Information on EC 2.8.2.2 - alcohol sulfotransferase and Organism(s) Homo sapiens

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Homo sapiens


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
2.8.2.2
-
RECOMMENDED NAME
GeneOntology No.
alcohol sulfotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate
show the reaction diagram
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 hide
LITERATURE
sulfate group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Steroid hormone biosynthesis
-
-
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 hide
9032-76-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knock-down of SULT2B1b inhibits cell growth and cyclinB1 levels in human hepatocarcinoma cells and suppressed xenograft growth in vivo
physiological function
-
SULT2B1b expression promotes proliferation of hepatocellular carcinoma cells in vitro and in vivo, which may contribute to the progression of hepatocellular carcinoma
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
show the reaction diagram
-
SULT1B1
-
-
?
3'-phosphoadenylyl sulfate + 17alpha-hydroxypregnenolone
adenosine 3',5'-bisphosphate + 17alpha-hydroxypregnenolone sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 5alpha,6alpha-epoxycholesterol
adenosine 3',5'-bisphosphate + 5alpha,6alpha-epoxycholesteryl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 5beta,6beta-epoxycholesterol
adenosine 3',5'-bisphosphate + 5beta,6beta-epoxycholesteryl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 7-oxo-cholesterol
adenosine 3',5'-bisphosphate + 7-oxo-cholesteryl 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 7-oxocholesterol
adenosine 3',5'-bisphosphate + 7-oxocholesterol 3-sulfate
show the reaction diagram
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + 7alpha-hydroxycholesterol
adenosine 3',5'-bisphosphate + 7alpha-hydroxycholesterol 3-sulfate
show the reaction diagram
SULT2B1b, the 7alpha derivative is highly preferred
-
-
?
3'-phosphoadenylyl sulfate + 7alpha-hydroxycholesterol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 7beta-hydroxycholesterol
adenosine 3',5'-bisphosphate + 7beta-hydroxycholesterol 3-sulfate
show the reaction diagram
SULT2B1b, the 7alpha derivative is highly preferred
-
-
?
3'-phosphoadenylyl sulfate + 7beta-hydroxycholesterol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + androsterone
adenosine 3',5'-bisphosphate + androsterone 3-sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesterol 3-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + cholesterol
adenosine 3',5'-bisphosphate + cholesteryl 3-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + cholesterol 7alpha-hydroperoxide
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
SULT2B1b
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + genistein
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone 3-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + raloxifene
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + tibolone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 1'-hydroxysafrole
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoenzyme DHEA-ST, sulfation and bioactivation to a lesser extent
-
-
?
3'-phosphoadenylylsulfate + 1-hydroxymethylpyrene
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoenzyme DHEA-ST, sulfation and bioactivation
-
-
?
3'-phosphoadenylylsulfate + 17alpha-ethinylestradiol
adenosine 3',5'-bisphosphate + 17alpha-ethinylestradiol sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylylsulfate + 2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 2-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-hydroxy-catecholestrogen
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
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'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 3,3'-diiodothyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + 3,5-diiodothyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + 3-O-phenyl-17beta-estradiol
adenosine 3',5'-bisphosphate + 3-phenolic hydroxyl beta-estradiol sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylylsulfate + 4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 4,4'-isopropylidenediphenol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + 4-(1,1,3,3-tetramethylbutyl)phenol
adenosine 3',5'-bisphosphate + 4-(1,1,3,3-tetramethylbutyl)phenyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3,5-dichlorobiphenyl
adenosine 3',5'-bisphosphate + 4-hydroxy-3,5-dichlorobiphenyl sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-n-nonylphenol
adenosine 3',5'-bisphosphate + 4-n-nonylphenyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoform SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 6-hydroxymethylbenzo[a]pyrene
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoenzyme DHEA-ST, sulfation and bioactivation
-
-
?
