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Information on EC 2.8.2.2 - alcohol sulfotransferase and Organism(s) Homo sapiens and UniProt Accession Q06520
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2.8.2.2 alcohol sulfotransferaseIUBMB Comments
Primary and secondary alcohols, including aliphatic alcohols, ascorbic acid, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15 steroid sulfotransferase).
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Word Map
- 2.8.2.2
- dehydrogenases
- testosterone
- estradiol
- androgen
-
sulfotransferases
- progesterone
- glucocorticoid
- adrenal
- estrone
-
steroidogenic
- cortisol
- phenol
- testis
- testicular
- aromatase
-
steroidogenesis
- sult1e1
-
sulfatase
- xenobiotics
- pregnenolone
-
sults
-
mineralocorticoid
- gonad
-
11-beta
- androstenedione
-
aldo-keto
-
leydig
- 3'-phosphoadenosine
- 5'-phosphosulfate
- aldosterone
-
sulfoconjugation
-
beta-hsd
-
estrogen-dependent
- beta-estradiol
- 3'-phosphoadenosine-5'-phosphosulfate
-
sulfurylation
- 17beta-hsds
- 5alpha-dihydrotestosterone
- cyp17a1
- sulphotransferase
-
intracrine
-
pnpla3
- 2,6-dichloro-4-nitrophenol
-
pre-receptor
- 3-ketosteroids
-
3alpha
- 3alpha-hsds
- hsd17b2
- synthesis
- diagnostics
- medicine
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
hydroxysteroid, estrogen sulfotransferase, dhea st, sult2b1a, sult6b1, iodothyronine sulfotransferase, ast-rb2, pz-sult, hydroxysteroid sulfotransferase sult2a1, hydroxysteroid sulfotransferase 2b1b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SULT2A1
-
3-hydroxysteroid sulfotransferase
-
-
-
-
3beta-hydroxy steroid sulfotransferase
-
-
-
-
3beta-hydroxysteroid sulfotransferase
-
-
-
-
5alpha-androstenol sulfotransferase
-
-
-
-
alcohol/hydroxysteroid sulfotransferase
-
-
-
-
cholesterol sulfotransferase
dehydroepiandrosterone sulfotransferase
DELTA5-3beta-hydroxysteroid sulfokinase
-
-
-
-
DHEA-ST
estrogen sulfokinase
-
-
-
-
estrogen sulfotransferase
HST
-
-
-
-
hydroxysteroid sulfotransferase
hydroxysteroid sulfotransferase ST2A3
-
also variously named as SULT2A1 or human DHEA-ST
steroid alcohol sulfotransferase
-
-
-
-
steroid sulfokinase
-
-
-
-
steroid sulfotransferase
-
-
-
-
sterol sulfokinase
-
-
-
-
sterol sulfotransferase
-
-
-
-
SULT1A1
SULT1B1
SULT2A1
SULT2B1
SULT2B1a
SULT2B1b
additional information
cholesterol sulfotransferase
-
-
-
-
dehydroepiandrosterone sulfotransferase
-
-
-
-
estrogen sulfotransferase
-
-
-
-
hydroxysteroid sulfotransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
random bi-bi mechanism catalytic mechanism of SULTs, many family members have distinct, but overlapping substrate specificities, the enzymes have a sequential catalytic mechanism that is susceptible to substrate inhibition
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:alcohol sulfotransferase
Primary and secondary alcohols, including aliphatic alcohols, ascorbic acid, chloramphenicol, ephedrine and hydroxysteroids, but not phenolic steroids, can act as acceptors (cf. EC 2.8.2.15 steroid sulfotransferase).
CAS REGISTRY NUMBER
COMMENTARY
9032-76-2
-
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 + (S)-dehydroepiandrosterone
adenosine 3',5'-bisphosphate + (S)-dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + androsterone
adenosine 3',5'-bisphosphate + androsterone 3-sulfate
-
-
-
?
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-sulfate
3'-phosphoadenylyl sulfate + glycolithocholic acid
adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + lithocholic acid
adenosine 3',5'-bisphosphate + lithocholate 3-sulfate
3'-phosphoadenylyl sulfate + raloxifene
adenosine 3',5'-bisphosphate + ?
substrate complex structure analysis
-
-
?
3'-phosphoadenylyl sulfate + taurolithocholic acid
adenosine 3',5'-bisphosphate + taurolithocholate 3-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 2-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 4-hydroxy-3,5-dichlorobiphenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + cortisol
adenosine 3',5'-bisphosphate + cortisol sulfate
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
SULT1B1
-
-
?
3'-phosphoadenylyl sulfate + 17alpha-hydroxypregnenolone
adenosine 3',5'-bisphosphate + 17alpha-hydroxypregnenolone 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 + 6-hydroxy-4-methylbenzo[d]thiazole-2-carbonitrile
adenosine 3',5'-bisphosphate + ?
i.e. proluciferin substrate UGT-Glo substrate A, GSA
-
-
?
3'-phosphoadenylyl sulfate + 7-oxo-cholesterol
adenosine 3',5'-bisphosphate + 7-oxo-cholesteryl 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 7-oxocholesterol
adenosine 3',5'-bisphosphate + 7-oxocholesterol 3-sulfate
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + 7alpha-hydroxycholesterol
adenosine 3',5'-bisphosphate + 7alpha-hydroxycholesterol 3-sulfate
SULT2B1b, the 7alpha derivative is highly preferred
-
-
?
3'-phosphoadenylyl sulfate + 7alpha-hydroxycholesterol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 7beta-hydroxycholesterol
adenosine 3',5'-bisphosphate + 7beta-hydroxycholesterol 3-sulfate
SULT2B1b, the 7alpha derivative is highly preferred
-
-
?
3'-phosphoadenylyl sulfate + 7beta-hydroxycholesterol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
3'-phosphoadenylyl sulfate + cholesterol 7alpha-hydroperoxide
adenosine 3',5'-bisphosphate + ?
SULT2B1b
-
-
?
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-sulfate
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + genistein
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + raloxifene
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + tibolone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 1'-hydroxysafrole
adenosine 3',5'-bisphosphate + ?
-
isoenzyme DHEA-ST, sulfation and bioactivation to a lesser extent
-
-
?
3'-phosphoadenylylsulfate + 1-hydroxymethylpyrene
adenosine 3',5'-bisphosphate + ?
-
isoenzyme DHEA-ST, sulfation and bioactivation
-
-
?
3'-phosphoadenylylsulfate + 17-beta-estradiol
adenosine 3',5'-bisphosphate + 17-beta-estradiol 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 17alpha-ethinylestradiol
adenosine 3',5'-bisphosphate + 17alpha-ethinylestradiol sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + 2-hydroxy-catecholestrogen
adenosine 3',5'-bisphosphate + ?
-
best substrate for this enzyme, also catalyzes the transformation of 4-hydroxy-estrogens and 16-hydroxy-estrogens, but with a lower affinity
-
-
r
3'-phosphoadenylylsulfate + 3,3'-diiodothyronine
adenosine 3',5'-bisphosphate + ?
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + 3,5-diiodothyronine
adenosine 3',5'-bisphosphate + ?
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + 4,4'-isopropylidenediphenol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 4-(1,1,3,3-tetramethylbutyl)phenol
adenosine 3',5'-bisphosphate + 4-(1,1,3,3-tetramethylbutyl)phenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-n-nonylphenol
adenosine 3',5'-bisphosphate + 4-n-nonylphenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + ?
-
isoform SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 6-hydroxymethylbenzo[a]pyrene
adenosine 3',5'-bisphosphate + ?
-
isoenzyme DHEA-ST, sulfation and bioactivation
-
-
?
3'-phosphoadenylylsulfate + alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + ?
-
isoenzyme DHEA-ST, sulfation and bioactivation to a lesser extent
-
-
?
3'-phosphoadenylylsulfate + alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + sulfuric acid mono-[(E)-4-[4-(2-dimethylaminoethoxy)-phenyl]-3,4-diphenylbut-3-enyl] ester
-
all enantiomers are substrates: E-(+)-alpha-hydroxytamoxifen, E-(-)-alpha-hydroxytamoxifen, Z-(+)-alpha-hydroxytamoxifen and Z-(-)-alpha-hydroxytamoxifen. The ratio of turnover-number to KM-value is higher with the Z enantiomers than with the E enantiomers
-
-
?
3'-phosphoadenylylsulfate + androstenediol
adenosine 3',5'-bisphosphate + androstenediol sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + androsterone
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + benzyl alcohol
adenosine 3',5'-bisphosphate + benzyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-O-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + budesonide-22R
adenosine 3',5'-bisphosphate + budesonide-22R,11 sulfate + budesonide-22R,21 sulfate
synthetic glucocorticosteroid, used in treatment of asthma and allergic reactions, rhinitis, and inflammatory bowel disease
-
-
r
3'-phosphoadenylylsulfate + budesonide-22S
adenosine 3',5'-bisphosphate + budesonide-22S,11 sulfate + budesonide-22S,21 sulfate
synthetic glucocorticosteroid, used in treatment of asthma and allergic reactions, rhinitis, and inflammatory bowel disease
-
-
r
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol sulfate
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylylsulfate + diiodothyronine
adenosine 3',5'-bisphosphate + ?
