of steroids in porcine liver. Partial purification of the cytosolic sulphotransferases for pregnenolone and 5alpha-androst-16-en-3beta-ol
FEBS Lett.
150
507-510
1982
Sus scrofa
brenda
Singer, S.S.; Federspiel, M.J.; Green, J.; Lewis, W.G.; Martin, V.; Witt, K.R.; Tappel, J.
Enzymatic sulfation of steroids. XV. Studies differentiating between rat liver androgen, estrogen, bile acid, glucocorticoid and phenol sulfotransferases
Biochim. Biophys. Acta
700
110-117
1982
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Sugiyama, Y.; Stolz, A.; Sugimoto, M.; Kuhlenkamp, J.; Yamada, T.; Kaplowitz, N.
Identification and partial purification of a unique phenolic steroid sulphotransferase in rat liver cytosol
Biochem. J.
224
947-953
1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Takikawa, H.; Stolz, A.; Kaplowitz, N.
Purification of a 32.5 kDa monomeric sulfotransferase from rat liver with activity for bile acids and phenolic steroids
FEBS Lett.
207
193-197
1986
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Falany, C.N.; Vasquez, M.E.; Kalb, J.M.
Purification and characterization of human liver dehydroepiandrosterone sulphotransferase
Biochem. J.
260
641-646
1989
Homo sapiens
brenda
Borthwick, E.B.; Burchell, A.; Coughtrie, M.W.H.
Purification and immunochemical charcterization of a male-specific rat liver oestrogen sulphotransferase
Biochem. J.
289
719-725
1993
Rattus norvegicus
-
brenda
Forbes-Bamforth, K.J.; Coughtrie, M.W.H.
Identification of a new adult human liver sulfotransferase with specificity for endogenous and xenobiotic estrogens
Biochem. Biophys. Res. Commun.
198
707-711
1994
Homo sapiens
brenda
Hobkirk, R.
Sulfation by guinea pig chorion and uterus: Differential action towards estrone and estradiol
J. Steroid Biochem. Mol. Biol.
59
479-484
1996
Cavia porcellus
brenda
Luu-The, V.; Bernier, F.; Dufort, I.
Steroid sulfotransferases
J. Endocrinol.
150
87-97
1996
Bos taurus, Cavia porcellus, Homo sapiens, Rattus norvegicus
brenda
Chetrite, G.; Pasqualini, J.R.
Steroid sulphotransferase and 17beta-hydroxysteroid dehydrogenase activities in Ishikawa human endometrial adenocarcinoma cells
J. Steroid Biochem. Mol. Biol.
61
27-34
1997
Homo sapiens
brenda
Kakuta, Y.; Pedersen, L.C.; Chae, K.; Song, W.C.; Leblanc, D.; London, R.; Carter, C.W.; Negishi, M.
Mouse steroid sulfotransferases. Substrate specificity and preliminary X-ray crystallographic analysis
Biochem. Pharmacol.
55
313-317
1998
Mus musculus
brenda
Park, B.C.; Lee, Y.C.; Strott, C.A.
Testosterone sulfotransferase: Evidence in the guinea pig that this reaction is carried out by 3alpha-hydroxysteroid sulfotransferase
Steroids
64
510-517
1999
Cavia porcellus
brenda
Rouleau, M.; Marsolais, F.; Richard, M.; Nicolle, L.; Voigt, B.; Adam, G.; Varin, L.
Inactivation of brassinosteroid biological activity by a salicylate-inducible steroid sulfotransferase from Brassica napus
J. Biol. Chem.
274
20925-20930
1999
Brassica napus
brenda
Faucher, F.; Lacoste, L.; Dufort, I.; Luu-The, V.
High metabolization of catecholestrogens by type 1 estrogen sulfotransferase (hEST1)
J. Steroid Biochem. Mol. Biol.
77
83-86
2001
Homo sapiens
brenda
Meloche, C.A.; Falany, C.N.
Expression and characterization of the human 3b-hydroxysteroid sulfotransferases (SULT2B1alpha and SULT2B1beta)
J. Steroid Biochem. Mol. Biol.
77
261-269
2001
Homo sapiens, Homo sapiens (O00204), Homo sapiens (Q06520)
brenda
Nakamura, Y.; Miki, Y.; Suzuki, T.; Nakata, T.; Darnel, A.D.; Moriya, T.; Tazawa, C.; Saito, H.; Ishibashi, T.; Takahashi, S.; Yamada, S.; Sasano, H.