3'-phosphoadenylylsulfate + alpha-hydroxytamoxifen
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylylsulfate + androsterone
adenosine 3',5'-bisphosphate + 5alpha-androstan-17-one 3-sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylylsulfate + benzyl alcohol
adenosine 3',5'-bisphosphate + benzyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylylsulfate + budesonide-22R
adenosine 3',5'-bisphosphate + budesonide-22R,11 sulfate + budesonide-22R,21 sulfate
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
3'-phosphoadenylylsulfate + cortisol
adenosine 3',5'-bisphosphate + cortisol sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + diiodothyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoform SULT1A3
-
-
?
3'-phosphoadenylylsulfate + estrone
adenosine 3',5'-bisphosphate + estrone sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylylsulfate + ethanol
adenosine 3',5'-bisphosphate + ethyl sulfate
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + hycanthone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoenzyme DHEA-ST, sulfation and bioactivation
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
antihypertensive agent and hair growth stimulator, activation by sulfation
-
-
?
3'-phosphoadenylylsulfate + N-hydroxy-2-acetylaminofluorene
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
isoenzyme DHEA-ST, sulfation and bioactivation to a lesser extent
-
-
?
3'-phosphoadenylylsulfate + R-(+)-1-naphthyl-1-ethanol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
S-(-)-enantiomer is not a substrate for the enzyme
-
-
?
3'-phosphoadenylylsulfate + R-(+)-2-naphthyl-1-ethanol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
both enantiomers are substrates for the enzyme
-
-
?
3'-phosphoadenylylsulfate + S-(-)-2-naphthyl-1-ethanol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
both enantiomers are substrates for the enzyme
-
-
?
3'-phosphoadenylylsulfate + testosterone
adenosine 3',5'-bisphosphate + testosterone 3-sulfate
show the reaction diagram
-
17-hydroxyl of testosterone
-
-
r
3'-phosphoadenylylsulfate + tetraiodothyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
3'-phosphoadenylylsulfate + triiodothyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
sulfation inactivates the substrate by addition of a sulfuryl moiety to the 4'-hydroxyl group
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + 17alpha-hydroxypregnenolone
adenosine 3',5'-bisphosphate + 17alpha-hydroxypregnenolone sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 7-oxocholesterol
adenosine 3',5'-bisphosphate + 7-oxocholesterol 3-sulfate
show the reaction diagram
O00204
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + androsterone
adenosine 3',5'-bisphosphate + androsterone 3-sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
O00204
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
show the reaction diagram
O00204
SULT2B1b, SULT2B1a, and SULT2A1
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + pregnenolone
adenosine 3',5'-bisphosphate + pregnenolone sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
-
2,6-Dichloro-4-nitrophenol
-
-
2-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
-
3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
-
3'-phosphoadenylyl sulfate
-
substrate inhibition of SULT2A1, structure analysis of SULT2A1/DHEA and SULT2A1/PAP or SULT2A1/ADT, overview
3,3',4'-dihydroxy-4-monochlorobiphenyl
-
-
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
4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
-
4'-hydroxy-2',3,4-trichlorobiphenyl
-
-
4'-hydroxy-2,3',4,5'-tetrachlorobiphenyl
-
-
4'-hydroxy-2,3',4-trichlorobiphenyl
-
-
4'-hydroxy-2,3'-dichlorobiphenyl
-
-
4'-hydroxy-2,5-dichlorobiphenyl
-
-
4'-hydroxy-3,4-dichlorobiphenyl
-
-
4'-hydroxy-4-monochlorobiphenyl
-
-
4-hydroxy-2',3,5-trichlorobiphenyl
-
-
4-hydroxy-2,4'-dichlorobiphenyl
-
-
4-hydroxy-3,3',5-trichlorobiphenyl
-
-
4-hydroxy-3,3'-dichlorobiphenyl
-
-
4-hydroxy-3,5-dichlorobiphenyl
-
-
4-n-octylphenol
-
-
4-tert-octylphenol
