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2 3'-phosphoadenylyl sulfate + 2 dopamine
2 adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + dopamine 4-O-sulfate
SULT1A3
NMR product structure analysis, dopamine 3-O-sulfate is the main product, overview
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 2-aminophenol
adenosine 3',5'-bisphosphate + 2-aminophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3-nitro-L-tyrosine
adenosine 3',5'-bisphosphate + 3-nitro-O-sulfo-L-tyrosine
specific reaction of SULT1A3, not performed by other SULT isozymes
-
-
?
3'-phosphoadenylyl sulfate + 3-nitro-L-tyrosine
adenosine 3',5'-bisphosphate + 3-nitro-O4-sulfo-L-tyrosine
sulfation serves as a pathway for the metabolism/regulation of nitrotyrosine, nitrotyrosine O-sulfate is released into the medium of Hep-G2 hepatoma cells
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + 6-hydroxydopamine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 7-hydroxyserotonin
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylyl sulfate + acetaminophen
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + catechol
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dextrorphan
adenosine 3',5'-bisphosphate + dextrorphan sulfate
i.e. active metabolite of the antitussive dextromethorphan
-
-
?
3'-phosphoadenylyl sulfate + DL-3-hydroxyphenylalanine
adenosine 3',5'-bisphosphate + DL-3-(sulfooxy)phenylalanine
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
3'-phosphoadenylyl sulfate + fenoterol
adenosine 3',5'-bisphosphate + ?
as fenoterol hydrobromide
-
-
?
3'-phosphoadenylyl sulfate + genistein
adenosine 3',5'-bisphosphate + genistein 4'-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + isoproterenol
adenosine 3',5'-bisphosphate + ?
as isoproterenol hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + L-DOPA
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + L-tyrosine
adenosine 3',5'-bisphosphate + O-sulfo-L-tyrosine
low activity
-
-
?
3'-phosphoadenylyl sulfate + morphine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
3'-phosphoadenylyl sulfate + O-desmethyl tramadol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + ritodrine
adenosine 3',5'-bisphosphate + ?
as ritodrine hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + rotigotine
adenosine 3',5'-bisphosphate + rotigotine 1-O-sulfate
i.e. (6S)-6-[propyl[2-(thiophen-2-yl)ethyl]amino]-5,6,7,8-tetrahydronaphthalen-1-ol, non-ergoline dopamine agonist
-
-
?
3'-phosphoadenylyl sulfate + salbutamol
adenosine 3',5'-bisphosphate + ?
as salbutamol hemisulfate
-
-
?
3'-phosphoadenylyl sulfate + serotonin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + tapentadol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + terbutaline
adenosine 3',5'-bisphosphate + ?
as terbutaline hemisulfate
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 4-chlorocatechol
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 4-chlorophenol
adenosine 3',5'-bisphosphate + 4-chlorophenyl sulfate
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 4-isopropylcatechol
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 4-methylcatechol
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 4-methylphenol
adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + benzyl alcohol
adenosine 3',5'-bisphosphate + benzyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + catechol
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + tyramine O-sulfate
SULT1A3
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-hydroxypyrene
adenosine 3',5'-bisphosphate + 1-hydroxypyrene sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
3'-phosphoadenylyl sulfate + 17alpha-ethinylestradiol
?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 2,3,3',5,5',6-hexachlorobiphenyl-4'-yl
adenosine 3',5'-bisphosphate + 2,2',3,3',5,5'-hexachlorobiphenyl-4'-yl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2,3,5,5',6-pentachlorobiphenyl-4'-yl
adenosine 3',5'-bisphosphate + 2,2',3,3',5'-pentachlorobiphenyl-4'-yl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2,6-dichloro-4-nitrophenol
adenosine 3',5'-bisphosphate + 2,6-dichloro-4-nitrophenyl sulfate
low activity, inhibitory
-
-
?
3'-phosphoadenylyl sulfate + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-amino-3-methyl-9H-pyrido[2,3-b]indole
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-amino-9H-pyrido[2,3-b]indole
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-aminophenol
adenosine 3',5'-bisphosphate + 2-aminophenyl sulfate
3'-phosphoadenylyl sulfate + 2-methoxyestradiol
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
3'-phosphoadenylyl sulfate + 3',4',5-trichlorobiphenyl-2-yl
adenosine 3',5'-bisphosphate + 3',4',5-trichlorobiphenyl-2-yl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3-amino-1-methyl-5H-pyrido[4,3-b]indole
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3-cyano-7-hydroxycoumarin
?
-
-
-
?
3'-phosphoadenylyl sulfate + 3-nitrobenzanthrone
adenosine 3',5'-bisphosphate + N-sulfoxy-3-aminobenzanthrone
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
3'-phosphoadenylyl sulfate + 4-chlorobiphenyl-3'-ol
adenosine 3',5'-bisphosphate + 4'-chlorobiphenyl-3-yl sulfate
low activity
-
-
?
3'-phosphoadenylyl sulfate + 4-chlorobiphenyl-4'-ol
adenosine 3',5'-bisphosphate + 4'-chlorobiphenyl-4-yl sulfate
low activity
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + 4-(sulfooxy)tamoxifen
3'-phosphoadenylyl sulfate + 4-methylumbelliferone
adenosine 3',5'-bisphosphate + 4-methylumbelliferyl sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + 5-amino-2-(4-amino-3-fluorophenyl)-6,8-difluoro-7-methyl-4H-1-benzopyran-4-one
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + 5-chloro-7-iodo-8-quinolinol
adenosine 3',5'-bisphosphate + 5-chloro-7-iodo-8-quinolinyl sulfate
-
isoform SULT1A3 is responsible for the 5-chloro-7-iodo-8-quinolinol sulfation in human jejunum
-
-
?
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-methylimidazo[1,2-a:5,4-b']dipyridin-2-amine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 9-(4'-aminophenyl)-9H-pyrido[3,4-b]indole
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylyl sulfate + acetaminophen
adenosine 3',5'-bisphosphate + 4-(acetylamino)phenylsulfate
-
-
-
?
3'-phosphoadenylyl sulfate + apigenin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + butylparaben
adenosine 3',5'-bisphosphate + butylparaben sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + catechol
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + chrysin
adenosine 3',5'-bisphosphate + ?
substrate of allozyme SULT1A1*1
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
as dopamine hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopaminyl sulfate
3'-phosphoadenylyl sulfate + doxorubicin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + epicatechin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + epigallocatechin gallate
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + epirubicin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol sulfate
-
the enzyme also performs the reaction of EC 2.8.2.4, estrone sulfotransferase, with low activity
-
-
?
3'-phosphoadenylyl sulfate + fenoterol
adenosine 3',5'-bisphosphate + ?
as fenoterol hydrobromide
-
-
?
3'-phosphoadenylyl sulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + imidazo[1,2-a:5,4-b']dipyridin-2-amine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + isoproterenol
adenosine 3',5'-bisphosphate + isoproterenol sulfate
as isoproterenol hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + minoxidil
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl-4-amine
SULT1C*2
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxyaristolactam I
adenosine 3',5'-bisphosphate + N-hydroxyaristolactam I sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + pentachlorophenol
adenosine 3',5'-bisphosphate + pentachlorophenyl sulfate
low activity, inhibitory
-
-
?
3'-phosphoadenylyl sulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + quercetin
adenosine 3',5'-bisphosphate + ?
allozyme SULT1A1*1
-
-
?
3'-phosphoadenylyl sulfate + resveratrol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + resveratrol
adenosine 3',5'-bisphosphate + trans-resveratrol-3-O sulfate
3,4',5-trihydroxy-trans-stilbene
-
-
?
3'-phosphoadenylyl sulfate + ritodrine
adenosine 3',5'-bisphosphate + ?
as ritodrine hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + rotigotine
adenosine 3',5'-bisphosphate + rotigotine 1-O-sulfate
i.e. (6S)-6-[propyl[2-(thiophen-2-yl)ethyl]amino]-5,6,7,8-tetrahydronaphthalen-1-ol, non-ergoline dopamine agonist
-
-
?
3'-phosphoadenylyl sulfate + salbutamol
adenosine 3',5'-bisphosphate + ?
as salbutamol hemisulfate
-
-
?
3'-phosphoadenylyl sulfate + terbutaline
adenosine 3',5'-bisphosphate + ?
as terbutaline hemisulfate
-
-
?
3'-phosphoadenylyl sulfate + trans-4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + trans-4-(sulfooxy)tamoxifen
substrate of the allozymes SULT1A1*2 and SULT1A1*1
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + (+/-)isoproterenol
adenosine 3',5'-bisphosphate + ?
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + (+/-)metoprolol
adenosine 3',5'-bisphosphate + ?
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + (+/-)salbutamol
adenosine 3',5'-bisphosphate + ?
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + (+/-)sotalol
adenosine 3',5'-bisphosphate + ?
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
3'-phosphoadenylylsulfate + 2-amino-4'-hydroxy-1-methyl-6-phenylimidazo[4,5-b]pyridine
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 2-ethylphenol
adenosine 3',5'-bisphosphate + 2-ethylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 2-methylphenol
adenosine 3',5'-bisphosphate + 2-methylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthylsulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 3,3',5'-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 3,3',5-triiodo-D-thyronine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 3,3',5-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 3,3'-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 3,4-dihydroxyphenylacetate
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 3,5-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 3-ethylphenol
adenosine 3',5'-bisphosphate + 3-ethylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 3-hydroxybenzo[a]pyrene
adenosine 3',5'-bisphosphate + benzo[a]pyrene 3-sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 3-methylphenol
adenosine 3',5'-bisphosphate + 3-methylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-chlorocatechol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-chlorophenol
adenosine 3',5'-bisphosphate + 4-chlorophenyl sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-ethylphenol
adenosine 3',5'-bisphosphate + 4-ethylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3-methoxyphenylglycol
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 4-isopropylcatechol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-methoxytyramine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-methylcatechol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-methylphenol
adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate
3'-phosphoadenylylsulfate + 4-methylumbelliferone
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + 4-n-amylphenol
adenosine 3',5'-bisphosphate + 4-n-amylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-n-butylphenol
adenosine 3',5'-bisphosphate + 4-n-butylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-n-propylphenol
adenosine 3',5'-bisphosphate + 4-n-propylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylylsulfate + 4-nonylphenol
adenosine 3',5'-bisphosphate + 4-nonylphenyl sulfate
3'-phosphoadenylylsulfate + 4-octylphenol
adenosine 3',5'-bisphosphate + 4-octylphenyl sulfate
3'-phosphoadenylylsulfate + 5,7-dihydroxyflavanone
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 5-(hydroxyphenyl)-5-(p-tolyl)-hydantoin
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 5-hydroxyindole
adenosine 3',5'-bisphosphate + 5-indoxyl sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 5-hydroxytryptophol
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 6-hydroxymelatonin
adenosine 3',5'-bisphosphate + melatonin 6-sulfate
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylylsulfate + acebutolol
adenosine 3',5'-bisphosphate + ?
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + acetaminophen
adenosine 3',5'-bisphosphate + ?