Steroid sulfatase and estrogen sulfotransferase in the atherosclerotic human aorta
Am. J. Pathol.
163
1329-1339
2003
Homo sapiens
brenda
Suzuki, T.; Nakata, T.; Miki, Y.; Kaneko, C.; Moriya, T.; Ishida, T.; Akinaga, S.; Hirakawa, H.; Kimura, M.; Sasano, H.
Estrogen sulfotransferase and steroid sulfatase in human breast carcinoma
Cancer Res.
63
2762-2770
2003
Homo sapiens
brenda
Yasuda, S.; Liu, C.C.; Takahashi, S.; Suiko, M.; Chen, L.; Snow, R.; Liu, M.C.
Identification of a novel estrogen-sulfating cytosolic SULT from zebrafish: molecular cloning, expression, characterization, and ontogeny study
Biochem. Biophys. Res. Commun.
330
219-225
2005
Danio rerio (Q6DHH8)
brenda
He, D.; Meloche, C.A.; Dumas, N.A.; Frost, A.R.; Falany, C.N.
Different subcellular localization of sulfotransferase 2B1b in human placenta and prostate
Biochem. J.
379
533-540
2004
Homo sapiens
brenda
He, D.; Frost, A.R.; Falany, C.N.
Identification and immunohistochemical localization of sulfotransferase 2B1b (SULT2B1b) in human lung
Biochim. Biophys. Acta
1724
119-126
2005
Homo sapiens
brenda
Ohkimoto, K.; Liu, M.Y.; Suiko, M.; Sakakibara, Y.; Liu, M.C.
Characterization of a zebrafish estrogen-sulfating cytosolic sulfotransferase: inhibitory effects and mechanism of action of phytoestrogens
Chem. Biol. Interact.
147
1-7
2004
Danio rerio (Q7ZUS4)
brenda
Cui, D.; Booth-Genthe, C.L.; Carlini, E.; Carr, B.; Schrag, M.L.
Heterotropic modulation of sulfotransferase 2A1 activity by celecoxib: product ratio switching of ethynylestradiol sulfation
Drug Metab. Dispos.
32
1260-1264
2004
Homo sapiens
brenda
Sinclair, P.A.; Squires, E.J.
Testicular sulfoconjugation of the 16-androstene steroids by hydroxysteroid sulfotransferase: its effect on the concentrations of 5alpha-androstenone in plasma and fat of the mature domestic boar
J. Anim. Sci.
83
358-365
2005
Sus scrofa
brenda
Chang, H.J.; Shi, R.; Rehse, P.; Lin, S.X.
Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex
J. Biol. Chem.
279
2689-2696
2004
Homo sapiens
brenda
Higashi, Y.; Fuda, H.; Yanai, H.; Lee, Y.; Fukushige, T.; Kanzaki, T.; Strott, C.A.
Expression of cholesterol sulfotransferase (SULT2B1b) in human skin and primary cultures of human epidermal keratinocytes
J. Invest. Dermatol.
122
1207-1213
2004
Homo sapiens
brenda
Harris, R.M.; Kirk, C.J.; Waring, R.H.
Non-genomic effects of endocrine disrupters: inhibition of estrogen sulfotransferase by phenols and chlorinated phenols
Mol. Cell. Endocrinol.
244
72-74
2005
Homo sapiens
brenda
Marsolais, F.; Sebastia, C.H.; Rousseau, A.; Varin, L.
Molecular and biochemical characterization of BNST4, an ethanol-inducible steroid sulfotransferase from Brassica napus, and regulation of BNST genes by chemical stress and during development
Plant Sci.
166
1359-1370
2004
Brassica napus (Q6T261)
brenda
Liu, Y.; Apak, T.I.; Lehmler, H.J.; Robertson, L.W.; Duffel, M.W.
Hydroxylated polychlorinated biphenyls are substrates and inhibitors of human hydroxysteroid sulfotransferase SULT2A1
Chem. Res. Toxicol.
19
1420-1425
2006
Homo sapiens
brenda
He, D.; Falany, C.N.
Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation
Drug Metab. Dispos.
34
1749-1755
2006
Homo sapiens
brenda
Miyata, M.; Matsuda, Y.; Tsuchiya, H.; Kitada, H.; Akase, T.; Shimada, M.; Nagata, K.; Gonzalez, F.J.; Yamazoe, Y.