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
isoform SULT1A3
-
-
?
3'-phosphoadenylylsulfate + E-(+)-alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + sulfuric acid mono-[(E)-4-[4-(2-dimethylaminoethoxy)-phenyl]-3,4-diphenylbut-3-enyl] ester
-
-
-
-
?
3'-phosphoadenylylsulfate + E-(-)-alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + sulfuric acid mono-[(E)-4-[4-(2-dimethylaminoethoxy)-phenyl]-3,4-diphenylbut-3-enyl] ester
-
-
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + ethanol
adenosine 3',5'-bisphosphate + ethyl sulfate
-
high activity with SULT1A2, SULT1B1, SULT2A1 and SULT1A3. SULT1A3 might be the predominant form for the sulphonation of ethanol
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + hycanthone
adenosine 3',5'-bisphosphate + ?
-
isoenzyme DHEA-ST, sulfation and bioactivation
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + ?
-
antihypertensive agent and hair growth stimulator, activation by sulfation
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-2-acetylaminofluorene
adenosine 3',5'-bisphosphate + ?
-
isoenzyme DHEA-ST, sulfation and bioactivation to a lesser extent
-
-
?
3'-phosphoadenylylsulfate + R-(+)-1-naphthyl-1-ethanol
adenosine 3',5'-bisphosphate + ?
-
S-(-)-enantiomer is not a substrate for the enzyme
-
-
?
3'-phosphoadenylylsulfate + R-(+)-2-naphthyl-1-ethanol
adenosine 3',5'-bisphosphate + ?
-
both enantiomers are substrates for the enzyme
-
-
?
3'-phosphoadenylylsulfate + S-(-)-2-naphthyl-1-ethanol
adenosine 3',5'-bisphosphate + ?
-
both enantiomers are substrates for the enzyme
-
-
?
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone 3-sulfate
-
17-hydroxyl of testosterone
-
-
r
3'-phosphoadenylylsulfate + tetraiodothyronine
adenosine 3',5'-bisphosphate + ?
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + Z-(+)-alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + sulfuric acid mono-[(Z)-4-[4-(2-dimethylaminoethoxy)-phenyl]-3,4-diphenylbut-3-enyl] ester
-
-
-
-
?
3'-phosphoadenylylsulfate + Z-(-)-alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + sulfuric acid mono-[(Z)-4-[4-(2-dimethylaminoethoxy)-phenyl]-3,4-diphenylbut-3-enyl] ester
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
the sulfation, catalyzed by SULT, is important in the regulation of biological activities of hormones and neurotransmitters, the metabolism of drugs, and the detoxification of xenobiotic toxicants. Sulfation also leads to the bioactivation of procarcinogens. Human SULT2A1 is a major sulfotransferase catalyzing the sulfation of hydroxysteroids and xenobiotic alcohols, mechanisms controlling the regulation of hSULT2A1, overview
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
i.e. PAPS and DHEA
-
-
?
3'-phosphoadenylyl sulfate + lithocholic acid
adenosine 3',5'-bisphosphate + lithocholate 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + lithocholic acid
adenosine 3',5'-bisphosphate + lithocholate 3-sulfate
substrate complex structure analysis
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
herbal preparations containing Aristolochia species lead to progressive nephropathy and urothelial cancer in humans, metabolic activation of aristolichic acid, mutagenic effect, overview
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
in renal target tissue, substrate of SULT1B1
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
preferred substrate of SULT2B1b
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
preferred substrate of SULT2B1b
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
SULT2A1, low activity with SULT2B1b and SULT2B1a
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
i.e. PAPS and DHEA
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
-
preferred substrate of SULT2B1a
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol sulfate
-
-
-
?
3'-phosphoadenylylsulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
steroid and bile-acid metabolism
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
sulfation is an important pathway in the metabolism of thyroid hormones, sulfated iodothyronines are elevated in nonthyroidal illnesses and in the normal fetal circulation
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
critical step in the provision of substrates for estrogen biosynthesis by the placenta during pregnancy, sulfation represents a major enzymatic reaction in the metabolism, excretion and homeostasis of steroid hormones and bile acids in addition to numerous other endogenous compounds and xenobiotics, regulating steroid hormone bioactivity
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
biotransformation of xenobiotics and hormones through sulfate conjugation, important metabolic pathway
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
biosynthesis of proteoglycans
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
catalyzes sulfonation of exogenous products like drugs and xenobiotics as well as endogenous compounds such as steroids and bile acids by transferring a sulfonate moiety from the cofactor 3'-phosphoadenosine-5'-phosphosulfate to a hydroxyl group of the substrate, this leads to detoxification or elimination because sulfation increases the hydrophilicity of chemical compounds and therefore their excretion, hEST1 also involved in the production of stable precursors for local steroid biosynthesis or in activation of promutagenic estrogen metabolites into carcinogens
-
-
r
additional information
?
-
SULT2A1 catalyzes the sulfation of hydroxysteroids such as dehydroepiandrosterone and various alcohol-containing androgens
-
-
-
additional information
?
-
-
SULT2A1 catalyzes the sulfation of hydroxysteroids such as dehydroepiandrosterone and various alcohol-containing androgens
-
-
-
additional information
?
-
cytosolic sulfotransferases (SULTs) can catalyze the sulfonation of small molecules by transferring a sulfonate group from the unique cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the substrates
-
-
-
additional information
?
-
SULT2A1 has broad substrate specificity, it can catalyze sulfonation of many hydroxysteroids, including DHEA, epiandrosterone, androsterone, testosterone, E2, cholesterol, various bile acids, pregnenolone, 17-ethinyl-E2 and cortisol
-
-
-
additional information
?
-
SULT2A1 has broad substrate specificity, it can catalyze sulfonation of many hydroxysteroids, including DHEA, epiandrosterone, androsterone, testosterone, E2, cholesterol, various bile acids, pregnenolone, 17-ethinyl-E2 and cortisol
-
-
-
additional information
?
-
-
estrone and phenolic steroids are no substrates
-
-
?
additional information
?
-
-
cortisol, corticosterone, betamathasone and dexamethasone are no substrates
-
-
?
additional information
?
-
-
hepatic clearance and metabolism of sex steroids
-
-
?
additional information
?
-
-
isoform DHEA-ST, sulfate conjugation involved in bioactivation of compounds to reactive electrophilic forms, the hydroxymethyl group is sulfated and undergoes subsequent sponaneous rearrangement to release the sulfate moiety and generate an electrophilic benzylic carbocation that can react with cellular nucleophiles such as DNA, RNA, and protein
-
-
?
additional information
?
-
-
regulation of human hepatic hydroxysteroid sulfotransferase gene expression by the peroxisome proliferator-activated receptor alpha transcription factor
-
-
?
additional information
?
-
SULT2B1 isoforms show selectivity for the sulfation of 3beta-hydroxysteroids including dehydroepiandrosterone and pregnenolone, and demonstrate little activity with 3alpha-hydroxysteroids and estrogens, SULT2B1a possesses a higher pregnenolone sulfation activity than SULT2B1b whereas SULT2B1b has a higher cholesterol sulfation activity, SULT2B1b is also capable of conjugating several drugs and xenobiotics including genistein, tibolone, and raloxifene
-
-
?
additional information
?
-
-
SULT2B1 isoforms show selectivity for the sulfation of 3beta-hydroxysteroids including dehydroepiandrosterone and pregnenolone, and demonstrate little activity with 3alpha-hydroxysteroids and estrogens, SULT2B1a possesses a higher pregnenolone sulfation activity than SULT2B1b whereas SULT2B1b has a higher cholesterol sulfation activity, SULT2B1b is also capable of conjugating several drugs and xenobiotics including genistein, tibolone, and raloxifene
-
-
?
additional information
?
-
SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview
-
-
?
additional information
?
-
role for 3'-phosphoadenylyl sulfate in priming the conformation of substrate binding loops, overview, substrate specificity and binding structure of SULT1B1, overview
-
-
?
additional information
?
-
-
SULT2B1b catalyzes the sulfonation of 3beta-hydroxysteroid hormones and cholesterol, whereas SULT2B1a preferentially catalyzes pregnenolone sulfonation
-
-
?
additional information
?
-
SULT2B1b is selective for the sulfation of 3beta-hydroxysteroids, such as DHEA, pregnenolone, androstenediol, and 5alpha-androstane-3beta,17beta-diol, no sulfation is detectable with 3alpha-hydroxysteroids or estrogens as substrates
-
-
?
additional information
?