-
M-PST and P-PST
-
-
?
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + bisphenol A
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + bupivacaine
adenosine 3',5'-bisphosphate + ?
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + catechol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + D-tyrosine
adenosine 3',5'-bisphosphate + D-tyrosyl sulfate
M-PST
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 4'-sulfate
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 7-sulfate + daidzein 4'-sulfate
3'-phosphoadenylylsulfate + daidzein 4'-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
3'-phosphoadenylylsulfate + daidzein 7-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + dexamethasone
adenosine 3',5'-bisphosphate + ?
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + DL-propanolol
adenosine 3',5'-bisphosphate + ?
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + DL-tyrosine
adenosine 3',5'-bisphosphate + DL-tyrosyl sulfate
3'-phosphoadenylylsulfate + dobutamine
adenosine 3',5'-bisphosphate + ?
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + ?
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 4'-sulfate
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate + genistein 4'-sulfate
3'-phosphoadenylylsulfate + genistein 4'-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
3'-phosphoadenylylsulfate + genistein 7-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
3'-phosphoadenylylsulfate + harmol
adenosine 3',5'-bisphosphate + harmol sulfate
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + L-thyroxine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + L-tyrosine
adenosine 3',5'-bisphosphate + L-tyrosyl O4-sulfate
M-PST
-
-
?
3'-phosphoadenylylsulfate + lidocaine
adenosine 3',5'-bisphosphate + ?
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
3'-phosphoadenylylsulfate + naringenin
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + norepinephrine
adenosine 3',5'-bisphosphate + ?
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + norepinephrine
adenosine 3',5'-bisphosphate + norepinephrine sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + normetanephrine
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
3'-phosphoadenylylsulfate + phentolamine
adenosine 3',5'-bisphosphate + phentolamine sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + ritodrine
adenosine 3',5'-bisphosphate + ritodrine sulfate
3'-phosphoadenylylsulfate + sakuranetin
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + salicylamide
adenosine 3',5'-bisphosphate + 2-sulfooxybenzamide
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + serotonin
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylylsulfate + troglitazone
adenosine 3',5'-bisphosphate + troglitazone sulfate
-
ST1A3, not ST1A5
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + tyramine O-sulfate
3'-phosphoadenylylsulfate + tyrosylglycine
?
-
-
-
-
?
3'-phosphoadenylylsulfate + umbelliferone
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
adenosine 3',5'-bisphosphate + 4-methylumbelliferyl sulfate
3'-phosphoadenylyl sulfate + 4-methylumbelliferone
-
-
-
-
r
adenosine 3',5'-bisphosphate + dopamine sulfate
3'-phosphoadenylyl sulfate + dopamine
-
-
-
-
r
additional information
?
-
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 6-hydroxydopamine
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 6-hydroxydopamine
adenosine 3',5'-bisphosphate + ?
specific substrate of SULT1A3, no activity with other SULT isozymes
-
-
?
3'-phosphoadenylyl sulfate + 7-hydroxyserotonin
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 7-hydroxyserotonin
adenosine 3',5'-bisphosphate + ?
specific substrate of SULT1A3, no activity with other SULT isozymes
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
as dopamine hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
SULT1B1
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
SULT1C*2
-
-
?
3'-phosphoadenylyl sulfate + 2-aminophenol
adenosine 3',5'-bisphosphate + 2-aminophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2-aminophenol
adenosine 3',5'-bisphosphate + 2-aminophenyl sulfate
preferred substrate of SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + 2-methoxyestradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methoxyestradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
SULT1B2
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
SULT1C*2
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + 4-(sulfooxy)tamoxifen
-
-
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + 4-(sulfooxy)tamoxifen
-
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + 4-(sulfooxy)tamoxifen
a potent inducer of apoptosis in breast tumor cell lines
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 5-amino-2-(4-amino-3-fluorophenyl)-6,8-difluoro-7-methyl-4H-1-benzopyran-4-one
adenosine 3',5'-bisphosphate + ?
i.e. aminoflavone, diaminoflavone analogues with potent growth-inhibitory activity against human breast and renal cancer cells in vitro and antitumor activity in mice bearing human tumor xenografts, aminoflavone binds to DNA in tumor cells and induces DNA-protein cross-links
-
-
?
3'-phosphoadenylyl sulfate + 5-amino-2-(4-amino-3-fluorophenyl)-6,8-difluoro-7-methyl-4H-1-benzopyran-4-one
adenosine 3',5'-bisphosphate + ?
i.e. aminoflavone
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
r
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
r
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
SULT1A1/2: preference for straight chain phenol substrates with C1-2 and C4-5 chain lengths, overview
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
SULT1A3 is not active with short chain alkylphenols
-
?
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, good substrate of SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
SULT1C*2
-
-
?
3'-phosphoadenylyl sulfate + catechol
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + catechol
adenosine 3',5'-bisphosphate + ?
SULT1A2
-
-
?
3'-phosphoadenylyl sulfate + catechol
adenosine 3',5'-bisphosphate + ?
SULT1C*2
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopaminyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopaminyl sulfate
-
specific substrate for isoform SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
SULT1A1
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
SULT1A2
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
ST1B2
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 3,3',5'-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 3,3',5'-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
ST1B2
-
-
?
3'-phosphoadenylylsulfate + 3,3',5'-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
SULT1A1 allozymes 1 and 2
-
-
?
3'-phosphoadenylylsulfate + 3,3',5-triiodo-D-thyronine
adenosine 3',5'-bisphosphate + ?
ST1B2
-
-
?
3'-phosphoadenylylsulfate + 3,3',5-triiodo-D-thyronine
adenosine 3',5'-bisphosphate + ?
SULT1A1 allozymes 1 and 2
-
-
?
3'-phosphoadenylylsulfate + 3,3',5-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 3,3',5-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
SULT1A1 allozymes 1 and 2
-
-
?
3'-phosphoadenylylsulfate + 3,3'-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + 3,3'-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
low activity
-
-
?
3'-phosphoadenylylsulfate + 3,3'-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
ST1B2
-
-
?
3'-phosphoadenylylsulfate + 3,3'-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
SULT1A1 allozymes 1 and 2
-
-
?
3'-phosphoadenylylsulfate + 3,5-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
no activity with
-
-
?
3'-phosphoadenylylsulfate + 3,5-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
no activity: ST1B2
-
-
?
3'-phosphoadenylylsulfate + 4-methylphenol
adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-methylphenol
adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-methylumbelliferone
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 4-methylumbelliferone
adenosine 3',5'-bisphosphate + ?
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
SULT1B1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
M-PST
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
P-PST
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
P-PST
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
ST1B2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
SULT1C1: specific for
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
SULT1C1: specific for
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
SULT1A2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
SULT1A3: no activity
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
preferred substrate of TS enzyme form
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
SULT1C2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
SULT1C2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
H-PST, preferred substrate
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + 4-nonylphenol
adenosine 3',5'-bisphosphate + 4-nonylphenyl sulfate
-
P-PST, M-PST, SULT1C2, not SULT1C1
-
-
?
3'-phosphoadenylylsulfate + 4-nonylphenol
adenosine 3',5'-bisphosphate + 4-nonylphenyl sulfate
-
P-PST: best substrate
-
-
?
3'-phosphoadenylylsulfate + 4-octylphenol
adenosine 3',5'-bisphosphate + 4-octylphenyl sulfate
-
SULT1C2: best substrate
-
-
?
3'-phosphoadenylylsulfate + 4-octylphenol
adenosine 3',5'-bisphosphate + 4-octylphenyl sulfate
-
P-PST, M-PST, SULT1C2, not SULT1C1
-
-
?
3'-phosphoadenylylsulfate + 6-hydroxymelatonin
adenosine 3',5'-bisphosphate + melatonin 6-sulfate
-
-
-
?
3'-phosphoadenylylsulfate + 6-hydroxymelatonin
adenosine 3',5'-bisphosphate + melatonin 6-sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
phase II drug metabolizing or detoxifying enzyme
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
sulfate conjugation of phenolic biogenic amines, important in the biotransformation of many neurotransmitters, hormones, drugs, and xenobiotic compounds
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
sulfation of environmental estrogens, overview
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
SULTs, especially SULT1A1, are important in xenobiotic and drug metabolism because of their broad substrate specificity and extensive tissue distribution
-
-
?
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + ?
no activity: ST1B2
-
-
?
3'-phosphoadenylylsulfate + bisphenol A
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + bisphenol A
adenosine 3',5'-bisphosphate + ?
-
P-PST, M-PST, SULT1C2, not SULT1C1
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
M-PST
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
-
i.e. D-Dopa
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
i.e. D-Dopa
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
i.e. D-Dopa
-
-
?
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
-
preferred isomer, stereospecific
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 7-sulfate + daidzein 4'-sulfate
-
enzyme form SULT1A1, ratio of 7-sulfate formation to 4'-sulfate formation is 4.4
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 7-sulfate + daidzein 4'-sulfate
-
enzyme form SULT1E1, ratio of 7-sulfate formation to 4'-sulfate formation is 1.1
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 7-sulfate + daidzein 4'-sulfate
-
enzyme form SULT2A1, ratio of 7-sulfate formation to 4'-sulfate formation is 11.8
-
-
?
3'-phosphoadenylylsulfate + daidzein 4'-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + daidzein 4'-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
-
enzyme form SULT1E1
-
-
?
3'-phosphoadenylylsulfate + daidzein 7-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + daidzein 7-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
-
enzyme form SULT1E1
-
-
?
3'-phosphoadenylylsulfate + DL-tyrosine
adenosine 3',5'-bisphosphate + DL-tyrosyl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + DL-tyrosine
adenosine 3',5'-bisphosphate + DL-tyrosyl sulfate
M-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
SULT1A3 is specific for dopamine and other biogenic amines
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
M-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
preferred substrate of TL enzyme form
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
H-PST, no activity with
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
M-PST: best substrate
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
P-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
P-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
SULT1A1 and SULT1A2: no activity
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
accounts for approximately 10% of the enzymic activity directed towards catabolism of dopamine
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
-
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
-
P-PST
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
-
H-PST, no activity
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate + genistein 4'-sulfate
-
enzyme form SULT1A1, ratio of 7-sulfate formation to 4'-sulfate formation is 8.8
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate + genistein 4'-sulfate
-
enzyme form SULT1E1, ratio of 7-sulfate formation to 4'-sulfate formation is 1.1
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate + genistein 4'-sulfate
-
enzyme form SULT2A1, ratio of 7-sulfate formation to 4'-sulfate formation is 8.8
-
-
?
3'-phosphoadenylylsulfate + genistein 4'-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + genistein 4'-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
-
enzyme form SULT1E1
-
-
?
3'-phosphoadenylylsulfate + genistein 7-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + genistein 7-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
-
enzyme form SULT1E1
-
-
?
3'-phosphoadenylylsulfate + harmol
adenosine 3',5'-bisphosphate + harmol sulfate
-
-
-
?
3'-phosphoadenylylsulfate + harmol
adenosine 3',5'-bisphosphate + harmol sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
-
low activity
-
-
?