Chenodeoxycholic acid-mediated activation of the farnesoid X receptor negatively regulates hydroxysteroid sulfotransferase
Drug Metab. Pharmacokinet.
21
315-323
2006
Mus musculus
brenda
Huang, Y.H.; Lee, C.Y.; Tai, P.J.; Yen, C.C.; Liao, C.Y.; Chen, W.J.; Liao, C.J.; Cheng, W.L.; Chen, R.N.; Wu, S.M.; Wang, C.S.; Lin, K.H.
Indirect regulation of human dehydroepiandrosterone sulfotransferase family 1A member 2 by thyroid hormones
Endocrinology
147
2481-2489
2006
Homo sapiens
brenda
Seo, Y.K.; Chung, Y.T.; Kim, S.; Echchgadda, I.; Song, C.S.; Chatterjee, B.
Xenobiotic- and vitamin D-responsive induction of the steroid/bile acid-sulfotransferase Sult2A1 in young and old mice: the role of a gene enhancer in the liver chromatin
Gene
386
218-223
2007
Mus musculus
brenda
Chen, X.; Maiti, S.; Zhang, J.; Chen, G.
Nuclear receptor interactions in methotrexate induction of human dehydroepiandrosterone sulfotransferase (hSULT2A1)
J. Biochem. Mol. Toxicol.
20
309-317
2006
Homo sapiens
brenda
Fuda, H.; Javitt, N.B.; Mitamura, K.; Ikegawa, S.; Strott, C.A.
Oxysterols are substrates for cholesterol sulfotransferase
J. Lipid Res.
48
1343-1352
2007
Homo sapiens
brenda
Sinclair, P.A.; Gilmore, W.J.; Lin, Z.; Lou, Y.; Squires, E.J.
Molecular cloning and regulation of porcine SULT2A1: relationship between SULT2A1 expression and sulfoconjugation of androstenone
J. Mol. Endocrinol.
36
301-311
2006
Sus scrofa (Q3S3F7)
brenda
Song, C.S.; Echchgadda, I.; Seo, Y.; Oh, T.; Kim, S.; Kim, S.; Cho, S.; Shi, L.; Chatterjee, B.
An essential role of the CAAT/enhancer binding protein-alpha in the vitamin D-induced expression of the human steroid/bile acid-sulfotransferase (SULT2A1)
Mol. Endocrinol.
20
1286
2006
Homo sapiens
brenda
Echchgadda, I.; Song, C.S.; Oh, T.; Ahmed, M.; De La Cruz, I.J.; Chatterjee, B.
The xenobiotic-sensing nuclear receptors pregnane X receptor, constitutive androstane receptor, and orphan nuclear receptor hepatocyte nuclear factor 4alpha in the regulation of human steroid-/bile acid-sulfotransferase
Mol. Endocrinol.
21
2099-2111
2007
Homo sapiens
brenda
Nowell, S.; Falany, C.N.
Pharmacogenetics of human cytosolic sulfotransferases
Oncogene
25
1673-1678
2006
Homo sapiens
brenda
Wang, M.; Ebmeier, C.C.; Olin, J.R.; Anderson, R.J.
Sulfation of tibolone metabolites by human postmenopausal liver and small intestinal sulfotransferases (SULTs)
Steroids
71
343-351
2006
Homo sapiens
brenda
Chen, X.; Zhang, J.; Baker, S.M.; Chen, G.
Human constitutive androstane receptor mediated methotrexate induction of human dehydroepiandrosterone sulfotransferase (hSULT2A1)
Toxicology
231
224-233
2007
Homo sapiens
brenda
Miyata, M.; Watase, H.; Hori, W.; Shimada, M.; Nagata, K.; Gonzalez, F.J.; Yamazoe, Y.
Role for enhanced faecal excretion of bile acid in hydroxysteroid sulfotransferase-mediated protection against lithocholic acid-induced liver toxicity
Xenobiotica
36
631-644
2006
Mus musculus
brenda
Senggunprai, L.; Yoshinari, K.; Yamazoe, Y.
Inhibitory effects of kynurenic acid, a tryptophan metabolite, and its derivatives on cytosolic sulfotransferases
Biochem. J.
422
455-462
2009
Homo sapiens, Mus musculus
brenda
Shimada, M.; Matsuda, T.; Sato, A.; Akase, T.; Matsubara, T.; Nagata, K.; Yamazoe, Y.