-
-
SULT2B1b is selective for the sulfation of 3beta-hydroxysteroids, such as DHEA, pregnenolone, androstenediol, and 5alpha-androstane-3beta,17beta-diol, no sulfation is detectable with 3alpha-hydroxysteroids or estrogens as substrates
-
-
?
additional information
?
-
-
EST is an enzyme that seems to play an important role in the growth of hormone-dependent tumors of the breast, prostate, and endometrium, EST expression is downregulated in endometrial stromal sarcomas, ESS. If the enzyme EST is missing in ESS, it is possible that the intratumoral levels of bio-active estrogen are high, and ESS tumor growth and progression are to be expected, overview
-
-
?
additional information
?
-
-
pentachlorophenols, tetrachlorophenols, and trichlorophenols are substrates of isozyme SULT2A1, while mono- and dichlorophenol are poor substrates, cf. EC 2.8.2.15
-
-
?
additional information
?
-
isozymes SULT2B1a and SULT2B1b catalyze sulfonation of 3beta-hydroxysteroids, pregnenolone, 17alpha-hydroxypregnenolone and DHEA
-
-
-
additional information
?
-
isozymes SULT2B1a and SULT2B1b catalyze sulfonation of 3beta-hydroxysteroids, pregnenolone, 17alpha-hydroxypregnenolone and DHEA
-
-
-
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 + androsterone
adenosine 3',5'-bisphosphate + androsterone 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 + glycolithocholic acid
adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + lithocholic acid
adenosine 3',5'-bisphosphate + lithocholate 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + taurolithocholic acid
adenosine 3',5'-bisphosphate + taurolithocholate 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17alpha-hydroxypregnenolone
adenosine 3',5'-bisphosphate + 17alpha-hydroxypregnenolone sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 7-oxocholesterol
adenosine 3',5'-bisphosphate + 7-oxocholesterol 3-sulfate
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
herbal preparations containing Aristolochia species lead to progressive nephropathy and urothelial cancer in humans, metabolic activation of aristolichic acid, mutagenic effect, overview
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 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 sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
the sulfation, catalyzed by SULT, is important in the regulation of biological activities of hormones and neurotransmitters, the metabolism of drugs, and the detoxification of xenobiotic toxicants. Sulfation also leads to the bioactivation of procarcinogens. Human SULT2A1 is a major sulfotransferase catalyzing the sulfation of hydroxysteroids and xenobiotic alcohols, mechanisms controlling the regulation of hSULT2A1, overview
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
SULT2A1, low activity with SULT2B1b and SULT2B1a
-
-
?
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
-
steroid and bile-acid metabolism
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
sulfation is an important pathway in the metabolism of thyroid hormones, sulfated iodothyronines are elevated in nonthyroidal illnesses and in the normal fetal circulation
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
critical step in the provision of substrates for estrogen biosynthesis by the placenta during pregnancy, sulfation represents a major enzymatic reaction in the metabolism, excretion and homeostasis of steroid hormones and bile acids in addition to numerous other endogenous compounds and xenobiotics, regulating steroid hormone bioactivity
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
biotransformation of xenobiotics and hormones through sulfate conjugation, important metabolic pathway
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
biosynthesis of proteoglycans
-
-
r
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
catalyzes sulfonation of exogenous products like drugs and xenobiotics as well as endogenous compounds such as steroids and bile acids by transferring a sulfonate moiety from the cofactor 3'-phosphoadenosine-5'-phosphosulfate to a hydroxyl group of the substrate, this leads to detoxification or elimination because sulfation increases the hydrophilicity of chemical compounds and therefore their excretion, hEST1 also involved in the production of stable precursors for local steroid biosynthesis or in activation of promutagenic estrogen metabolites into carcinogens
-
-
r
additional information
?
-
SULT2A1 catalyzes the sulfation of hydroxysteroids such as dehydroepiandrosterone and various alcohol-containing androgens
-
-
-
additional information
?
-
-
SULT2A1 catalyzes the sulfation of hydroxysteroids such as dehydroepiandrosterone and various alcohol-containing androgens
-
-
-
additional information
?
-
-
regulation of human hepatic hydroxysteroid sulfotransferase gene expression by the peroxisome proliferator-activated receptor alpha transcription factor
-
-
?
additional information
?
-
SULT2B1 isoforms show selectivity for the sulfation of 3beta-hydroxysteroids including dehydroepiandrosterone and pregnenolone, and demonstrate little activity with 3alpha-hydroxysteroids and estrogens, SULT2B1a possesses a higher pregnenolone sulfation activity than SULT2B1b whereas SULT2B1b has a higher cholesterol sulfation activity, SULT2B1b is also capable of conjugating several drugs and xenobiotics including genistein, tibolone, and raloxifene
-
-
?
additional information
?
-
-
SULT2B1 isoforms show selectivity for the sulfation of 3beta-hydroxysteroids including dehydroepiandrosterone and pregnenolone, and demonstrate little activity with 3alpha-hydroxysteroids and estrogens, SULT2B1a possesses a higher pregnenolone sulfation activity than SULT2B1b whereas SULT2B1b has a higher cholesterol sulfation activity, SULT2B1b is also capable of conjugating several drugs and xenobiotics including genistein, tibolone, and raloxifene
-
-
?
additional information
?
-
SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview
-
-
?
additional information
?
-
-
EST is an enzyme that seems to play an important role in the growth of hormone-dependent tumors of the breast, prostate, and endometrium, EST expression is downregulated in endometrial stromal sarcomas, ESS. If the enzyme EST is missing in ESS, it is possible that the intratumoral levels of bio-active estrogen are high, and ESS tumor growth and progression are to be expected, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-phosphoadenylyl sulfate
substrate inhibition of SULT2A1, structure analysis of SULT2A1/DHEA and SULT2A1/PAP or SULT2A1/ADT, overview
abiraterone
antiandrogen drug, metabolite abiraterone, not the parent drug abiraterone acetate, is responsible for the inhibition
tamoxifen
tamoxifen is linked to the development of cholestasis, and it inhibits sulfotransferase 2A1 (SULT2A1)-catalyzed dehydroepiandrosterone (DHEA) sulfonation
3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide
DBHM
3,5-dibromo-4-hydroxybenzoic acid (6,8-dichloro-4-oxo-4H-chromen-3-ylmethylene) hydrazide
DBHD
abiraterone
antiandrogen drug, metabolite abiraterone, not the parent drug abiraterone acetate, is responsible for the inhibition
adenosine 5'-(beta,gamma-imido) triphosphate
i.e. AMP-PNP, a non-hydrolysable ATP analogue
dehydroepiandrosterone
substrate inhibition of SULT2B1a and SULT2B1b
S-(-)-1-naphthyl-1-ethanol
-
inhibitor of the sulfation of dehydroepiandrosterone
dehydroepiandrosterone
substrate inhibition of SULT2A1, structure analysis of SULT2A1/DHEA and SULT2A1/PAP or SULT2A1/ADT, overview
dehydroepiandrosterone
the potent substrate inhibition can be explained by trapping PAP in a dead-end complex, which impedes the release of the nucleotide coenzyme
raloxifene
raloxifene is linked to the development of cholestasis, and it inhibits sulfotransferase 2A1 (SULT2A1)-catalyzed dehydroepiandrosterone (DHEA) sulfonation, full noncompetitive inhibition
additional information
2-mercaptoethanol and DL-dithiothreitol do not affect the enzyme activity
-
additional information
hydroxylated and sulfated metabolites of commonly occurring airborne polychlorinated biphenyls inhibit human steroid sulfotransferases SULT1E1 (EC 2.8.2.4) and SULT2A1. No inhibition by 3,3'-dichloro-4-biphenylsulfate at up to 0.01 mM
-
additional information
-
hydroxylated and sulfated metabolites of commonly occurring airborne polychlorinated biphenyls inhibit human steroid sulfotransferases SULT1E1 (EC 2.8.2.4) and SULT2A1. No inhibition by 3,3'-dichloro-4-biphenylsulfate at up to 0.01 mM
-
additional information
inhibition of human sulfotransferase 2A1-catalyzed sulfonation of lithocholic acid (LCA), glycolithocholic acid (GLCA), and taurolithocholic acid (TLCA) by selective estrogen receptor modulators and various analogs and metabolites. The triphenylethylene, benzothiophene, tetrahydronaphthalene, indole, and and benzopyran classes of selective estrogen receptor modulator (SERM) inhibit LCA, GLCA, and TLCA sulfonation, mode of inhibition, and MIC values, overview. Bazedoxifene and raloxifene are the most effective inhibitors of LCA, GLCA, and TLCA sulfonation, while tamoxifen is the least potent inhibitor. No inhibition by amoxicillin. The order of inhibition of LCA sulfonation by toremifene and its oxidative metabolites is N-desmethyl-4-hydroxytoremifene > 4-hydroxytoremifene > toremifene > N-desmethyltoremifene
-
additional information
-