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
-
i.e. L-dopa
-
-
?
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
i.e. L-dopa
-
-
?
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
i.e. L-dopa
-
-
?
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
M-PST
-
-
?
3'-phosphoadenylylsulfate + L-thyroxine
adenosine 3',5'-bisphosphate + ?
no activity: ST1B2
-
-
?
3'-phosphoadenylylsulfate + L-thyroxine
adenosine 3',5'-bisphosphate + ?
SULT1A1 allozymes 1 and 2
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
M-PST
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
P-PST
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
TL- and TS-PST
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
activation of the substrate
-
?
3'-phosphoadenylylsulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + ritodrine
adenosine 3',5'-bisphosphate + ritodrine sulfate
-
enzyme form SULT1A1
-
-
?
3'-phosphoadenylylsulfate + ritodrine
adenosine 3',5'-bisphosphate + ritodrine sulfate
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + serotonin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + serotonin
adenosine 3',5'-bisphosphate + ?
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + tyramine O-sulfate
-
-
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + tyramine O-sulfate
SULT1A1
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + tyramine O-sulfate
-
ST1A3 and ST1A5
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
regulation of human SULT1A genes by glucocorticoids, overview
-
-
?
additional information
?
-
-
regulation of human SULT1A genes by glucocorticoids, overview
-
-
?
additional information
?
-
SULT is involved in drug metabolism, detoxification and hormone regulation
-
-
?
additional information
?
-
-
SULT is involved in drug metabolism, detoxification and hormone regulation
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 plays important roles in the presystemic inactivation of b2 agonists in the intestine
-
-
?
additional information
?
-
SULT1A3 plays important roles in the presystemic inactivation of b2 agonists in the intestine
-
-
?
additional information
?
-
-
SULT1A3 plays important roles in the presystemic inactivation of b2 agonists in the intestine
-
-
?
additional information
?
-
the enzyme plays an important role in the regulation and homeostasis of monoamine neurotransmitters, by serving as substrates for SULT1A3, 7-hydroxyserotonin or 6-hydroxydopamine may interfere with the homeostasis of endogenous serotonin and dopamine
-
-
?
additional information
?
-
-
the enzyme plays an important role in the regulation and homeostasis of monoamine neurotransmitters, by serving as substrates for SULT1A3, 7-hydroxyserotonin or 6-hydroxydopamine may interfere with the homeostasis of endogenous serotonin and dopamine
-
-
?
additional information
?
-
analysis of binding site similarities between members of the human cytosolic sulfotransferase family, correlation with small-molecule binding profiles, e.g. of 3,5-dibromo-4-hydroxy-benzoic acid (6,8-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide, 3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide, pyridoxal 5'-phosphate, resveratrol, quercetin dihydrate, and adenosine 5'-(beta,gamma-imino)triphosphate, analysis by combination of computational analysis and experimental data, overview
-
-
?
additional information
?
-
-
analysis of binding site similarities between members of the human cytosolic sulfotransferase family, correlation with small-molecule binding profiles, e.g. of 3,5-dibromo-4-hydroxy-benzoic acid (6,8-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide, 3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide, pyridoxal 5'-phosphate, resveratrol, quercetin dihydrate, and adenosine 5'-(beta,gamma-imino)triphosphate, analysis by combination of computational analysis and experimental data, overview
-
-
?
additional information
?
-
DOPA and 6-hydroxy-DOPA are poor substrates for SULT1A3
-
-
?
additional information
?
-
-
DOPA and 6-hydroxy-DOPA are poor substrates for SULT1A3
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A3
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
estrogens and related compounds are substrate only for P-PST
-
-
?
additional information
?
-
-
2 forms, TL: thermolabile, sulfate conjugation of dopamine and other phenolic monoamines, TS: thermostable, sulfate conjugation of simple phenols, e.g. p-nitrophenol
-
-
?
additional information
?
-
-
sterol-like structures cannot bind to M-PST
-
-
?
additional information
?
-
-
hydroxysteroids are no substrates
-
-
?
additional information
?
-
-
no activity with 5-hydroxyindole acetic acid
-
-
?
additional information
?
-
-
hippocampal H-PST is not active with neuropeptide substrates
-
-
?
additional information
?
-
-
different enzyme forms show overlapping substrate specificities, overview
-
-
?
additional information
?
-
different enzyme forms show overlapping substrate specificities, overview
-
-
?
additional information
?
-
different enzyme forms show overlapping substrate specificities, overview
-
-
?
additional information
?
-
different enzyme forms show overlapping substrate specificities, overview
-
-
?
additional information
?
-
-
M-PST shows no activity with phentolamine
-
-
?
additional information
?
-
-
biogenic amines: the absence of a meta substituent on the phenolic ring, or the presence of a beta-OH group on the aliphatic amine side chain greatly reduces their binding affinities
-
-
?
additional information
?
-
-
no activity: serotonin
-
-
?
additional information
?
-
-
culture of HT-29 cells with TNF-alpha increases activity of SULT1A1, TGF-beta increases activity to a lesser extent, insulin also increases activity of SULT1A1. TNF-alpha, TNF-beta and insulin have little effect on activity of enzyme in neuronal cell line SK-N-SH
-
-
?
additional information
?
-
phenolsulfotransferase is a key enzyme in drug metabolism, bile acid detoxification, and the regulation of intratissue active hormone levels. The increased gene expression of phenolsulfotransferase promotes the efficiency of detoxification. Certain antioxidant phenolic acids could induce PST-P activity in HepG2 cells, by promoting PST-P mRNA and protein expression, suggesting a novel mechanism by which phenolic acids may be implicated in phase II sulfate conjugation. Gallic acid, gentisic acid, p-hydroxybenzoic acid, and p-coumaric acid increase PST-P activity, in a dose-dependent manner. A maximum of 4fold and 5fold induction of PST-P activity is observed for both gallic acid and gentisic acid, adverse effect on cell growth at higher concentrations. A 2fold or 2.5fold increase of PST-P activity is found with either p-coumaric or p-hydroxybenzoic acid treatment, no significant effect is found for ferulic acid treatment
-
-
?
additional information
?
-
-
phenolsulfotransferase is a key enzyme in drug metabolism, bile acid detoxification, and the regulation of intratissue active hormone levels. The increased gene expression of phenolsulfotransferase promotes the efficiency of detoxification. Certain antioxidant phenolic acids could induce PST-P activity in HepG2 cells, by promoting PST-P mRNA and protein expression, suggesting a novel mechanism by which phenolic acids may be implicated in phase II sulfate conjugation. Gallic acid, gentisic acid, p-hydroxybenzoic acid, and p-coumaric acid increase PST-P activity, in a dose-dependent manner. A maximum of 4fold and 5fold induction of PST-P activity is observed for both gallic acid and gentisic acid, adverse effect on cell growth at higher concentrations. A 2fold or 2.5fold increase of PST-P activity is found with either p-coumaric or p-hydroxybenzoic acid treatment, no significant effect is found for ferulic acid treatment
-
-
?
additional information
?
-
-
SULT1A1, occurring in liver plays the most important role among the human sulfotransferases in the hepatic cytosolic 7-preferential sulfation of phytoestrogens
-
-
?
additional information
?
-
-
SULT1A1 catalyzes the sulfation of small planar phenols such as neurotransmitters, steroid hormones, acetaminophen, and 4-nitrophenol
-
-
?
additional information
?
-
SULT1A1 is a phase II metabolism enzyme responsible for xenobiotic sulfonation, substrate specificity and catalytic function, including its role in the sulfonation of endogenous substrates such as oestrogens from crystal structure, overview, SULT1A1 can also bioactivate compounds, e.g. sulfonate pro-carcinogens such as hydroxymethyl polycyclic aromatic hydrocarbons leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis, roles of allelic variants, regulation of expression and activities, overview
-
-
?
additional information
?
-
-
SULT1A1 is a phase II metabolism enzyme responsible for xenobiotic sulfonation, substrate specificity and catalytic function, including its role in the sulfonation of endogenous substrates such as oestrogens from crystal structure, overview, SULT1A1 can also bioactivate compounds, e.g. sulfonate pro-carcinogens such as hydroxymethyl polycyclic aromatic hydrocarbons leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis, roles of allelic variants, regulation of expression and activities, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 plays important roles in the presystemic inactivation of b2 agonists in the liver
-
-
?
additional information
?
-
SULT1A1 plays important roles in the presystemic inactivation of b2 agonists in the liver
-
-
?
additional information
?
-
-
SULT1A1 plays important roles in the presystemic inactivation of b2 agonists in the liver
-
-
?
additional information
?
-
SULT1A1 sulfates a wide variety of phenolic xenobiotics, as well as iodothyronines, and also certain N-hydroxy heterocyclic and aromatic amines, SULT1A1 is a detoxifying enzyme, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
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
?
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
-
no activity with caffeic acid, catechol, 17beta-estradiol, N-hydroxy-4-aminobiphenyl, DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1B2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A1
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1A2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
-
no activity with DDT, 4-aminobiphenyl and 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by SULT1C*2
-
-
?
additional information
?
-
-
role for 3'-phosphoadenylyl sulfate in priming the conformation of substrate binding loops, overview, substrate specificities and binding structures of SULT1B1, SULT1A1, SULT1A3, SULT1C1, SULT1C2, and SULT1C3, overview
-
-
?
additional information
?
-
-
substrate specifiicty of SULT1A1*1, *2, and *3, allozyme activities against catecholestrogens and dietary flavonoids, overview
-
-
?
additional information
?
-
SULT1A1 catalyzes the sulfation of small planar phenolic compounds, substrate specificity of the three allozymes SULT1A1*1, *2, and *3, overview
-
-
?
additional information
?
-
-
SULT1A1 catalyzes the sulfation of small planar phenolic compounds, substrate specificity of the three allozymes SULT1A1*1, *2, and *3, overview
-
-
?
additional information
?
-
SULT1A1 catalyzes the sulfation of the active metabolizes of tamoxifen and endoxifen
-
-
?
additional information
?
-
-
the enzyme is active in conjugating the polychlorobiphenyl alcohols, e.g. 3'-OH-trichlorobiphenyl, 4'-OH-trichlorobiphenyl and 4'-OH-(chlorobiphenyl)112, SULT2A1 is active with 4-OH-(chlorobiphenyl)34 and 4'-OH-(chlorobiphenyl)68, but not with 4'-OH-nonachlorobiphenyl
-
-
?
additional information
?
-
-
epigallocatechin gallate is not a substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 3'-phosphoadenylyl sulfate + 2 dopamine
2 adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + dopamine 4-O-sulfate
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3-nitro-L-tyrosine
adenosine 3',5'-bisphosphate + 3-nitro-O4-sulfo-L-tyrosine
sulfation serves as a pathway for the metabolism/regulation of nitrotyrosine, nitrotyrosine O-sulfate is released into the medium of Hep-G2 hepatoma cells
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + 6-hydroxydopamine
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 7-hydroxyserotonin
adenosine 3',5'-bisphosphate + ?
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
-
-
-
?