Expression of a skin cholesterol sulfotransferase, St2b2, is a trigger of epidermal cell differentiation
Xenobiotica
38
1487-1499
2008
Mus musculus
brenda
Zhang, X.; Bai, Q.; Xu, L.; Kakiyama, G.; Pandak, W.M.; Zhang, Z.; Ren, S.
Cytosolic sulfotransferase 2B1b promotes hepatocyte proliferation gene expression in vivo and in vitro
Am. J. Physiol. Gastrointest. Liver Physiol.
303
G344-G355
2012
Homo sapiens
brenda
Gulcan, H.O.; Duffel, M.W.
Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: studies on the formation of catalytically non-productive enzyme complexes
Arch. Biochem. Biophys.
507
232-240
2011
Homo sapiens
brenda
Ekuase, E.J.; Liu, Y.; Lehmler, H.J.; Robertson, L.W.; Duffel, M.W.
Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1
Chem. Res. Toxicol.
24
1720-1728
2011
Homo sapiens
brenda
Kurogi, K.; Sakakibara, Y.; Kamemoto, Y.; Takahashi, S.; Yasuda, S.; Liu, M.C.; Suiko, M.
Mouse cytosolic sulfotransferase SULT2B1b interacts with cytoskeletal proteins via a proline/serine-rich C-terminus
FEBS J.
277
3804-3811
2010
Mus musculus
brenda
Koizumi, M.
Momoeda, M.; Hiroi, H.; Hosokawa, Y.; Tsutsumi, R.; Osuga, Y.; Yano, T.; Taketani, Y.: Expression and regulation of cholesterol sulfotransferase (SULT2B1b) in human endometrium
Fertil. Steril.
93
1538-1544
2010
Homo sapiens
brenda
Ou, Z.; Shi, X.; Gilroy, R.K.; Kirisci, L.; Romkes, M.; Lynch, C.; Wang, H.; Xu, M.; Jiang, M.; Ren, S.; Gramignoli, R.; Strom, S.C.; Huang, M.; Xie, W.
Regulation of the human hydroxysteroid sulfotransferase (SULT2A1) by RORalpha and RORgamma and its potential relevance to human liver diseases
Mol. Endocrinol.
27
106-115
2013
Homo sapiens
brenda
Yang, X.; Xu, Y.; Guo, F.; Ning, Y.; Zhi, X.; Yin, L.; Li, X.
Hydroxysteroid sulfotransferase SULT2B1b promotes hepatocellular carcinoma cells proliferation in vitro and in vivo
PLoS ONE
8
e60853
2013
Homo sapiens
brenda
Maiti, S.; Chen, G.
Ethanol up-regulates phenol sulfotransferase (SULT1A1) and hydroxysteroid sulfotransferase (SULT2A1) in rat liver and intestine
Arch. Physiol. Biochem.
121
68-74
2015
Rattus norvegicus
brenda
Ou, Z.; Jiang, M.; Hu, B.; Huang, Y.; Xu, M.; Ren, S.; Li, S.; Liu, S.; Xie, W.; Huang, M.
Transcriptional regulation of human hydroxysteroid sulfotransferase SULT2A1 by LXR?
Drug Metab. Dispos.
42
1684-1689
2014
Homo sapiens
brenda
Squirewell, E.J.; Qin, X.; Duffel, M.W.
Endoxifen and other metabolites of tamoxifen inhibit human hydroxysteroid sulfotransferase 2A1 (hSULT2A1)
Drug Metab. Dispos.
42
1843-1850
2014
Homo sapiens (Q06520), Homo sapiens
brenda
Falany, C.N.; Rohn-Glowacki, K.J.
SULT2B1: unique properties and characteristics of a hydroxysteroid sulfotransferase family
Drug Metab. Rev.
45
388-400
2013
Homo sapiens (O00204), Homo sapiens
brenda
Huang, C.; Zhou, T.; Chen, Y.; Sun, T.; Zhang, S.; Chen, G.
Estrogen-related receptor ERRalpha regulation of human hydroxysteroid sulfotransferase (SULT2A1) gene expression in human Caco-2 cells
J. Biochem. Mol. Toxicol.
28
32-38
2014
Homo sapiens (Q06520)
brenda
Hashiguchi, T.; Kurogi, K.; Shimohira, T.; Teramoto, T.; Liu, M.C.; Suiko, M.; Sakakibara, Y.
DELTA4-3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases
Biochim. Biophys. Acta
1861
2883-2890
2017
Homo sapiens (Q06520)
brenda
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