environmental contaminants may exert effects on neuronal function both by direct inhibition of sulfotransferase enzymes and by interrupting the supply of PAPS
-
additional information
-
rifampicin-liganded PXR suppresses SULT2A1 expression by interfering with HNF4alpha activity, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaCl
-
leads to a greater activation of the cDNA-expressed DHEA ST when assayed with dehydroepiandrosterone
additional information
methotrexate and 6-(4-chlorophenyl)imidazo [2,1-b][1,3] thiazole-5-carbaldehyde O-(3,4-dichlorobenzyl)oxime induction of hSULT2A1 through interacting with androstane receptor and retinoid X receptor alpha mediated by the IR2 element, mechanism, overview
-
additional information
-
rifampicin induces SULT2A1 expression about 12fold in a manner dependent on 5'-flanking regions containing rifampicin-responsive information as a hepatocyte nuclear factor 4, HNF4, binding site. Upregulation of SULT2A1 does not occur in cells, that do not contain the binding site. Binding of HNF4 to the HNF4-54 region of the endogenous SULT2A1 gene leads to increased SULT2A1 mRNA production and enzyme activity, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
dehydroepiandrosterone
SULT2A1, pH and temperature not specified in the publication
0.0036
dehydroepiandrosterone
pH 7.0, 25°C, recombinant mutant M137I/Y238A
0.0042
dehydroepiandrosterone
pH 7.0, 25°C, recombinant mutant M137V/Y238A
0.0065
dehydroepiandrosterone
pH 7.0, 25°C, recombinant mutant M137V/Y238A
0.0006
dehydroepiandrosterone
pH 7.5, 37°C, recombinant truncated mutant SULT2B1
0.0023
dehydroepiandrosterone
isoform SULT2B1a, pH and temperature not specified in the publication
0.0023
dehydroepiandrosterone
SULT2B1a, pH and temperature not specified in the publication
0.0025
dehydroepiandrosterone
isoform SULT2A1, pH and temperature not specified in the publication
0.0038
dehydroepiandrosterone
pH 7.5, 37°C, recombinant wild-type, full-length SULT2B1
0.0044
dehydroepiandrosterone
isoform SULT2B1b, pH and temperature not specified in the publication
0.0044
dehydroepiandrosterone
SULT2B1b, pH and temperature not specified in the publication
additional information
additional information
substrate binding kinetics
-
additional information
additional information
the complete kinetic mechanism of SULT2A1 has been defined, which reveals that the binding of DHEA and PAPS is random, while the rate-limiting step is nucleotide release
-
additional information
additional information
the complete kinetic mechanism of SULT2A1 has been defined, which reveals that the binding of DHEA and PAPS is random, while the rate-limiting step is nucleotide release
-
additional information
additional information
the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the kinetic activity of this SULT isoform, overview
-
additional information
additional information
-
the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the kinetic activity of this SULT isoform, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
arzoxifene
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid, mixed inhibition
0.0002
bazedoxifene
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid, noncompetitive inhibition
0.0058
clomifene
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid, competitive inhibition
0.0046
droloxifene
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid, mixed inhibition
0.0008
lasofoxifene
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid, noncompetitive inhibition
0.0005
raloxifene
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid, noncompetitive inhibition
0.0061
dehydroepiandrosterone
SULT2A1, pH and temperature not specified in the publication
0.466
dehydroepiandrosterone
pH 7.0, 25°C, recombinant mutant M137V/Y238A
0.022
dehydroepiandrosterone
SULT2B1b, pH and temperature not specified in the publication
0.048
dehydroepiandrosterone
SULT2B1a, pH and temperature not specified in the publication
additional information
additional information
inhibition kinetics and modeling, detailed overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
2,2',5,5'-tetrachloro-4-biphenylsulfate
Homo sapiens
recombinant SULT2A1, pH 7.4, 37°C
-
0.0013
2,2',5,5'-tetrachloro-4-hydroxybiphenyl
Homo sapiens
recombinant SULT2A1, pH 7.4, 37°C
-
0.0049
2,3',4-trichloro-4'-hydroxybiphenyl
Homo sapiens
recombinant SULT2A1, pH 7.4, 37°C
-
0.046
2,4'-dichloro-4-biphenylsulfate
Homo sapiens
recombinant SULT2A1, pH 7.4, 37°C
-
0.0015
2,4'-dichloro-4-hydroxybiphenyl
Homo sapiens
recombinant SULT2A1, pH 7.4, 37°C
-
0.023
3,3'-dichloro-4-hydroxybiphenyl
Homo sapiens
recombinant SULT2A1, pH 7.4, 37°C
-
0.0018
4'-hydroxytoremifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.0044
4-hydroxytoremifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.0029
7-methoxylasofoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.00006
bazedoxifene N-oxide
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.0014
cis-4-(1,2,3,4-tetrahydro-6-methoxy-2-phenyl-1-naphthalenyl)phenol
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.00016
des(1-azepanyl)ethylbazedoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.0129
N-desmethyl-4-hydroxytoremifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.0184
N-desmethyltoremifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
-
0.007
acolbifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0101
acolbifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.0129
acolbifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.00008
arzoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0002
arzoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.00029
arzoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.00013
bazedoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.00021
bazedoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.00029
bazedoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.0015
clomifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0036
clomifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.00075
droloxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0015
droloxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.0015
droloxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.00025
lasofoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0005
lasofoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.001
lasofoxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.0014
nafoxidine
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0066
nafoxidine
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.0122
nafoxidine
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.0023
ospemifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.00255
ospemifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.00018
raloxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.00028
raloxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
0.00041
raloxifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.0101
tamoxifen
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0137
tamoxifen
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate glycolithocholic acid
0.0032
toremifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate taurolithocholic acid
0.0092
toremifene
Homo sapiens
liver cytosol, pH 7.4, 37°C, substrate lithocholic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
enzyme activity at pH 5.0 is 6% of the maximum in the optimum range, 50% of activity maximum at pH 6.0, no activity is detected at either pH 4.0 or 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
enzyme activity at 25°C and 30°C drops to 35% and 56%, repective to the maximum activity at 45°C, residual activity is determined to be 62% of the maximum at 50°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
endometrial stromal, from 29 patients, reduced or no expression of EST
additional information
-
present in proximal and distal tubules, loops of Henle and collecting ducts, but at no time expressed in the vascular glomerulus
-
-
645741, 645778, 645779, 645780, 645782, 645783, 645785, 645786, 645789, 645790, 645797, 692098, 693816
prostate epithelial cells, prostate benign prostatic hyperplasia, prostate adenocarcinoma and LNCaP prostate adenocarcinoma cells
additional information
no expression of SULT2B1b in alveolar tissue and in liver cytosol
additional information
-
no expression of SULT2B1b in alveolar tissue and in liver cytosol
additional information
androgen responsive cell lines LNCaP, VCaP, RWPE-1, and the castration nonresponsive line C4-2 generally express higher levels of SULT2B1b than AR- cell lines, such as PC-3 and DU-145 cells
additional information
the SULT2B1 isoforms SULT2B1a and SULT2B1b are expressed in different tissues. SULT1B1a is expressed in colon, ovary, and fetal brain, and SULT2B1b in liver, colon, small intestine, placenta, ovary, uterus, and prostate
additional information
the SULT2B1 isoforms SULT2B1a and SULT2B1b are expressed in different tissues. SULT1B1a is expressed in colon, ovary, and fetal brain, and SULT2B1b in liver, colon, small intestine, placenta, ovary, uterus, and prostate
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
isozyme SULT2B1b, T47D or MCF-7 breast cancer cells, in prostate epithelial cells, prostate benign prostatic hyperplasia, prostate adenocarcinoma and LNCaP prostate adenocarcinoma cells isozyme SULT2B1b is expressed only in the cytosol
the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the nuclear translocation of this SULT isoform, overview