3'-phosphoadenylyl sulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + serotonin
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 17alpha-ethinylestradiol
?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methoxyestradiol
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
sulfation inactivates the hydroxylated metabolite of tibolone, a synthetic steroid used for the treatment for climacteric symptoms and postmenopausal osteoporosis
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + 4-(sulfooxy)tamoxifen
a potent inducer of apoptosis in breast tumor cell lines
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
3'-phosphoadenylyl sulfate + 5-amino-2-(4-amino-3-fluorophenyl)-6,8-difluoro-7-methyl-4H-1-benzopyran-4-one
adenosine 3',5'-bisphosphate + ?
i.e. aminoflavone, diaminoflavone analogues with potent growth-inhibitory activity against human breast and renal cancer cells in vitro and antitumor activity in mice bearing human tumor xenografts, aminoflavone binds to DNA in tumor cells and induces DNA-protein cross-links
-
-
?
3'-phosphoadenylyl sulfate + 5-chloro-7-iodo-8-quinolinol
adenosine 3',5'-bisphosphate + 5-chloro-7-iodo-8-quinolinyl sulfate
-
isoform SULT1A3 is responsible for the 5-chloro-7-iodo-8-quinolinol sulfation in human jejunum
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylyl sulfate + acetaminophen
adenosine 3',5'-bisphosphate + 4-(acetylamino)phenylsulfate
-
-
-
?
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 + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
-
-
-
-
r
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopaminyl sulfate
-
specific substrate for isoform SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol sulfate
-
the enzyme also performs the reaction of EC 2.8.2.4, estrone sulfotransferase, with low activity
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + minoxidil
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
-
-
-
?
3'-phosphoadenylyl sulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
accounts for approximately 10% of the enzymic activity directed towards catabolism of dopamine
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
adenosine 3',5'-bisphosphate + dopamine sulfate
3'-phosphoadenylyl sulfate + dopamine
-
-
-
-
r
additional information
?
-
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
-
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
phase II drug metabolizing or detoxifying enzyme
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
sulfate conjugation of phenolic biogenic amines, important in the biotransformation of many neurotransmitters, hormones, drugs, and xenobiotic compounds
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
sulfation of environmental estrogens, overview
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
-
SULTs, especially SULT1A1, are important in xenobiotic and drug metabolism because of their broad substrate specificity and extensive tissue distribution
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
TL- and TS-PST
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
-
activation of the substrate
-
?
additional information
?
-
regulation of human SULT1A genes by glucocorticoids, overview
-
-
?
additional information
?
-
-
regulation of human SULT1A genes by glucocorticoids, overview
-
-
?
additional information
?
-
SULT is involved in drug metabolism, detoxification and hormone regulation
-
-
?
additional information
?
-
-
SULT is involved in drug metabolism, detoxification and hormone regulation
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1A3 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A3 plays important roles in the presystemic inactivation of b2 agonists in the intestine
-
-
?
additional information
?
-
SULT1A3 plays important roles in the presystemic inactivation of b2 agonists in the intestine
-
-
?
additional information
?
-
-
SULT1A3 plays important roles in the presystemic inactivation of b2 agonists in the intestine
-
-
?
additional information
?
-
the enzyme plays an important role in the regulation and homeostasis of monoamine neurotransmitters, by serving as substrates for SULT1A3, 7-hydroxyserotonin or 6-hydroxydopamine may interfere with the homeostasis of endogenous serotonin and dopamine
-
-
?
additional information
?
-
-
the enzyme plays an important role in the regulation and homeostasis of monoamine neurotransmitters, by serving as substrates for SULT1A3, 7-hydroxyserotonin or 6-hydroxydopamine may interfere with the homeostasis of endogenous serotonin and dopamine
-
-
?
additional information
?
-
-
culture of HT-29 cells with TNF-alpha increases activity of SULT1A1, TGF-beta increases activity to a lesser extent, insulin also increases activity of SULT1A1. TNF-alpha, TNF-beta and insulin have little effect on activity of enzyme in neuronal cell line SK-N-SH
-
-
?
additional information
?
-
phenolsulfotransferase is a key enzyme in drug metabolism, bile acid detoxification, and the regulation of intratissue active hormone levels. The increased gene expression of phenolsulfotransferase promotes the efficiency of detoxification. Certain antioxidant phenolic acids could induce PST-P activity in HepG2 cells, by promoting PST-P mRNA and protein expression, suggesting a novel mechanism by which phenolic acids may be implicated in phase II sulfate conjugation. Gallic acid, gentisic acid, p-hydroxybenzoic acid, and p-coumaric acid increase PST-P activity, in a dose-dependent manner. A maximum of 4fold and 5fold induction of PST-P activity is observed for both gallic acid and gentisic acid, adverse effect on cell growth at higher concentrations. A 2fold or 2.5fold increase of PST-P activity is found with either p-coumaric or p-hydroxybenzoic acid treatment, no significant effect is found for ferulic acid treatment
-
-
?
additional information
?
-
-
phenolsulfotransferase is a key enzyme in drug metabolism, bile acid detoxification, and the regulation of intratissue active hormone levels. The increased gene expression of phenolsulfotransferase promotes the efficiency of detoxification. Certain antioxidant phenolic acids could induce PST-P activity in HepG2 cells, by promoting PST-P mRNA and protein expression, suggesting a novel mechanism by which phenolic acids may be implicated in phase II sulfate conjugation. Gallic acid, gentisic acid, p-hydroxybenzoic acid, and p-coumaric acid increase PST-P activity, in a dose-dependent manner. A maximum of 4fold and 5fold induction of PST-P activity is observed for both gallic acid and gentisic acid, adverse effect on cell growth at higher concentrations. A 2fold or 2.5fold increase of PST-P activity is found with either p-coumaric or p-hydroxybenzoic acid treatment, no significant effect is found for ferulic acid treatment
-
-
?
additional information
?
-
-
SULT1A1, occurring in liver plays the most important role among the human sulfotransferases in the hepatic cytosolic 7-preferential sulfation of phytoestrogens
-
-
?
additional information
?
-
-
SULT1A1 catalyzes the sulfation of small planar phenols such as neurotransmitters, steroid hormones, acetaminophen, and 4-nitrophenol
-
-
?
additional information
?
-
SULT1A1 is a phase II metabolism enzyme responsible for xenobiotic sulfonation, substrate specificity and catalytic function, including its role in the sulfonation of endogenous substrates such as oestrogens from crystal structure, overview, SULT1A1 can also bioactivate compounds, e.g. sulfonate pro-carcinogens such as hydroxymethyl polycyclic aromatic hydrocarbons leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis, roles of allelic variants, regulation of expression and activities, overview
-
-
?
additional information
?
-
-
SULT1A1 is a phase II metabolism enzyme responsible for xenobiotic sulfonation, substrate specificity and catalytic function, including its role in the sulfonation of endogenous substrates such as oestrogens from crystal structure, overview, SULT1A1 can also bioactivate compounds, e.g. sulfonate pro-carcinogens such as hydroxymethyl polycyclic aromatic hydrocarbons leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis, roles of allelic variants, regulation of expression and activities, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1A1 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A1 plays important roles in the presystemic inactivation of b2 agonists in the liver
-
-
?
additional information
?
-
SULT1A1 plays important roles in the presystemic inactivation of b2 agonists in the liver
-
-
?
additional information
?
-
-
SULT1A1 plays important roles in the presystemic inactivation of b2 agonists in the liver
-
-
?
additional information
?
-
SULT1A1 sulfates a wide variety of phenolic xenobiotics, as well as iodothyronines, and also certain N-hydroxy heterocyclic and aromatic amines, SULT1A1 is a detoxifying enzyme, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1A2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
additional information
?
-
-
SULT1C*2 is involved in sulfation of toxicants in cigarette smoke extracts. By serving as substrates for SULTs, cigarette smoke toxicants may interfere with the metabolism of 17beta-estradiol and other endogenous compounds, overview
-
-
?
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
?
-
-
the enzyme is active in conjugating the polychlorobiphenyl alcohols, e.g. 3'-OH-trichlorobiphenyl, 4'-OH-trichlorobiphenyl and 4'-OH-(chlorobiphenyl)112, SULT2A1 is active with 4-OH-(chlorobiphenyl)34 and 4'-OH-(chlorobiphenyl)68, but not with 4'-OH-nonachlorobiphenyl
-
-
?
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Aberrant Crypt Foci
Intestinal carcinogenesis of two food processing contaminants, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine and 5-hydroxymethylfurfural, in transgenic FVB min mice expressing human sulfotransferases.
Acquired Immunodeficiency Syndrome
Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation.
Acute Kidney Injury
Suppressed Hepatic Production of Indoxyl Sulfate Attenuates Cisplatin-Induced Acute Kidney Injury in Sulfotransferase 1a1-Deficient Mice.
Adenocarcinoma
Expression of the orphan cytosolic sulfotransferase SULT1C3 in human intestine: characterization of the transcript variant and implications for function.
Adenocarcinoma
Features of the Copy Number Variation of Certain Genes in Tumor Cells in Patients with Serous Ovarian Adenocarcinoma.
Adenocarcinoma
Genomic characteristics of pancreatic squamous cell carcinoma, an investigation by using high throughput sequencing after in-solution hybrid capture.
Adenocarcinoma
Interaction of the cytochrome P4501A2, SULT1A1 and NAT gene polymorphisms with smoking and dietary mutagen intake in modification of the risk of pancreatic cancer.
Adenocarcinoma
Regulation of SULT1E1 expression in Ishikawa adenocarcinoma cells by tibolone.
Adenocarcinoma
Steroid sulphotransferase and 17beta-hydroxysteroid dehydrogenase activities in Ishikawa human endometrial adenocarcinoma cells.
Adenocarcinoma
Sulfotransferase 1A1 polymorphism and gastric cancer risk: a pilot case-control study.
Adenocarcinoma
Transcriptional Regulation of Cytosolic Sulfotransferase 1C2 by Vitamin D Receptor in LS180 Human Colorectal Adenocarcinoma Cells.
Adenocarcinoma
Transcriptional Regulation of Human Cytosolic Sulfotransferase 1C3 by Peroxisome Proliferator-Activated Receptor ? in LS180 Human Colorectal Adenocarcinoma Cells.
Adenoma
Benign cortisol-secreting adrenocortical adenomas produce small amounts of androgens.
Adenoma
Effect of SULT1A1 and NAT2 genetic polymorphism on the association between cigarette smoking and colorectal adenomas.
Adenoma
Polymorphisms in heterocyclic aromatic amines metabolism-related genes are associated with colorectal adenoma risk.
Adenomyosis
Adenomyosis: genetics of estrogen metabolism.
Alopecia
Characterization of follicular minoxidil sulfotransferase activity in a cohort of pattern hair loss patients from the Indian Subcontinent.
Alopecia
Minoxidil Sulfotransferase Enzyme (SULT1A1) genetic variants predicts response to oral minoxidil treatment for female pattern hair loss.
Alopecia
SULT1A1 (Minoxidil Sulfotransferase) enzyme booster significantly improves response to topical minoxidil for hair regrowth.