-
-
5,3',4'-dihydroxy-2,3-dichlorobiphenyl
-
-
6'-hydroxy-3,3'4-trichlorobiphenyl
-
-
-
adenosine 5'-(beta,gamma-imido) triphosphate
-
i.e. AMP-PNP, a non-hydrolysable ATP analogue
androsterone
-
-
bis(2-ethylhexyl)phthalate
-
-
dehydroepiandrosterone
-
substrate inhibition of SULT2A1, structure analysis of SULT2A1/DHEA and SULT2A1/PAP or SULT2A1/ADT, overview
diisodecyl phthalate
-
-
pyridoxal 5'-phosphate
-
a competitive inhibitor for sulfotransferases
S-(-)-1-naphthyl-1-ethanol
-
inhibitor of the sulfation of dehydroepiandrosterone
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
-
leads to a greater activation of the cDNA-expressed DHEA ST when assayed with dehydroepiandrosterone
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0256
2-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0063
3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.00013
3'-phosphoadenylylsulfate
-
pH 7.5, 37C
0.00295 - 0.00973
3,3'-diiodothyronine
0.00484
3,5-diiodothyronine
-
pH 6.0, 37C, isoform SULT2A1
0.0121
4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0043
4,4'-isopropylidenediphenol
pH 7.4, 37C
0.0051
4-(1,1,3,3-tetramethylbutyl)phenol
pH 7.4, 37C
0.0085
4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0715
4-n-nonylphenol
pH 7.4, 37C
0.0002 - 0.0096
androsterone
0.0685
benzyl alcohol
isoform SULT1A1, at pH 7.0 and 37C
0.0209
budesonide-22R
-
pH 7.4, 37C
0.0111
budesonide-22S
-
pH 7.4, 37C
0.1673
daidzein
pH 7.4, 37C
0.0006 - 0.0065
dehydroepiandrosterone
0.0465
E-(+)-alpha-hydroxytamoxifen
-
pH 8.0, 37C
0.0358
E-(-)-alpha-hydroxytamoxifen
-
pH 8.0, 37C
0.041
genistein
pH 7.4, 37C
3.9
minoxidil
-
pH 7.5, 37C
0.24
R-(+)-1-naphthyl-1-ethanol
-
pH 7.0, 37C
0.25
R-(+)-2-naphthyl-1-ethanol
-
pH 7.0, 37C
-
0.54
S-(-)-2-naphthyl-1-ethanol
-
pH 7.0, 37C
0.00136
tetraiodothyronine
-
pH 6.0, 37C, isoform SULT1E1
0.00463 - 0.0143
triiodothyronine
0.0669
Z-(+)-alpha-hydroxytamoxifen
-
pH 8.0, 37C
-
0.0405
Z-(-)-alpha-hydroxytamoxifen
-
pH 8.0, 37C
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
benzyl alcohol
isoform SULT1A1, at pH 7.0 and 37C; isoform SULT1A1, at pH 7.0 and 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.2
2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
1.3
2-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
12.4
3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
4.5
4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
5.9
4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.019
benzyl alcohol
isoform SULT1A1, at pH 7.0 and 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.259
2'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.323
2-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0775
3'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.032
3,3',4'-dihydroxy-4-monochlorobiphenyl
-
at pH 7.0 and 37C
0.219
4'-fluoro-4-hydroxy-3,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.003
4'-hydroxy-2',3,4-trichlorobiphenyl
-
at pH 7.0 and 37C
0.0006
4'-hydroxy-2,3',4,5'-tetrachlorobiphenyl
-
at pH 7.0 and 37C
0.003
4'-hydroxy-2,3',4-trichlorobiphenyl
-
at pH 7.0 and 37C
0.0054
4'-hydroxy-2,3'-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0007
4'-hydroxy-2,5-dichlorobiphenyl
-
at pH 7.0 and 37C
0.004
4'-hydroxy-3,4-dichlorobiphenyl
-
at pH 7.0 and 37C
0.017
4'-hydroxy-4-monochlorobiphenyl
-
at pH 7.0 and 37C
0.0008
4-hydroxy-2',3,5-trichlorobiphenyl
-
at pH 7.0 and 37C
0.005
4-hydroxy-2,4'-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0034
4-hydroxy-3,3',5-trichlorobiphenyl
-
at pH 7.0 and 37C
0.012
4-hydroxy-3,3'-dichlorobiphenyl
-
at pH 7.0 and 37C
0.0135 - 0.221
4-hydroxy-3,5-dichlorobiphenyl
0.0028
4-tert-octylphenol
-
-
0.014
5,3',4'-dihydroxy-2,3-dichlorobiphenyl
-
at pH 7.0 and 37C
0.009
6'-hydroxy-3,3'4-trichlorobiphenyl
-
at pH 7.0 and 37C
-
0.0007 - 0.159
androsterone
0.0061 - 0.466
dehydroepiandrosterone
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00008
isoform SULT1B1, at pH 7.0 and 37C
0.00188
isoform SULT1A2, at pH 7.0 and 37C
0.0019
-
recombinant SULT2B1b, substrate 7beta-hydroxycholesterol