isozyme SULT2B1b, T47D or MCF-7 breast cancer cells, SULT2B1b is not tightly bound in the nuclei
the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the nuclear translocation of this SULT isoform, overview
additional information
a unique 3'-extension of SULT2B1b is required for nuclear localization in human BeWo placental choriocarcinoma cells, the nuclear localization is stimulated by forskolin treatment in BeWo cells and serine phosphorylation in the 3'-extension
-
additional information
-
a unique 3'-extension of SULT2B1b is required for nuclear localization in human BeWo placental choriocarcinoma cells, the nuclear localization is stimulated by forskolin treatment in BeWo cells and serine phosphorylation in the 3'-extension
-
additional information
-
subcellular localization of isozymes SULT2B1a and SULT2B1b, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
malfunction
metabolism
physiological function
additional information
mechanism for the effect of cofactor (PAP) and ligands (LCA, raloxifene, alpha-hydroxytamoxifen, ouabain, and 3'-phosphoadenylyl sulfate) on structural stability and selectivity of SULT2A1 from the perspective of the dynamic behavior of SULT2A1 structures. Structural stability and network analyses indicated that the cooperation between PAP and LCA may enhance the thermal stability and compact communication in enzymes. Molecular dynamic simulations, docking study using the crystal structure of the SULT2A1 complex with PAP and lithocholic acid (LCA) (PDB ID 3F3Y). The free SULT2A1 and binary complexes (SULT2A1/LCA and SULT2A1/PAP) are derived from the crystal structure of the SULT2A1 complex with both PAP and LCA (PDB ID3F3Y), modeling, detailed overview. The smaller substrates such as LCA could bind stably to the active pocket in the presence of PAP. The substrates or inhibitors with a large spatial structure need to bind to the open conformation (without PAP) prior to PAPS binding
evolution
human cytosolic sulfotransferases (hSULTs) canbe classified into four families (hSULT1, hSULT2, hSULT4, and hSULT6) based on sequence similarity
evolution
more than 160 cSNPs have been reported for SULT2A1. SULT2A1 SNPs Ala63Pro, Lys227Glu, and Ala261Thr have only been found in African-American populations, and these might explain the interethnic differences in SULT2A1 activity
malfunction
Functional analysis has revealed that the nonsynonymous SNPs Met57Thr, Glu186Val, Ala63Pro, and Lys227Glu result in decreased SULT2A1 activity when expressed in COS-1 cells
malfunction
tamoxifen or raloxifene are linked to the development of cholestasis, and inhibit sulfotransferase 2A1 (SULT2A1)-catalyzed dehydroepiandrosterone (DHEA) sulfonation
metabolism
both SULT1E1 and SULT2A1 can play important roles in steroid signaling through regulation of the active forms of the hormones
metabolism
in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Further activation of estrone to the most potent estrogen, estradiol, is catalyzed by 17-ketosteroid reductases, while estradiol can also be formed from dehydroepiandrosterone by the sequential actions of 3beta-hydroxysteroid dehydrogenase-DELTA4-isomerase, aromatase, and 17-ketosteroid reductase. Roles of the STS and SULT enzymes in local estrogen biosynthesis, overview. The expression of SULT2A1 is regulated at the transcriptional level by the constitutive androstane receptor and pregnane X receptor
physiological function
cytosolic sulfotransferases (SULTs) act as phase II metabolic enzymes
physiological function
in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Sulfotransferases 2A1 (SULT2A1) and SULT2B1 catalyze the conjugation of dehydroepiandrosterone (DHEA). In general, SULT2s catalyze sulfonation of the hydroxyl groups of steroids (SULT2A1, SULT2B1)
physiological function
SULT2A1 catalyzes the formation of dehydroepiandrosterone sulfate (DHEAS) the most abundant circulating steroid in humans. DHEAS serves as a transport form for dehydroepiandrosterone (DHEA) in the serum. Following uptake of DHEAS by tissues and its subsequent hydrolysis catalyzed by steroid sulfatase, DHEA serves as a precursor for both androgens and estrogens
malfunction
knock-down of SULT2B1b inhibits cell growth and cyclinB1 levels in human hepatocarcinoma cells and suppressed xenograft growth in vivo
malfunction
knockout of SULT2B1b increases tumor necrosis factor alpha (TNF) expression in prostate cancer cells and results in NF-kappaB activation in a TNF-dependent manner. More importantly, SULT2B1b knockout significantly enhances TNF-mediated apoptosis in both TNF-sensitive LNCaP cells and TNF-resistant C4-2 cells. Overexpression of SULT2B1b in LNCaP cells also decreases sensitivity to TNF-mediated cell death, suggesting that SULT2B1b modulates pathways dictating the TNF sensitivity capacity of prostate cancer cells. RNA interference (RNAi)-mediated knockdown (KD) of SULT2B1b, the cholesterol sulfotransferase, induces apoptosis in a variety of prostate cancer cell lines including C4-2 cells, a model of CRPC. NF-kappaB activation by SULT2B1b knockdown is due to the induction of TNF expression in LNCaP cells
malfunction
SULT2B1b knockdown induces cell death in prostate cancer cells. SULT2B1b knockdown increases the percentage of sub-G1 nuclei by cell-cycle analysis and significantly increased caspase-3 activity and PARP cleavage in LNCaP, VCaP, and C4-2 cells. Targeted knockdown of SULT2B1b impairs growth/viability of prostate cancer cells and induces apoptosis. LNCaP cells with SULT2B1b overexpression (hSULT2B1b vector) show a significant decrease in liver X receptor (LXR) activity and a trend of decreased transcription of downstream target gene, ATP-binding cassette (ABC)-G1. LXR activity in LNCaP cells has been demonstrated to be due to transcriptional activation of LXRbeta
metabolism
in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Further activation of estrone to the most potent estrogen, estradiol, is catalyzed by 17-ketosteroid reductases, while estradiol can also be formed from dehydroepiandrosterone by the sequential actions of 3beta-hydroxysteroid dehydrogenase-DELTA4-isomerase, aromatase, and 17-ketosteroid reductase. Roles of the STS and SULT enzymes in local estrogen biosynthesis, overview
metabolism
regulation of cholesterol sulfotransferase SULT2B1b by hepatocyte nuclear factor 4alpha constitutes a negative feedback control of hepatic gluconeogenesis. The SULT2B1b gene is a transcriptional target of HNF4alpha
metabolism
SULT2B1b expression is inversely correlated with TNF-related genes, including TNF, CD40LG, FADD, and NFKB1
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
cholesterol sulfotransferase, SULT2B1b, modulates both androgen receptor activity and cell growth properties within prostate cancer cells. SULT2B1b regulates TNF-mediated cell signaling
physiological function
in peripheral tissues, estrogens can be formed from the inactive precursors dehydroepiandrosterone sulfate and estrone sulfate. Sulfatase and sulfotransferases have pivotal roles in these processes, where sulfatase hydrolyzes estrone sulfate to estrone, and dehydroepiandrosterone sulfate to dehydroepiandrosterone, and sulfotransferases catalyze the reverse reactions. Sulfotransferases 2A1 (SULT2A1) and SULT2B1 catalyze the conjugation of dehydroepiandrosterone (DHEA). In general, SULT2s catalyze sulfonation of the hydroxyl groups of steroids (SULT2A1, SULT2B1)
physiological function
role of SULT2B1b in the growth and progression of cancer cells. Cholesterol sulfate accumulation correlates with SULT2B1b expression in prostate cancer cells and human prostate specimens. SULT2B1b activity modulates androgen receptor (AR) activity in prostate cancer cells, SULT2B1b is a regulator of AR activity and cell growth in prostate cancer
physiological function
sulfotransferases (SULTs) catalyze the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to an acceptor molecule. Sulfation plays an essential role in regulating the chemical and functional homeostasis of endogenous and exogenous molecules. The cholesterol sulfotransferase SULT2B1b preferentially catalyzes the sulfoconjugation of cholesterol to synthesize cholesterol sulfate. SULT2B1b inhibits hepatic gluconeogenesis by antagonizing the gluconeogenic activity of hepatocyte nuclear factor 4alpha (HNF4alpha). Regulation of cholesterol sulfotransferase SULT2B1b by hepatocyte nuclear factor 4alpha constitutes a negative feedback control of hepatic gluconeogenesis. SULT2B1b also plays a restrictive role in HNF4alpha-mediated fasting-responsive gluconeogenesis
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). ST2A1_HUMAN
285
0
33780
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33770
-
calculated from putative amino acid sequence, estimated from cDNA
34000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
detailed structural analysis and comparison of SULT family enzymes, comparison of substrate binding structures of SULT1B1, overview, chemical library preparation and ligand binding screens
additional information
SULT2B1 isoforms possess a 50 amino acid N-terminal extension that is enriched in serine and proline residues
additional information
-
SULT2B1 isoforms possess a 50 amino acid N-terminal extension that is enriched in serine and proline residues
additional information