Alzheimer Disease
Reduced sulfotransferase SULT2A1 activity in patients with Alzheimer's disease.
aryl sulfotransferase deficiency
A cerebroside sulphotransferase deficiency in a human disorder of myelin.
aryl sulfotransferase deficiency
A Cerebroside Sulphotransferase Deficiency in a Human Disorder of Myelin.
Asthma
SULT 1A3 single-nucleotide polymorphism and the single dose pharmacokinetics of inhaled salbutamol enantiomers: Are some athletes at risk of higher urine levels?
Atherosclerosis
Interaction of Native- and Oxidized-Low-Density Lipoprotein with Human Estrogen Sulfotransferase.
Atherosclerosis
Peculiarities of Immune Regulation in Men of Perm Region with Atherosclerosis Related to Polymorphism of Candidate Genes.
Brain Neoplasms
Sulfotransferase 1A1 (SULT1A1) polymorphism and susceptibility to primary brain tumors.
Breast Diseases
Expression of estrogenicity genes in a lineage cell culture model of human breast cancer progression.
Breast Neoplasms
Acute Effect of High-dose Isoflavones from Pueraria lobata (Willd.) Ohwi on Lipid and Bone Metabolism in Ovariectomized Mice.
Breast Neoplasms
Adrenal androgen concentrations in breast tumours and in normal breast tissue. The relationship to oestradiol metabolism.
Breast Neoplasms
Alterations in Hepatic mRNA Expression of Phase-II Enzymes and Xenobiotic Transporters after Targeted Disruption of Hepatocyte Nuclear Factor 4 alpha.
Breast Neoplasms
Altered expression of the hormone- and xenobiotic-metabolizing sulfotransferase enzymes 1A2 and 1C1 in malignant breast tissue.
Breast Neoplasms
Association between sulfotransferase 1A1 genotype and survival of breast cancer patients receiving tamoxifen therapy.
Breast Neoplasms
Association between SULT1A1 Arg213His (rs9282861) Polymorphism and Risk of Breast Cancer: A Systematic Review and Meta-Analysis.
Breast Neoplasms
Association of sulfotransferase SULT1A1 with breast cancer risk: a meta-analysis of case-control studies with subgroups of ethnic and menopausal statue.
Breast Neoplasms
Association of SULT1A1 Arg²¹³His polymorphism with male breast cancer risk: results from a multicenter study in Italy.
Breast Neoplasms
Associations between tamoxifen, estrogens, and FSH serum levels during steady state tamoxifen treatment of postmenopausal women with breast cancer.
Breast Neoplasms
Bacterial expression and kinetic characterization of the human monoamine-sulfating form of phenol sulfotransferase.
Breast Neoplasms
Bilateral adrenalectomy for metastatic breast carcinoma.
Breast Neoplasms
Bile Salt Homeostasis in Normal and Bsep Gene Knockout Rats with Single and Repeated Doses of Troglitazone.
Breast Neoplasms
Biotransformation of melatonin in human breast cancer cell lines: role of sulfotransferase 1A1.
Breast Neoplasms
Cancer and molecular biomarkers of phase 2.
Breast Neoplasms
Case-control study and meta-analysis of SULT1A1 Arg213His polymorphism for gene, ethnicity and environment interaction for cancer risk.
Breast Neoplasms
Characterization of Formononetin Sulfonation in SULT1A3 Overexpressing HKE293 Cells: Involvement of Multidrug Resistance-Associated Protein 4 in Excretion of Sulfate.
Breast Neoplasms
Common germline polymorphisms in COMT, CYP19A1, ESR1, PGR, SULT1E1 and STS and survival after a diagnosis of breast cancer.
Breast Neoplasms
CYP17 and SULT1A1 gene polymorphisms in Indian breast cancer.
Breast Neoplasms
Do single nucleotide polymorphisms in xenobiotic metabolizing genes determine breast cancer susceptibility and treatment outcomes?
Breast Neoplasms
Effect of interferon-?2b on the expression of various drug-metabolizing enzymes and transporters in co-cultures of freshly prepared human primary hepatocytes.
Breast Neoplasms
Effects of SULT1A1 Copy Number Variation on Estrogen Concentration and Tamoxifen-Associated Adverse Drug Reactions in Premenopausal Thai Breast Cancer Patients: A Preliminary Study.
Breast Neoplasms
Epigenetic silencing of the sulfotransferase 1A1 gene by hypermethylation in breast tissue.
Breast Neoplasms
Estrogen metabolism-related genes and breast cancer risk: the multiethnic cohort study.
Breast Neoplasms
Estrogen sulfotransferases in breast and endometrial cancers.
Breast Neoplasms
Estrogen-related genes and their contribution to racial differences in breast cancer risk.
Breast Neoplasms
Expression of estrogenicity genes in a lineage cell culture model of human breast cancer progression.
Breast Neoplasms
Expression of hydroxysteroid sulphotransferase is related to estrogen receptor status in human mammary cancer.
Breast Neoplasms
Genetic polymorphism of estrogen metabolizing enzymes in siberian women with breast cancer.
Breast Neoplasms
Genetic polymorphisms in human SULT1A1 and UGT1A1 genes associate with breast tumor characteristics: a case-series study.
Breast Neoplasms
Genetic polymorphisms of SULT1A1 and SULT1E1 and the risk and survival of breast cancer.
Breast Neoplasms
Genetic variants of CYP3A5, CYP2D6, SULT1A1, UGT2B15 and tamoxifen response in postmenopausal patients with breast cancer.
Breast Neoplasms
Genetic variants of the sulfotransferase 1A1 and breast cancer risk.
Breast Neoplasms
Genotype of metabolic enzymes and the benefit of tamoxifen in postmenopausal breast cancer patients.
Breast Neoplasms
Genotypic and allelic frequencies of SULT1A1 polymorphisms in women receiving adjuvant tamoxifen therapy.
Breast Neoplasms
Identification and characterization of cytosolic sulfotransferase activities in MCF-7 human breast carcinoma cells.
Breast Neoplasms
Identification and targeting of selective vulnerability rendered by tamoxifen resistance.
Breast Neoplasms
Immunohistochemical localisation of hydroxysteroid sulphotransferase in human breast carcinoma tissue: a preliminary study.
Breast Neoplasms
Indoxylsulfate, a Metabolite of the Microbiome, Has Cytostatic Effects in Breast Cancer via Activation of AHR and PXR Receptors and Induction of Oxidative Stress.
Breast Neoplasms
Interactions between genetic polymorphism of cytochrome P450-1B1, sulfotransferase 1A1, catechol-o-methyltransferase and tobacco exposure in breast cancer risk.
Breast Neoplasms
Investigation of prognostic value of polymorphisms within estrogen metabolizing genes in Lithuanian breast cancer patients.
Breast Neoplasms
Metabolism of resveratrol in breast cancer cell lines: Impact of sulfotransferase 1A1 expression on cell growth inhibition.
Breast Neoplasms
Modifying effects of sulfotransferase 1A1 gene polymorphism on the association of breast cancer risk with body mass index or endogenous steroid hormones.
Breast Neoplasms
Need for clarification of results in the recent meta-analysis about SULT1A1 codon 213 polymorphism and breast cancer risk.
Breast Neoplasms
Pairwise combinations of estrogen metabolism genotypes in postmenopausal breast cancer etiology.
Breast Neoplasms
Phenol sulfotransferases: hormonal regulation, polymorphism, and age of onset of breast cancer.
Breast Neoplasms
Phytoestrogens and xenoestrogens: the contribution of diet and environment to endocrine disruption.
Breast Neoplasms
Polymorphisms of estrogen-metabolizing genes and breast cancer risk: a multigenic study.
Breast Neoplasms
Possible Risk Modification by Polymorphisms of Estrogen Metabolizing Genes in Familial Breast Cancer Susceptibility in an Indian Population.
Breast Neoplasms
Properties of estrogen and hydroxysteroid sulphotransferases in human mammary cancer.
Breast Neoplasms
Relationship between genotypes Sult1a2 and Cyp2d6 and tamoxifen metabolism in breast cancer patients.
Breast Neoplasms
Steroid sulphotransferase activity in human hormone-independent MDA-MB-468 mammary cancer cells.
Breast Neoplasms
Sulfation disposition of liquiritigenin in SULT1A3 overexpressing HEK293 cells: The role of breast cancer resistance protein (BCRP) and multidrug resistance-associated protein 4 (MRP4) in sulfate efflux of liquiritigenin.
Breast Neoplasms
Sulfation through the looking glass--recent advances in sulfotransferase research for the curious.
Breast Neoplasms
Sulfonation of raloxifene in HEK293 cells overexpressing SULT1A3: Involvement of breast cancer resistance protein (BCRP/ABCG2) and multidrug resistance-associated protein 4 (MRP4/ABCC4) in excretion of sulfate metabolites.
Breast Neoplasms
Sulfotransferase 1A1 (SULT1A1) gene expression is regulated by members of the NFI transcription factors in human breast cancer cells.
Breast Neoplasms
Sulfotransferase 1A1 (SULT1A1) polymorphism and breast cancer risk in Chinese women.
Breast Neoplasms
Sulfotransferase 1A1 (SULT1A1) polymorphism, PAH-DNA adduct levels in breast tissue and breast cancer risk in a case-control study.
Breast Neoplasms
Sulfotransferase 1A1 genotype as a potential modifier of breast cancer risk among premenopausal women.
Breast Neoplasms
Sulfotransferase 1A1 polymorphism, endogenous estrogen exposure, well-done meat intake, and breast cancer risk.
Breast Neoplasms
Sulfotransferase 1A2*2 is a risk factor for early-onset breast cancer.
Breast Neoplasms
Sulfotransferase SULT1A1 Arg213His polymorphism with cancer risk: a meta-analysis of 53 case-control studies.
Breast Neoplasms
SULT1A1 Arg213His Polymorphism, Smoked Meat, and Breast Cancer Risk: A Case-Control Study and Meta-Analysis.
Breast Neoplasms
SULT1A1 catalyzes 2-methoxyestradiol sulfonation in MCF-7 breast cancer cells.
Breast Neoplasms
SULT1A1 genotype, active and passive smoking, and breast cancer risk by age 50 years in a German case-control study.
Breast Neoplasms
SULT1A1 polymorphism and esophageal cancer in males.
Breast Neoplasms
SULT1A1 R213H polymorphism and breast cancer risk: a meta-analysis based on 8,454 cases and 11,800 controls.
Breast Neoplasms
SULT1A1 rs9282861 polymorphism-a potential modifier of efficacy of the systemic adjuvant therapy in breast cancer?
Breast Neoplasms
SULT1A1, CYP2C19 and disease-free survival in early breast cancer patients receiving tamoxifen.
Breast Neoplasms
SULT1E1 and ID2 genes as candidates for inherited predisposition to breast and ovarian cancer in Jewish women.
Breast Neoplasms
SULT1E1 inhibits cell proliferation and invasion by activating PPAR? in breast cancer.
Breast Neoplasms
The association of SULT1A1 codon 213 polymorphism and breast cancer susceptibility: meta-analysis from 16 studies involving 23,445 subjects.
Breast Neoplasms
[A case-control study on association of SULT1A1 polymorphism, smoked meat intake with breast cancer risk].