0.0048
-
recombinant SULT2B1b, substrate cholesterol 7alpha-hydroperoxide
0.0071
-
recombinant SULT2B1b, substrate 7-oxocholesterol
0.0075
-
recombinant SULT2B1b, substrate cholesterol
0.01052
isoform SULT1A1, at pH 7.0 and 37C
0.021
-
recombinant SULT2B1b, substrate 7alpha-hydroxycholesterol
0.15
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.5
-
assay at
5.5
-
assay at
7 - 8
-
-
7 - 9
-
recombinant enzyme, expressed in Escherichia coli
7
-
assay at
7.1 - 7.5
-
assay at
7.4
-
isoform SULT2A1
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
25
-
assay at
40 - 45
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
enzyme activity at 25C and 30C drops to 35% and 56%, repective to the maximum activity at 45C, residual activity is determined to be 62% of the maximum at 50C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
endometrial stromal, from 29 patients, reduced or no expression of EST
Manually annotated by BRENDA team
-
medulloblastoma-derived cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33770
-
calculated from putative amino acid sequence, estimated from cDNA
35000
-
2 * 35000, SDS-PAGE
35930
calculated from putative amino acid sequence, estimated from cDNA
67200
-
gel filtration
68000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
DHEA-ST
-
human cholesterol sulfotransferase SULT2B1b
-
purified recombinant mutants M137I and M137W, hanging drop vapor diffusion method at 18C, 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
-
purified SULT1B1 is crystallized in the presence of 2 mM PAP using the hanging drop method at 20C 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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
45
-
90% basal activity remains after 15 min
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
partially, 5 ST activities in liver preparation
-
recombinant GST-tagged SULT2B1 by glutathione affinity chromatography
-
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
; cloned and expressed in Escherichia coli
-
; SULT2A1 bacterially expressed as His tagged protein in Escherichia coli
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 and SULT2A1 cloned and expressed in COS-1 cells
-
DHEA ST cloned from cDNA and expressed in COS-1 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
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in the mouse hepatocarcinoma cell line Hepa1-6
-
expression of GFP-tagged wild-type allozymes and mutant truncated SULT2B1a and SULT2B1b variants lacking the SULT2B1 proline-rich tail in COS-1 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
-
expression of GST-tagged SULT2B1; expression of SULT2B1b eliminates the cytotoxic effect of 7-oxo-cholesterol on 293T cells, which are normally devoid of SULT2B1b
-
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 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
SULT2A1 real time RT-PCR expression analysis in presence of different plasticizers
-
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
-
SULT2A1, expression in Escherichia coli
-
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 enzyme expression is upregulated in endometrial cancer
-
the expression of SULT2B1 at the mRNA level is decreased in ovarian endometriosis compared to normal endometrium
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D176N
-
naturally occuring polymorphism in SULT2B1a
L36S
-
naturally occuring polymorphism in SULT2B1a
M137I
-
site-directed mutagenesis, substrate binding structure, the Ki for androsterone is increased 28.6fold compared to the wild-type enzyme, overview
M137K
-
site-directed mutagenesis, inactive mutant
M137K/Y238A
-
site-directed mutagenesis, inactive mutant
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
P330L
-
naturally occuring polymorphism in SULT2B1a
R215H
-
naturally occuring polymorphism in SULT2B1a
V260A
-
site-directed mutagenesis, a monomeric mutant
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
EST expression is a prognostic factor in breast cancer
medicine