SULT2B1b has an extension at the proline- and serine-rich carboxyl end of about 53 amino acids, structure and function, the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the immunogenicity, nuclear translocation, kinetic activity, and thermostability of this SULT isoform, overview
additional information
-
SULT2B1b has an extension at the proline- and serine-rich carboxyl end of about 53 amino acids, structure and function, the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the immunogenicity, nuclear translocation, kinetic activity, and thermostability of this SULT isoform, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
recombinant wild-type, full-length SULT2B1b, but not truncated SULT2B1b, is phosphorylated by casein kinase or Cdc2 protein kinase in vitro
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutants M137I and M137W, hanging drop vapor diffusion method at 18°C, 0.002 ml hanging drops by mixing equal volumes of protein solution and a reservoir solution containing 1.6 M (NH4)2SO4, 100 mM NaCl, and 0.1 M HEPES at pH 7.5, 3-7 days, X-ray diffraction structure determination and analysis at 2.6 and 3.0 A resolution, respectively, modeling
several crystal structures of SULT2A1 binary complexes have been resolved, including complexes with DHEA (PDB ID 1J99) and PAPS (PDB ID 4IFB)
crystal structure analysis of both SULT2B1a and SULT2B1b in binary complexes with PAP (PDB IDs 1Q1Q, and 1Q1Z, respectively) have been resolved, as have two ternary complexes of SULT1Bb with PAP and pregnenolone (PDB ID 1Q2O), and with PAP and DHEA (PDB ID 1Q22)
purified SULT1B1 is crystallized in the presence of 2 mM PAP using the hanging drop method at 20°C by mixing for SULT1B1: 0.002 ml of the protein solution with 0.002 ml of the reservoir solution containing 0.1 M Bis-Tris, pH 6.5, 0.2 M ammonium sulfate and 16%-20% PEG 4000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A261T
polymorphism of SULT2A1. The SULT2A1 SNP Ala261Thr has an allele frequency of 13% in African-American populations and is located within the dimerization motif, where it prevents formation of SULT2A1 dimers. But Ala261Thr still has 93% of the wild-type enzyme activity
A63P
polymorphism of SULT2A1. The SULT2A1 SNP Ala63Pro has an allele frequency of 5% in African-American populations
M137I
site-directed mutagenesis, substrate binding structure, the Ki for androsterone is increased 28.6fold compared to the wild-type enzyme, overview
M137V
site-directed mutagenesis, substrate binding structure, the Ki for androsterone is increased 5fold and for dehydroepiandrosterone 9fold compared to the wild-type enzyme, overview
M137V/Y238A
site-directed mutagenesis, the mutant shows no substrate inhibition by dehydroepiandrosterone
M137W
site-directed mutagenesis, substrate binding structure, the Ki for androsterone is increased 11.1fold compared to the wild-type enzyme, overview
M137W/Y238A
site-directed mutagenesis, the mutant shows no substrate inhibition by dehydroepiandrosterone
V260A/Y238A
site-directed mutagenesis, a monomeric mutant, shows increased Ki for dehydroepiandosterone compared to the wild-type enzyme, no inhibition by androsterone
Y238A
site-directed mutagenesis, exhibits no substrate inhibition with ADT as substrate, the Ki value of DHEA increases 7.4fold compared with that of wild-type SULT2A1, no inhibition by androsterone
Y238F
site-directed mutagenesis, the Ki values of DHEA and ADT for Y238F SULT2A1 mutant increase for approximately 2 to 3fold compared with those of the wild type enzyme
Y238W
site-directed mutagenesis, the Ki values of DHEA and ADT for Y238W SULT2A1 mutant increase for approximately 2 to 3fold compared with those of the wild type enzyme
additional information
additional information
SULT2A1 downreguletion by siRNA, and progressive promoter deletion, expression analysis. An IR2 element of the hSULT2A1 promoter region mediates the methotrexate induction of hSULT2A1 through interacting with androstane receptor and retinoid X receptor alpha
additional information
more than 160 cSNPs are reported for SULT2A1. Functional analysis has revealed that the nonsynonymous SNPs Met57Thr, Glu186Val, Ala63Pro, and Lys227Glu result in decreased SULT2A1 activity when expressed in COS-1 cells
additional information
more than 160 cSNPs are reported for SULT2A1. Functional analysis has revealed that the nonsynonymous SNPs Met57Thr, Glu186Val, Ala63Pro, and Lys227Glu result in decreased SULT2A1 activity when expressed in COS-1 cells
additional information
construction of a truncated mutant SULT2B1b lacking the 53 amino acid-proline- and serine-rich carboxyl extension, the mutant enzyme shows decreased Km for dehydroepiandrosterone and a kcat reduced by 91% compared to the wild-type full-length SULT2B1b
additional information
-
construction of a truncated mutant SULT2B1b lacking the 53 amino acid-proline- and serine-rich carboxyl extension, the mutant enzyme shows decreased Km for dehydroepiandrosterone and a kcat reduced by 91% compared to the wild-type full-length SULT2B1b
additional information
-
construction of truncated SULT2B1a and SULT2B1b variants that lack the SULT2B1 proline-rich tail, genotype-to-phenotype approach to identify and characterize common sequence variation in SULT2B1, determination and analysis of 100 polymorphisms in African-American and Caucasian-American individuals, including four nonsynonymous coding single nucleotide polymorphisms and one 6-base pair deletion, within the shared region of the open reading frame, overview
additional information
-
construction of truncated SULT2b1a and SULT2B1b variants by site-directed mutagenesis to introduce a translation termination codon immediately before the final 53 amino acids at the C terminus of the protein. Pharmacogenomics, gene sequence variation and functional genomics, determination of 100 polymorphisms, including four nonsynonymous coding single nucleotide polymorphisms and one 6-base pair deletion, in African-American and Caucasian-American individuals, overview
additional information
construction of SULT2B1b knockdown prostate cells using siRNA or shRNA targeting and LNCaP cells. SULT2B1b knockdown results in a decrease in growth/viability of LNCaP, VCaP, C4-2, and RWPE-1 cells as well as decreased softagar colony formation in LNCaP cells, and it induces cell death in prostate cancer cells. A significant decrease in cell growth/viability is observed using multiple SULT2B1b RNAi sequences in LNCaP cells. SULT2B1b knockdown increases the percentage of sub-G1 nuclei by cell-cycle analysis and significantly increased caspase-3 activity and PARP cleavage in LNCaP, VCaP, and C4-2 cells. LNCaP cells with SULT2B1b knockdown analyzed by flow cytometry show an increased percentage of Annexin V+/propidium iodide (PI)x02cells compared with control cells. Double KD of SULT2B1b/LXRbeta does not affect the siRNA knockdown efficiency compared with SULT2B1b or LXRbeta knockdown alone. LNCaP cells with SULT2B1b overexpression (hSULT2B1b vector) show a significant decrease in liver X receptor (LXR) activity and a trend of decreased transcription of downstream target gene, ATP-binding cassette (ABC)-G1. LXR activity in LNCaP cells has been demonstrated to be due to transcriptional activation of LXRbeta. Phenotype of SULT2B1b knockout cells, overview
additional information
construction of SULT2B1b knockdown prostate cells using siRNA targeting, single-cell mRNA sequencing (scRNA-seq) is conducted to compare the transcriptomes of SULT2B1b KO cells versus control KD LNCaP cells. NF-kappaB activation is induced by TNF expression within SULT2B1b-deficient LNCaP cells. In C4-2 cells with knocked down SULT2B1b, neither TNF expression nor NF-kappaB activity is significantly increased, but SULT2B1b knockdown does activate phosphorylation of IkappaB
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 43
42
30 min, the activity of the recombinant wild-type, full-length SULT2B1b is reduced by 30%, but the activity of the recombinant truncated SULT2B1bmutant is reduced 3.5fold more
additional information
additional information
the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the thermostability of this SULT isoform, overview
additional information
-
the proline- and serine-rich carboxyl extension of SULT2B1b is an important site in the thermostability of this SULT isoform, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full-length SULT2B1b and of truncated SULT2B1b lacking proline- and serine-rich carboxyl extension from Escherichia coli strain DH5alpha by nickel affinity chromatography
recombinant SULT2A1 from Escherichia coli by anion exchange chromatography, ultrafiltration, and hydroxyapatite chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SULT2A1, localized to chromosome 19 (19q13.3), different transcripts and genetic variants, overview
recombinant expression of the enzyme in Escherichia coli strain BL21(DE3)
SULT2A1, expression in Caco-2 cells and analysis of the transcriptional regulation mechanism of hSULT2A1 promoter, quantitative enzyme expression analysis. Constitutive androstane receptor and retinoid X receptor alpha are involved in the transcriptional regulation of hSULT2A1, overview
cDNA encoding alcohol/hydroxysteroid sulfotransferase h-ST-a cloned from a liver cDNA library
-
cDNA encoding liver DHEA-ST isolated from Uni-Zap XR human liver cDNA library cloned, expressed in green monkey COS-7 cells
-
DHEA-ST cloned and expressed in glutathione sulfotransferase fusion form in Escherichia coli
-
DHEA-ST cloned and expressed in Salmonella typhimurium, Escherichia coli and COS cells