Breast Neoplasms
[Association of polymorphisms in SULT1A1 and UGT1A1 Genes with breast cancer risk and phenotypes in Russian women]
Breast Neoplasms
[Study on the relationship between polymorphisms of genes (CYP17, CYP19 and SULT1A1) and susceptibility to breast cancer in Chinese women]
Breast Neoplasms
[The association of sulfotransferase1A1 His allele and breast cancer in Han ethnic Chinese women]
Breast Neoplasms, Male
Association of SULT1A1 Arg²¹³His polymorphism with male breast cancer risk: results from a multicenter study in Italy.
Breast Neoplasms, Male
SULT1A1 gene deletion in BRCA2-associated male breast cancer: a link between genes and environmental exposures?
Carcinogenesis
Dietary flavonoids: Effects on xenobiotic and carcinogen metabolism.
Carcinogenesis
Effect of cigarette smoke on mutagenic activation of environmental carcinogens by cytochrome P450 2A8 and inactivation by glucuronidation in hamster liver.
Carcinogenesis
Effect of estrogen sulfation by SULT1E1 and PAPSS on the development of estrogen-dependent cancers.
Carcinogenesis
Epigenetic silencing of the sulfotransferase 1A1 gene by hypermethylation in breast tissue.
Carcinogenesis
Examination of human tissue cytosols for expression of sulfotransferase isoform 1A2 (SULT1A2) using a SULT1A2-specific antibody.
Carcinogenesis
Genetic polymorphisms in CYP1A1, CYP2D6, UGT1A6, UGT1A7, and SULT1A1 genes and correlation with benzene exposure in a Chinese occupational population.
Carcinogenesis
Possible involvement of sulfotransferase 1A1 in estragole-induced DNA modification and carcinogenesis in the livers of female mice.
Carcinogenesis
Relationship of SULT1A1 copy number variation with estrogen metabolism and human health.
Carcinogenesis
Sulfotransferase 1A1 as a Biomarker for Susceptibility to Carcinogenesis: From Molecular Genetics to the Role of Dietary Flavonoids.
Carcinogenesis
Sulfotransferase SULT1A1 Arg213His polymorphism with cancer risk: a meta-analysis of 53 case-control studies.
Carcinogenesis
The loss of phenol sulfotransferase 1 in hepatocellular carcinogenesis.
Carcinogenesis
Transcriptomic-based toxicological investigations of ethanol to human umbilical vein endothelial cells.
Carcinogenesis
[A case-control study on the association between the genetic polymorphism of sulfotransferase 1A1, diet and susceptibility of colorectal cancer]
Carcinoma
A case-control study investigating the role of sulfotransferase 1A1 polymorphism in head and neck cancer.
Carcinoma
Coffee reduces SULT1E1 expression in human colon carcinoma Caco-2 cells.
Carcinoma
Combined effects of GSTO1 and SULT1A1 polymorphisms and cigarette smoking on urothelial carcinoma risk in a Taiwanese population.
Carcinoma
Cytochrome P450 (CYP) 1A2, sulfotransferase (SULT) 1A1, and N-acetyltransferase (NAT) 2 polymorphisms and susceptibility to urothelial cancer.
Carcinoma
Epigallocatechin gallate (EGCG) inhibits the sulfation of 1-naphthol in a human colon carcinoma cell line, Caco-2.
Carcinoma
Gene-environment interaction: the role of SULT1A1 and CYP3A5 polymorphisms as risk modifiers for squamous cell carcinoma of the oesophagus.
Carcinoma
Genotypes of CYP1A1,?SULT1A1 and SULT1A2 and risk of squamous cell carcinoma of esophagus: outcome of a case-control study from Kashmir, India.
Carcinoma
Human phenol sulfotransferases hP-PST and hM-PST activate propane 2-nitronate to a genotoxicant.
Carcinoma
Immunohistochemical localisation of hydroxysteroid sulphotransferase in human breast carcinoma tissue: a preliminary study.
Carcinoma
Inhibitory effects of green tea and grape juice on the phenol sulfotransferase activity of mouse intestines and human colon carcinoma cell line, Caco-2.
Carcinoma
Phenol sulfotransferase SULT1A1*2 allele and enhanced risk of upper urinary tract urothelial cell carcinoma.
Carcinoma
Quantitative analysis of the association between sulfotransferase isoform 1A1 polymorphism and risk of urothelial carcinoma.
Carcinoma
Sulfotransferase 1A1 haplotypes associated with oral squamous cell carcinoma susceptibility in male Taiwanese.
Carcinoma
SULT1A1 polymorphism and esophageal cancer in males.
Carcinoma, Hepatocellular
Activity of sulfotransferase 1A1 is dramatically upregulated in patients with hepatocellular carcinoma secondary to chronic hepatitis B virus infection.
Carcinoma, Hepatocellular
Gel-based proteomics of liver cancer progression in rat.
Carcinoma, Hepatocellular
Generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible.
Carcinoma, Hepatocellular
Induction of human sulfotransferase 1A3 (SULT1A3) by glucocorticoids.
Carcinoma, Hepatocellular
Involvement of p38 MAPK and Nrf2 in phenolic acid-induced P-form phenol sulfotransferase expression in human hepatoma HepG2 cells.
Carcinoma, Hepatocellular
Manganese-dependent Dopa/tyrosine sulfation in HepG2 human hepatoma cells: novel Dopa/tyrosine sulfotransferase activities associated with the human monoamine-form phenol sulfotransferase.
Carcinoma, Hepatocellular
Overexpression of SULT2B1b Promotes Angiogenesis in Human Gastric Cancer.
Carcinoma, Hepatocellular
Substrate specificity of human monoamine (M)-form phenol sulfotransferase: preparation and analysis of Dopa 3-O-sulfate and Dopa 4-O-sulfate.
Carcinoma, Hepatocellular
Suppression of DHEA sulfotransferase (Sult2A1) during the acute-phase response.
Carcinoma, Hepatocellular
Transcriptional profiling reveals a role for ROR{alpha} in regulating gene expression in obesity-associated inflammation and hepatic steatosis.
Carcinoma, Non-Small-Cell Lung
Potentially functional genetic variants in PLIN2, SULT2A1 and UGT1A9 genes of the ketone pathway and survival of nonsmall cell lung cancer.
Carcinoma, Squamous Cell
A case-control study investigating the role of sulfotransferase 1A1 polymorphism in head and neck cancer.
Carcinoma, Squamous Cell
Gene-environment interaction: the role of SULT1A1 and CYP3A5 polymorphisms as risk modifiers for squamous cell carcinoma of the oesophagus.
Carcinoma, Squamous Cell
Genotypes of CYP1A1,?SULT1A1 and SULT1A2 and risk of squamous cell carcinoma of esophagus: outcome of a case-control study from Kashmir, India.
Carcinoma, Transitional Cell
Cytochrome P450 (CYP) 1A2, sulfotransferase (SULT) 1A1, and N-acetyltransferase (NAT) 2 polymorphisms and susceptibility to urothelial cancer.
Chemical and Drug Induced Liver Injury
ASS and SULT2A1 are Novel and Sensitive Biomarkers of Acute Hepatic Injury-A Comparative Study in Animal Models.
Cholangitis, Sclerosing
Liver Expression of Sulphotransferase 2A1 Enzyme Is Impaired in Patients with Primary Sclerosing Cholangitis: Lack of the Response to Enhanced Expression of PXR.
Cholestasis
A novel constitutive androstane receptor-mediated and CYP3A-independent pathway of bile acid detoxification.
Cholestasis
Bile salt sulphation in man. Liver bile salt sulphotransferase activity in patients with primary biliary cirrhosis.
Cholestasis
Bile salt sulphotransferase activity in the liver of cholestatic infants.
Cholestasis
Cholestasis-induced bile acid elevates estrogen level via farnesoid X receptor-mediated suppression of the estrogen sulfotransferase SULT1E1.
Cholestasis
Enzymatic sulphation of bile salts in man. Bile salt sulphotransferase activity in percutaneous liver biopsy specimens from patients with liver disease.
Cholestasis
Hepatic expression of detoxification enzymes is decreased in human obstructive cholestasis due to gallstone biliary obstruction.
Cholestasis
Upregulation of UGT2B4 Expression by 3'-Phosphoadenosine-5'-Phosphosulfate Synthase Knockdown: Implications for Coordinated Control of Bile Acid Conjugation.
Colonic Neoplasms
A novel constitutive androstane receptor-mediated and CYP3A-independent pathway of bile acid detoxification.
Colonic Neoplasms
Alterations of O-glycan biosynthesis in human colon cancer tissues.
Colorectal Neoplasms
Analysis of total meat intake and exposure to individual heterocyclic amines in a case-control study of colorectal cancer: contribution of metabolic variation to risk.
Colorectal Neoplasms
Association of the SULT1A1 R213H polymorphism with colorectal cancer.
Colorectal Neoplasms
Case-only study of interactions between metabolic enzymes and smoking in colorectal cancer.
Colorectal Neoplasms
Lack of association of SULT1A1 R213H polymorphism with colorectal cancer: a meta-analysis.
Colorectal Neoplasms
Metabolic differences and their impact on human disease Sulfotransferase and colorectal cancer.
Colorectal Neoplasms
Phenol sulphotransferase SULT1A1*1 genotype is associated with reduced risk of colorectal cancer.
Colorectal Neoplasms
Polymorphisms in sulfotransferase 1A1 and glutathione S-transferase P1 genes in relation to colorectal cancer risk and patients' survival.
Colorectal Neoplasms
Polymorphisms in sulfotransferases SULT1A1 and SULT1A2 are not related to colorectal cancer.
Colorectal Neoplasms
Red meat intake, doneness, polymorphisms in genes that encode carcinogen-metabolizing enzymes, and colorectal cancer risk.
Colorectal Neoplasms
SULT1A1 genotype and susceptibility to colorectal cancer.
Colorectal Neoplasms
The Interaction of Smoking with Gene Polymorphisms on Four Digestive Cancers: A Systematic Review and Meta-Analysis.
Colorectal Neoplasms
[A case-control study on the association between the genetic polymorphism of sulfotransferase 1A1, diet and susceptibility of colorectal cancer]
Corneal Dystrophies, Hereditary
Macular corneal dystrophy type I and type II are caused by distinct mutations in a new sulphotransferase gene.
Coronary Artery Disease
Genetic polymorphisms in platelet-related proteins and coronary artery disease: investigation of candidate genes, including N-acetylgalactosaminyltransferase 4 (GALNT4) and sulphotransferase 1A1/2 (SULT1A1/2).
Crohn Disease
Phase 1 Clinical Study of siRNA Targeting Carbohydrate Sulphotransferase 15 in Crohn's Disease Patients with Active Mucosal Lesions.
Cystic Fibrosis
Elevated hepatic SULT1E1 activity in mouse models of cystic fibrosis alters the regulation of estrogen responsive proteins.
Cystic Fibrosis
Elevation of hepatic sulphotransferase activities in mice with resistance to cystic fibrosis.
Cystic Fibrosis
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases.
Cystic Fibrosis
Regulation of hepatic sulfotransferase (SULT) 1E1 expression and effects on estrogenic activity in cystic fibrosis (CF).