-
expression of GFP-tagged wild-type allozymes and mutant truncated SULT2B1a and SULT2B1b variants lacking the SULT2B1 proline-rich tail in COS-1 cells
-
expression of His-tagged full-length SULT2B1b and of truncated SULT2B1b lacking proline- and serine-rich carboxyl extension in Escherichia coli strain DH5alpha, expression and serine phosphorylation of SULT2B1b in transfected BeWo cells, overview
expression of SULT2B1b eliminates the cytotoxic effect of 7-oxo-cholesterol on 293T cells, which are normally devoid of SULT2B1b
expression of SULTs in Escherichia coli strain BL21 DE3, in Salmonella typhimurium strain TA1538, and in chinese hamster V79 cells, and application of aristolochic acid, mutagenicity with expression of different SULT isozymes and allozymes of SULT1A1, detailed overview
gene SULT2B1, localized to chromosome 19 (19g13.3), isozymes SULT2B1a and SULT2B1b, different transcripts and genetic variants, overview. The SULT2B1 isoforms SULT2B1a and SULT2B1b are products of alternative transcriptional initiation and mRNA splicing of the same gene. SULT1B1a and SULT1B1b, which has an additional 23 N-terminal amino-acid residues, have been cloned and expressed in prokaryotic and eukaryotic systems
gene SULT2B1b, quantitative RT-PCR enzyme expression analysis, recombinant overexpression in LNCaP and DU-145 prostate cells
isozymes SULT2B1a and SULT2B1b are encoded by a single SULT2B1 gene as a result of alternative transcription initiation and alternative splicing, genotyping of African-American and Caucasian-American individuals, transient expression of GFP-tagged SULT2B1a and SULT2B1b in COS-1 cells, in vitro transcription and translation of truncated SULT2B1a and SULT2B1b variants that lack the SULT2B1 proline-rich tail using rabbit reticulocyte lysate
-
SULT2A1 real time RT-PCR expression analysis in presence of different plasticizers
-
SULT2B1a and SULT2B1b, DNA and amino acid sequence determination and analysis, genetic structure, the two different isozymes are encoded by the gene SULT2B1 utilizing different start sites of transcription resulting in the incorporation of different first exons, SULT2B1a and SULT2B1b are 350 and 365 amino acids in length, respectively, and the last 342 amino acids are identical, expression of His-tagged or GST-tagged SULT2B1b in Escherichia coli, expression of SULT2B1a and SULT2B1b in COS-1 cells
transient expression of SULT2A1 in Hep-G2 cells, expression analysis in presence or absence of rifampicin and/or PXR, regulation, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
The expression of SULT2A1 is regulated at the transcriptional level by the constitutive androstane receptor and pregnane X receptor. SULT2A1 appears to be regulated also at the epigenetic level, as shown by induction of SULT2A1 expression after treatment of MCF7 cells with a histone deacetylase inhibitor. In the adrenal gland, the expression of SULT2A1 depends on two transcription factors: steroidogenic factor 1 and GATA-6
the SULT2A1 gene is induced by E2 activation of estrogen receptor (ER)alpha via classical, direct binding to the estrogen response element, and via nonclassical, AP-1-mediated mechanisms
HNF4alpha induces the expression of SULT2B1b in human liver cells. In the human hepatoma HepG2 cells, transfection with the HNF4alpha expression vector increases the expression of SULT2B1b. In human primary hepatocytes (HPH), treatment of cells with the HNF4alpha activator linoleic acid induces the expression of both SULT2B1b
the basal expression levels of SULT2B1b and G6Pase ae decreased in human primary epatocytes treated with the HNF4alpha inhibitor BIM5078
the expression of SULT2B1 at the mRNA level is decreased in ovarian endometriosis compared to normal endometrium
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
cytosolic sulfotransferases (SULTs) acting as phase II metabolic enzymes can be used in the sulfonation of small molecules by transferring a sulfonate group from the unique co-factor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the substrates
analysis
a modified variant of sulfotransferase assay employs permeabilized fission yeast cells (enzyme bags). A new and convenient SULT activity assay is based on the sulfation of a proluciferin compound, which is catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1
medicine
synthesis
generation of a complete set of recombinant fission yeast strains each expressing one of the 14 human SULT enzymes. The intracellular production of the cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) necessary for SULT activity is sufficiently high to support metabolite production
medicine
-
hEST1 involved in the production of stable precursors for local steroid biosynthesis or in activation of promutagenic estrogen metabolites into carcinogens
medicine
-
isoenzyme EST 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
-
diagnostic of liver diseases, in chronic hepatitis the immunopositive area of DHEA-ST is significantly increased compared to normal liver
medicine
the HNF4alpha-SULT2B1b-CS axis represents a key endogenous mechanism to prevent uncontrolled gluconeogenesis. Thiocholesterol may be used as a therapeutic agent to manage hyperglycemia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Hernandez, J.S.; Watson, R.W.G.; Wood, T.C.; Weinshilboum, R.M.
Sulfation of estrone and 17beta-estradiol in human liver. Catalysis by thermostable phenol sulfotransferase and by dehydroepiandrosterone sulfotransferase
Drug Metab. Dispos.
20
413-422
1992
Homo sapiens
Kong, A.N.T.; Yang, L.; Ma, M.; Tao, D.; Bjornsson, T.D.
Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver
Biochem. Biophys. Res. Commun.
187
448-454
1992
Homo sapiens
Comer, K.A.; Falany, J.L.; Falany, C.N.
Cloning and expression of human liver dehydroepiandrosterone sulphotransferase
Biochem. J.
289
233-240
1993
Homo sapiens
-
Barker, E.V.; Hume, R.; Hallas, A.; Coughtrie, W.H.
Dehydroepiandrosterone sulfotransferase in the developing human fetus: quantitative biochemical and immunological characterization of the hepatic, renal, and adrenal enzymes
Endocrinology
134
982-989
1994
Homo sapiens
Falany, C.N.; Comer, K.A.; Dooley, T.P.; Glatt, H.
Human dehydroepiandrosterone sulfotransferase. Purification, molecular cloning, and characterization
Ann. N. Y. Acad. Sci.
774
59-72
1995
Homo sapiens
Strott, C.A.
Steroid sulfotransferases
Endocr. Rev.
17
670-697
1996
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus
Kudlacek, P.E.; Clemens, D.L.; Halgard, C.M.; Anderson, R.J.
Characterization of recombinant human liver dehydroepiandrosterone sulfotransferase with minoxidil as the substrate
Biochem. Pharmacol.
53
215-221
1997
Homo sapiens
Li, X.; Anderson, R.J.
Sulfation of iodothyronines by recombinant human liver steroid sulfotransferases
Biochem. Biophys. Res. Commun.
263
632-639
1999
Homo sapiens
Narasaka, T.; Moriya, T.; Endoh, M.; Suzuki, T.; Shizawa, S.; Mizokami, Y.; Matsuoka, T.; Sasano, H.
17Beta-hydroxysteroid dehydrogenase type 2 and dehydroepiandrosterone sulfotransferase in the human liver
Endocr. J.
47
697-705
2000
Homo sapiens
Chang, H.J.; Zhou, M.; Lin, S.X.
Human dehydroepiandrosterone sulfotransferase: purification and characterization of a recombinant protein
J. Steroid Biochem. Mol. Biol.
77
159-165
2001
Homo sapiens
Faucher, F.; Lacoste, L.; Luu-The, V.
Human type 1 estrogen sulfotransferase: catecholestrogen metabolism and potential involvement in cancer promotion
Ann. N. Y. Acad. Sci.
963
221-228
2002
Homo sapiens
Meloche, C.A.; Sharma, V.; Swedmark, S.; Andersson, P.; Falany, C.N.
Sulfation of budesonide by human cytosolic sulfotransferase, dehydroepiandrosterone-sulfotransferase (DHEA-ST)
Drug Metab. Dispos.
30
582-585
2002
Homo sapiens (O00204)
Miki, Y.; Nakata, T.; Suzuki, T.; Darnel, A.D.; Moriya, T.; Kaneko, C.; Hidaka, K.; Shiotsu, Y.; Kusaka, H.; Sasano, H.
Systemic distribution of steroid sulfatase and estrogen sulfotransferase in human adult and fetal tissues
J. Clin. Endocrinol. Metab.
87
5760-5768
2002
Homo sapiens
Nishiyama, T.; Ogura, K.; Nakano, H.; Kaku, T.; Takahashi, E.; Ohkubo, Y.; Sekine, K.; Hiratsuka, A.; Kadota, S.; Watabe, T.
Sulfation of environmental estrogens by cytosolic human sulfotransferases
Drug Metab. Pharmacokinet.
17
221-228
2002
Homo sapiens, Homo sapiens (Q06520)
Rehse, P.H.; Zhou, M.; Lin, S.X.
Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate
Biochem. J.
364
165-171
2002
Homo sapiens
Lee, K.A.; Fuda, H.; Lee, Y.C.; Negishi, M.; Strott, C.A.; Pedersen, L.C.
Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms
J. Biol. Chem.
278
44593-44599
2003
Homo sapiens (O00204), Homo sapiens
Sheng, J.J.; Duffel, M.W.
Enantioselectivity of human hydroxysteroid sulfotransferase ST2A3 with naphthyl-1-ethanols
Drug Metab. Dispos.
31
697-700
2003
Homo sapiens
Schneider, H.; Glatt, H.
Sulpho-conjugation of ethanol in humans in vivo and by individual sulphotransferase forms in vitro
Biochem. J.
383
543-549
2004
Homo sapiens
Apak, T.I.; Duffel, M.W.
Interactions of the stereoisomers of alpha-hydroxytamoxifen with human hydroxysteroid sulfotransferase SULT2A1 and rat hydroxysteroid sulfotransferase STa
Drug Metab. Dispos.
32
1501-1508
2004
Homo sapiens, Rattus norvegicus
Stanley, E.L.; Hume, R.; Coughtrie, M.W.H.
Expression profiling of human fetal cytosolic sulfotransferases involved in steroid and thyroid hormone metabolism and in detoxification
Mol. Cell. Endocrinol.