Dementia
Evaluation of factors of importance for clinical dementia diagnosis.
Diabetes Mellitus, Type 2
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases.
Drug-Related Side Effects and Adverse Reactions
Effects of SULT1A1 Copy Number Variation on Estrogen Concentration and Tamoxifen-Associated Adverse Drug Reactions in Premenopausal Thai Breast Cancer Patients: A Preliminary Study.
Endometrial Neoplasms
CHEK2, MGMT, SULT1E1 and SULT1A1 polymorphisms and endometrial cancer risk.
Endometrial Neoplasms
CYP1A1, SULT1A1, and SULT1E1 polymorphisms are risk factors for endometrial cancer susceptibility.
Endometrial Neoplasms
Disturbed expression of phase I and phase II estrogen-metabolizing enzymes in endometrial cancer: Lower levels of CYP1B1 and increased expression of S-COMT.
Endometrial Neoplasms
Estrogen sulfation genes, hormone replacement therapy, and endometrial cancer risk.
Endometrial Neoplasms
The relationship between oestradiol metabolism and adrenal steroids in the endometrium of postmenopausal women with and without endometrial cancer.
Endometriosis
Effects of steroid hormone on estrogen sulfotransferase and on steroid sulfatase expression in endometriosis tissue and stromal cells.
Endotoxemia
ASS and SULT2A1 are Novel and Sensitive Biomarkers of Acute Hepatic Injury-A Comparative Study in Animal Models.
Ependymoma
Identification of tumor-specific molecular signatures in intracranial ependymoma and association with clinical characteristics.
Epilepsy
Platelet 3H-imipramine binding and sulphotransferase activity in primary headache.
Esophageal Neoplasms
SULT1A1 polymorphism and esophageal cancer in males.
Esophageal Squamous Cell Carcinoma
SULT1A1 polymorphism and esophageal cancer in males.
Fatty Liver
Exome-wide scan identifies significant association of rs4788084 in IL27 promoter with increase in hepatic fat content among Indians.
Fatty Liver
Hepatic oestrone sulphotransferase activity and plasma levels of oestrone sulphate, oestrone and oestradiol in male guinea pigs with fatty liver.
Genital Diseases, Female
Estrogen-metabolizing gene polymorphisms in the assessment of female hormone-dependent cancer risk.
Glioma
Regulation of SULT2B1a (pregnenolone sulfotransferase) expression in rat C6 glioma cells: relevance of AMPA receptor-mediated NO signaling.
Goiter, Nodular
Human thyroid phenol sulfotransferase enzymes 1A1 and 1A3: activities in normal and diseased thyroid glands, and inhibition by thyroid hormones and phytoestrogens.
Head and Neck Neoplasms
A case-control study investigating the role of sulfotransferase 1A1 polymorphism in head and neck cancer.
Hepatitis B, Chronic
Activity of sulfotransferase 1A1 is dramatically upregulated in patients with hepatocellular carcinoma secondary to chronic hepatitis B virus infection.
Herpes Simplex
Transcriptomic-based toxicological investigations of ethanol to human umbilical vein endothelial cells.
Herpes Zoster
Alteration of the steroidogenesis in boys with autism spectrum disorders.
Herpes Zoster
Development of adrenal cortical zonation and expression of key elements of adrenal androgen production in the chimpanzee (Pan troglodytes) from birth to adulthood.
Hypersensitivity
Relationship of SULT1A1 copy number variation with estrogen metabolism and human health.
Hypotension
Induction of rat hepatic aryl sulfotransferase (SULT1A1) gene expression by triamcinolone acetonide: impact on minoxidil-mediated hypotension.
Infections
Cytosolic sulfotransferase 1A1 regulates HIV-1 minus-strand DNA elongation in primary human monocyte-derived macrophages.
Infections
Influenza A virus infection activates cholesterol sulfotransferase (SULT2B1b) in the lung of female C57BL/6 mice.
Infections
Transcriptomic-based toxicological investigations of ethanol to human umbilical vein endothelial cells.
Intestinal Diseases
Elevation of hepatic sulphotransferase activities in mice with resistance to cystic fibrosis.
Leukemia
Expression of sulfotransferase SULT1A1 in cancer cells predicts susceptibility to the novel anticancer agent NSC-743380.
Leukemia
Polymorphisms in CYP1B1, CYP3A5, GSTT1, and SULT1A1 Are Associated with Early Age Acute Leukemia.
Leukemia, Myeloid, Acute
Anti-leukemia activity of NSC-743380 in SULT1A1-expressing acute myeloid leukemia cells is associated with inhibitions of cFLIP expression and PI3K/AKT/mTOR activities.
Leukemia, Myeloid, Acute
Polymorphisms in CYP1B1, CYP3A5, GSTT1, and SULT1A1 Are Associated with Early Age Acute Leukemia.
Liver Cirrhosis, Alcoholic
Downregulation of sulfotransferase expression and activity in diseased human livers.
Liver Cirrhosis, Biliary
Bile salt sulphation in man. Liver bile salt sulphotransferase activity in patients with primary biliary cirrhosis.
Liver Diseases
Bile salt sulphation in man. Liver bile salt sulphotransferase activity in patients with primary biliary cirrhosis.
Liver Diseases
Conjugation pathways in liver disease.
Liver Diseases
Elevated hepatic SULT1E1 activity in mouse models of cystic fibrosis alters the regulation of estrogen responsive proteins.
Liver Diseases
Enzymatic sulphation of bile salts in man. Bile salt sulphotransferase activity in percutaneous liver biopsy specimens from patients with liver disease.
Liver Diseases
Gestation under chronic constant light leads to extensive gene expression changes in the fetal rat liver.
Liver Diseases
Oxysterol sulfation by cytosolic sulfotransferase suppresses liver X receptor/sterol regulatory element binding protein-1c signaling pathway and reduces serum and hepatic lipids in mouse models of nonalcoholic fatty liver disease.
Liver Diseases
Reduced hepatic content of dehydroepiandrosterone sulphotransferase in chronic liver diseases.
Liver Diseases
Toxicogenomics directory of chemically exposed human hepatocytes.
Liver Neoplasms
Gel-based proteomics of liver cancer progression in rat.
Liver Neoplasms
The Interaction of Smoking with Gene Polymorphisms on Four Digestive Cancers: A Systematic Review and Meta-Analysis.
Lung Neoplasms
A functional polymorphism in the SULT1A1 gene (G638A) is associated with risk of lung cancer in relation to tobacco smoking.
Lung Neoplasms
An investigation of the relationship between SULT1A1 Arg(213)His polymorphism and lung cancer susceptibility in a Turkish population.
Lung Neoplasms
Association between Cancer Risk and Drug Metabolizing Enzyme Gene (CYP2A6, CYP2A13, CYP4B1, SULT1A1, GSTM1, and GSTT1) Polymorphisms in Japanese Cases of Lung Cancer.
Lung Neoplasms
Genetic polymorphism of Arg213His variant in the SULT1A1 gene is associated with reduced susceptibility to lung cancer in North Indian population.
Lung Neoplasms
Genetic variants of SULT1A1 and XRCC1 genes and risk of lung cancer in Bangladeshi population.
Lung Neoplasms
Impact of polymorphism in sulfotransferase gene on the risk of lung cancer.
Lung Neoplasms
Multiple analytical approaches reveal distinct gene-environment interactions in smokers and non smokers in lung cancer.
Lung Neoplasms
Potentially functional genetic variants in PLIN2, SULT2A1 and UGT1A9 genes of the ketone pathway and survival of nonsmall cell lung cancer.
Lung Neoplasms
Sulfotransferase (SULT) 1A1 polymorphism as a predisposition factor for lung cancer: a case-control analysis.
Lung Neoplasms
SULT1A1 Arg213His polymorphism and lung cancer risk: a meta-analysis.
Lymphatic Metastasis
Genetic variants of the sulfotransferase 1A1 and breast cancer risk.
Lymphatic Metastasis
Polymorphisms of estrogen-metabolizing genes and breast cancer risk: a multigenic study.
Metabolic Diseases
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases.
Migraine Disorders
Platelet 3H-imipramine binding and sulphotransferase activity in primary headache.
Migraine Disorders
Platelet sulphotransferase activity, plasma sulphate levels and sulphation capacity in patients with migraine and tension headache.
Migraine Disorders
[Platelet phenol sulfotransferase activities: a migraine marker?]
Migraine without Aura
Platelet 3H-imipramine binding and sulphotransferase activity in primary headache.
Mouth Neoplasms
Polymorphic variants of drug-metabolizing enzymes alter the risk and survival of oral cancer patients.
Mouth Neoplasms
SULT1A1 genetic polymorphisms and the association between smoking and oral cancer in a case-control study in Brazil.
Moyamoya Disease
Probing Estrogen Sulfotransferase-Mediated Inflammation with [11C]-PiB in the Living Human Brain.
Mucopolysaccharidosis III
Brain glycosaminoglycans and glycosaminoglycan sulphotransferase in Sanfilippo syndrome.
Nasal Polyps
Phenol sulfotransferase activities and localization in human nasal polyp epithelium.
Neoplasm Metastasis
Genetic variants of the sulfotransferase 1A1 and breast cancer risk.
Neoplasm Metastasis
Genomic profiling in locally advanced and inflammatory breast cancer and its link to DCE-MRI and overall survival.
Neoplasm Metastasis
Inhibition of SCAMP1 suppresses cell migration and invasion in human pancreatic and gallbladder cancer cells.
Neoplasm Metastasis
Polymorphic variants of drug-metabolizing enzymes alter the risk and survival of oral cancer patients.
Neoplasm Metastasis
Polymorphisms of estrogen-metabolizing genes and breast cancer risk: a multigenic study.
Neoplasms
Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3.
Neoplasms
Activity of sulfotransferase 1A1 is dramatically upregulated in patients with hepatocellular carcinoma secondary to chronic hepatitis B virus infection.
Neoplasms
Alterations of O-glycan biosynthesis in human colon cancer tissues.
Neoplasms
Altered expression of the hormone- and xenobiotic-metabolizing sulfotransferase enzymes 1A2 and 1C1 in malignant breast tissue.
Neoplasms
Alternative splicing events implicated in carcinogenesis and prognosis of colorectal cancer.
Neoplasms
An investigation of the relationship between SULT1A1 Arg(213)His polymorphism and lung cancer susceptibility in a Turkish population.
Neoplasms
Anti-leukemia activity of NSC-743380 in SULT1A1-expressing acute myeloid leukemia cells is associated with inhibitions of cFLIP expression and PI3K/AKT/mTOR activities.
Neoplasms
Association between Cancer Risk and Drug Metabolizing Enzyme Gene (CYP2A6, CYP2A13, CYP4B1, SULT1A1, GSTM1, and GSTT1) Polymorphisms in Japanese Cases of Lung Cancer.
Neoplasms
Association of genotypes of carcinogen-activating enzymes, phenol sulfotransferase SULT1A1 (ST1A3) and arylamine N-acetyltransferase NAT2, with urothelial cancer in a Japanese population.
Neoplasms
Association of SULT1A1 Arg²¹³His polymorphism with male breast cancer risk: results from a multicenter study in Italy.