240
32-42
2005
Homo sapiens
Fang, H.L.; Strom, S.C.; Cai, H.; Falany, C.N.; Kocarek, T.A.; Runge-Morris, M.
Regulation of human hepatic hydroxysteroid sulfotransferase gene expression by the peroxisome proliferator-activated receptor alpha transcription factor
Mol. Pharmacol.
67
1257-1267
2005
Homo sapiens
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 (O00204), Homo sapiens
Meinl, W.; Pabel, U.; Osterloh-Quiroz, M.; Hengstler, J.G.; Glatt, H.
Human sulphotransferases are involved in the activation of aristolochic acids and are expressed in renal target tissue
Int. J. Cancer
118
1090-1097
2006
Homo sapiens (O00204)
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, Homo sapiens (O00204)
Ji, Y.; Moon, I.; Zlatkovic, J.; Salavaggione, O.E.; Thomae, B.A.; Eckloff, B.W.; Wieben, E.D.; Schaid, D.J.; Weinshilboum, R.M.
Human hydroxysteroid sulfotransferase SULT2B1 pharmacogenomics: gene sequence variation and functional genomics
J. Pharmacol. Exp. Ther.
322
529-540
2007
Homo sapiens
Falany, C.N.; He, D.; Dumas, N.; Frost, A.R.; Falany, J.L.
Human cytosolic sulfotransferase 2B1: isoform expression, tissue specificity and subcellular localization
J. Steroid Biochem. Mol. Biol.
102
214-221
2006
Homo sapiens (O00204), Homo sapiens, Mus musculus (O35400), Rattus norvegicus (Q29YR5)
Allali-Hassani, A.; Pan, P.W.; Dombrovski, L.; Najmanovich, R.; Tempel, W.; Dong, A.; Loppnau, P.; Martin, F.; Thonton, J.; Edwards, A.M.; Bochkarev, A.; Plotnikov, A.N.; Vedadi, M.; Arrowsmith, C.H.
Structural and chemical profiling of the human cytosolic sulfotransferases
PLoS Biol.
5
1063-1078
2007
Homo sapiens (O00204)
-
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 (Q06520)
Gulcan, H.O.; Liu, Y.; Duffel, M.W.
Pentachlorophenol and other chlorinated phenols are substrates for human hydroxysteroid sulfotransferase hSULT2A1
Chem. Res. Toxicol.
21
1503-1508
2008
Homo sapiens
Harris, R.; Turan, N.; Kirk, C.; Ramsden, D.; Waring, R.
Effects of endocrine disruptors on dehydroepiandrosterone sulfotransferase and enzymes involved in PAPS synthesis: genomic and nongenomic pathways
Environ. Health Perspect.
115 Suppl 1
51-54
2007
Homo sapiens
Fang, H.L.; Strom, S.C.; Ellis, E.; Duanmu, Z.; Fu, J.; Duniec-Dmuchowski, Z.; Falany, C.N.; Falany, J.L.; Kocarek, T.A.; Runge-Morris, M.
Positive and negative regulation of human hepatic hydroxysteroid sulfotransferase (SULT2A1) gene transcription by rifampicin: roles of hepatocyte nuclear factor 4alpha and pregnane X receptor
J. Pharmacol. Exp. Ther.
323
586-598
2007
Homo sapiens
Lu, L.Y.; Hsieh, Y.C.; Liu, M.Y.; Lin, Y.H.; Chen, C.J.; Yang, Y.S.
Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1)
Mol. Pharmacol.
73
660-668
2008
Homo sapiens (Q06520)
Reich, O.; Singer, C.; Hudelist, G.; Regauer, S.
Estrogen sulfotransferase expression in endometrial stromal sarcomas: an immunohistochemical study
Pathol. Res. Pract.
203
85-87
2007
Homo sapiens
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 (O00204), Homo sapiens
Ekuase, E.J.; Lehmler, H.J.; Robertson, L.W.; Duffel, M.W.
Binding interactions of hydroxylated polychlorinated biphenyls (OHPCBs) with human hydroxysteroid sulfotransferase hSULT2A1
Chem. Biol. Interact.
212
56-64
2014
Homo sapiens (Q06520)
Ekuase, E.J.; van t Erve, T.J.; Rahaman, A.; Robertson, L.W.; Duffel, M.W.; Luthe, G.
Mechanistic insights into the specificity of human cytosolic sulfotransferase 2A1 (hSULT2A1) for hydroxylated polychlorinated biphenyls through the use of fluoro-tagged probes
Environ. Sci. Pollut. Res. Int.
23
2119-2127
2016
Homo sapiens (Q06520)
Rizner, T.L.
The important roles of steroid sulfatase and sulfotransferases in gynecological diseases
Front. Pharmacol.
7
30
2016
Homo sapiens (O00204)
Zhang, L.; Kurogi, K.; Liu, M.; Schnapp, A.; Williams, F.; Sakakibara, Y.; Suiko, M.; Liu, M.
Sulfation of benzyl alcohol by the human cytosolic sulfotransferases (SULTs): A systematic analysis
J. Appl. Toxicol.
36
1090-1094
2016
Homo sapiens (O43704), Homo sapiens (P50225), Homo sapiens (P50226)
Bansal, S.; Lau, A.J.
Human liver cytosolic sulfotransferase 2A1-dependent dehydroepiandrosterone sulfation assay by ultra-high performance liquid chromatography-tandem mass spectrometry
J. Pharm. Biomed. Anal.
120
261-269
2016
Homo sapiens (Q06520)
Zhu, J.; Qi, R.; Liu, Y.; Zhao, L.; Han, W.
Mechanistic insights into the effect of ligands on structural stability and selectivity of sulfotransferase 2A1 (SULT2A1)
ACS Omega
4
22021-22034
2019
Homo sapiens (Q06520)
Sun, Y.; Machalz, D.; Wolber, G.; Parr, M.; Bureik, M.
Functional expression of all human sulfotransferases in fission yeast, assay development, and structural models for isoforms SULT4A1 and SULT6B1
Biomolecules
10
1-17
2020
Homo sapiens (Q6IMI4), Homo sapiens
Yip, C.K.Y.; Bansal, S.; Wong, S.Y.; Lau, A.J.
Identification of galeterone and abiraterone as inhibitors of dehydroepiandrosterone sulfonation catalyzed by human hepatic cytosol, SULT2A1, SULT2B1b, and SULT1E1
Drug Metab. Dispos.
46
470-482
2018
Homo sapiens (O00204), Homo sapiens (Q06520)
Parker, V.S.; Squirewell, E.J.; Lehmler, H.J.; Robertson, L.W.; Duffel, M.W.
Hydroxylated and sulfated metabolites of commonly occurring airborne polychlorinated biphenyls inhibit human steroid sulfotransferases SULT1E1 and SULT2A1
Environ. Toxicol. Pharmacol.
58
196-201
2018
Homo sapiens (Q06520), Homo sapiens
Rizner, T.L.
The important roles of steroid sulfatase and sulfotransferases in gynecological diseases
Front. Pharmacol.
7
30
2016
Homo sapiens (O00204), Homo sapiens (Q06520)
Feng, L.; Yuen, Y.L.; Xu, J.; Liu, X.; Chan, M.Y.; Wang, K.; Fong, W.P.; Cheung, W.T.; Lee, S.S.
Identification and characterization of a novel PPARalpha-regulated and 7alpha-hydroxyl bile acid-preferring cytosolic sulfotransferase mL-STL (Sult2a8)
J. Lipid Res.
58
1114-1131
2017
Homo sapiens (O00204)
Bansal, S.; Lau, A.J.
Inhibition of human sulfotransferase 2A1-catalyzed sulfonation of lithocholic acid, glycolithocholic acid, and taurolithocholic acid by selective estrogen receptor modulators and various analogs and metabolites
J. Pharmacol. Exp. Ther.
369
389-405
2019
Homo sapiens (Q06520)
Vickman, R.E.; Yang, J.; Lanman, N.A.; Cresswell, G.M.; Zheng, F.; Zhang, C.; Doerge, R.W.; Crist, S.A.; Mesecar, A.D.; Hu, C.D.; Ratliff, T.L.
Cholesterol sulfotransferase SULT2B1b modulates sensitivity to death receptor ligand TNFalpha in castration-resistant prostate cancer
Mol. Cancer Res.
17
1253-1263
2019
Homo sapiens (O00204)
Bi, Y.; Shi, X.; Zhu, J.; Guan, X.; Garbacz, W.G.; Huang, Y.; Gao, L.; Yan, J.; Xu, M.; Ren, S.; Ren, S.; Liu, Y.; Ma, X.; Li, S.; Xie, W.
Regulation of cholesterol sulfotransferase SULT2B1b by hepatocyte nuclear factor 4alpha constitutes a negative feedback control of hepatic gluconeogenesis
Mol. Cell. Biol.
38
e00654-17
2018
Homo sapiens (O00204), Mus musculus (O35400)
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