Neoplasms
Benign cortisol-secreting adrenocortical adenomas produce small amounts of androgens.
Neoplasms
Case-control study and meta-analysis of SULT1A1 Arg213His polymorphism for gene, ethnicity and environment interaction for cancer risk.
Neoplasms
Clinical significance of the estrogen-modifying enzymes steroid sulfatase and estrogen sulfotransferase in epithelial ovarian cancer.
Neoplasms
Comparative analysis of SNP in estrogen-metabolizing enzymes for ovarian, endometrial, and breast cancers in Novosibirsk, Russia.
Neoplasms
Copy number alterations and expression profiles of candidate genes in a pulmonary inflammatory myofibroblastic tumor.
Neoplasms
Cytochrome P450 (CYP) 1A2, sulfotransferase (SULT) 1A1, and N-acetyltransferase (NAT) 2 polymorphisms and susceptibility to urothelial cancer.
Neoplasms
Double adenomas with different pathological and hormonal features in the left adrenal gland of a patient with Cushing's syndrome.
Neoplasms
Down-regulation of dehydroepiandrosterone sulfotransferase gene in human hepatocellular carcinoma.
Neoplasms
Effect of estrogen sulfation by SULT1E1 and PAPSS on the development of estrogen-dependent cancers.
Neoplasms
Epigenetic silencing of the sulfotransferase 1A1 gene by hypermethylation in breast tissue.
Neoplasms
Estrogen sulfotransferase (SULT1E1) expression in benign and malignant human bone tumors.
Neoplasms
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases.
Neoplasms
Estrogen-metabolizing gene polymorphisms in the assessment of female hormone-dependent cancer risk.
Neoplasms
Expression and prognostic value of SULT1A2 in bladder cancer.
Neoplasms
Expression of glutathione S-transferase and phenol sulfotransferase, but not of UDP-glucuronosyltransferase, in the human lung tumor cell lines NCI-H322 and NCI-H358.
Neoplasms
Expression of sulfotransferase SULT1A1 in cancer cells predicts susceptibility to the novel anticancer agent NSC-743380.
Neoplasms
Expression of sulfotransferases and sulfatases in human breast cancer: Impact on resveratrol metabolism.
Neoplasms
Further evidence for null association of phenol sulfotransferase SULT1A1 polymorphism with prostate cancer risk: a case-control study of familial prostate cancer in a Japanese population.
Neoplasms
Genetic polymorphism in the sulfotransferase SULT1A1 gene in cancer.
Neoplasms
Genetic polymorphism of estrogen metabolizing enzymes in siberian women with breast cancer.
Neoplasms
Genetic polymorphism of sulfotransferase 1A1, cigarette smoking, hazardous chemical exposure and urothelial cancer risk in a Taiwanese population.
Neoplasms
Genetic polymorphisms in human SULT1A1 and UGT1A1 genes associate with breast tumor characteristics: a case-series study.
Neoplasms
Genetic variants of the sulfotransferase 1A1 and breast cancer risk.
Neoplasms
Genomic profiling in locally advanced and inflammatory breast cancer and its link to DCE-MRI and overall survival.
Neoplasms
Human cytosolic sulfotransferase SULT1A1.
Neoplasms
Human NAD(P)H:quinone oxidoreductase 1 (NQO1) and sulfotransferase 1A1 (SULT1A1) polymorphisms and urothelial cancer risk in Taiwan.
Neoplasms
Identification and targeting of selective vulnerability rendered by tamoxifen resistance.
Neoplasms
Impact of p53 function on the sulfotransferase-mediated bioactivation of the alkylated polycyclic aromatic hydrocarbon 1-hydroxymethylpyrene in vitro.
Neoplasms
Increased estrogen sulfation of estradiol 17beta-D-glucuronide in metastatic tumor rat livers.
Neoplasms
Inhibition of phenolsulphotransferase by salicylic acid: a possible mechanism by which aspirin may reduce carcinogenesis.
Neoplasms
Intestinal carcinogenesis of two food processing contaminants, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine and 5-hydroxymethylfurfural, in transgenic FVB min mice expressing human sulfotransferases.
Neoplasms
LC-MS/MS quantification of sulfotransferases is better than conventional immunogenic methods in determining human liver SULT activities: implication in precision medicine.
Neoplasms
Meat intake and bladder cancer in a prospective study: a role for heterocyclic aromatic amines?
Neoplasms
Metabolic Enzyme Sulfotransferase 1A1 Is the Trigger for N-Benzyl Indole Carbinol Tumor Growth Suppression.
Neoplasms
Metabolism of the oral contraceptive steroids ethynylestradiol and norgestimate by normal (Huma 7) and malignant (MCF-7 and ZR-75-1) human breast cells in culture.
Neoplasms
Methylation patterns of genes coding for drug-metabolizing enzymes in tamoxifen-resistant breast cancer tissues.
Neoplasms
Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma.
Neoplasms
Pharmacogenetics of soluble sulfotransferases (SULTs).
Neoplasms
Phenol sulfotransferase SULT1A1*2 allele and enhanced risk of upper urinary tract urothelial cell carcinoma.
Neoplasms
Polymorphisms of estrogen-metabolizing genes and breast cancer risk: a multigenic study.
Neoplasms
Steroid hormones and human breast cancer. An hypothesis.
Neoplasms
Structural and Dynamic Characterizations Highlight the Deleterious Role of SULT1A1 R213H Polymorphism in Substrate Binding.
Neoplasms
Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition.
Neoplasms
Sulfotransferase 1A1 (SULT1A1) polymorphism and bladder cancer risk: a case-control study.
Neoplasms
Sulfotransferase 1A1 (SULT1A1) polymorphism and susceptibility to primary brain tumors.
Neoplasms
Sulfotransferase 1A1 as a Biomarker for Susceptibility to Carcinogenesis: From Molecular Genetics to the Role of Dietary Flavonoids.
Neoplasms
Sulfotransferase genetic variation: from cancer risk to treatment response.
Neoplasms
Sulfotransferase SULT1A1 Arg213His polymorphism with cancer risk: a meta-analysis of 53 case-control studies.
Neoplasms
SULT1A1 Arg213His polymorphism and susceptibility of environment-related cancers: a meta analysis of 5,915 cases and 7,900 controls.
Neoplasms
SULT1A1 copy number variation: ethnic distribution analysis in an Indian population.
Neoplasms
SULT1A1, CYP2C19 and disease-free survival in early breast cancer patients receiving tamoxifen.
Neoplasms
SULT1E1 inhibits cell proliferation and invasion by activating PPAR? in breast cancer.
Neoplasms
Systemic Inflammatory Protein Profiles Distinguish Irritable Bowel Syndrome (IBS) and Ulcerative Colitis, Irrespective of Inflammation or IBS-Like Symptoms.
Neoplasms
The impact of p53 function on the metabolic activation of the carcinogenic air pollutant 3-nitrobenzanthrone and its metabolites 3-aminobenzanthrone and N-hydroxy-3-aminobenzanthrone in human cells.
Neoplasms
The Interaction of Smoking with Gene Polymorphisms on Four Digestive Cancers: A Systematic Review and Meta-Analysis.
Neoplasms
The loss of phenol sulfotransferase 1 in hepatocellular carcinogenesis.
Neoplasms
The relationship among the polymorphisms of SULT1A1, 1A2 and different types of cancers in Taiwanese.
Neoplasms
The sulfatase pathway for estrogen formation: targets for the treatment and diagnosis of hormone-associated tumors.
Neoplasms
UDP-glucuronosyltransferase and sulfotransferase polymorphisms, sex hormone concentrations, and tumor receptor status in breast cancer patients.
Neoplasms
Upregulation of 24(R/S),25-epoxycholesterol and 27-hydroxycholesterol suppresses the proliferation and migration of gastric cancer cells.
Neoplasms
[A case-control study on the association between the genetic polymorphism of sulfotransferase 1A1, diet and susceptibility of colorectal cancer]
Neoplasms
[Justifying genetic and immune markers of efficiency and sensitivity under combined exposure to risk factors in mining industry workers].
Neoplasms, Multiple Primary
Case-control study and meta-analysis of SULT1A1 Arg213His polymorphism for gene, ethnicity and environment interaction for cancer risk.
Neuroblastoma
Concerted action of the cytosolic sulfotransferase, SULT1A3, and catechol-O-methyltransferase in the metabolism of dopamine in SK-N-MC human neuroblastoma cells.
Neuroblastoma
Expression profiling of sulfotransferases in human cell lines derived from extra-hepatic tissues.
Neuroblastoma
SULT4A1 Protects Against Oxidative-Stress Induced Mitochondrial Dysfunction in Neuronal Cells.
Neuroblastoma
[Sulfurtransferase activity in cultured neuronal clone cells]
Neurodegenerative Diseases
Cytosolic sulfotransferase 1A3 is induced by dopamine and protects neuronal cells from dopamine toxicity: role of D1 receptor-N-methyl-D-aspartate receptor coupling.
Neurodegenerative Diseases
Phosphorylation/dephosphorylation of human SULT4A1: Role of Erk1 and PP2A.
Neurodegenerative Diseases
Regulation of mouse brain-selective sulfotransferase sult4a1 by cAMP response element-binding protein and activating transcription factor-2.
Neuroinflammatory Diseases
Transcript analysis of laser capture microdissected white matter astrocytes and higher phenol sulfotransferase 1A1 expression during autoimmune neuroinflammation.
Neuronal Ceroid-Lipofuscinoses
Analysis of Batten disease candidate genes STP and STM.
Neuronal Ceroid-Lipofuscinoses
Mapping of two phenol sulphotransferase genes, STP and STM, to 16p: candidate genes for Batten disease.
Neuronal Ceroid-Lipofuscinoses
Phenol sulfotransferases: candidate genes for Batten disease.
Non-alcoholic Fatty Liver Disease
A case-control study on the effect of metabolic gene polymorphisms, nutrition, and their interaction on the risk of non-alcoholic fatty liver disease.
Non-alcoholic Fatty Liver Disease
Exome-wide scan identifies significant association of rs4788084 in IL27 promoter with increase in hepatic fat content among Indians.
Non-alcoholic Fatty Liver Disease
Gestation under chronic constant light leads to extensive gene expression changes in the fetal rat liver.
Non-alcoholic Fatty Liver Disease
Oxysterol sulfation by cytosolic sulfotransferase suppresses liver X receptor/sterol regulatory element binding protein-1c signaling pathway and reduces serum and hepatic lipids in mouse models of nonalcoholic fatty liver disease.
Obesity
Coding Variants are Relevant to the Expression of Obesity-Related Genes for Pediatric Adiposity.
Obesity
Many obesity-associated SNPs strongly associate with DNA methylation changes at proximal promoters and enhancers.
Obesity
Pharmacogenetics of soluble sulfotransferases (SULTs).
Osteoporosis
A Nucleotide-Gated Molecular Pore Selects Sulfotransferase Substrates.
Osteosarcoma
Analysis of Drug Metabolizing Gene Panel in Osteosarcoma Patients Identifies Association Between Variants in SULT1E1, CYP2B6 and CYP4F8 and Methotrexate Levels and Toxicities.
Osteosarcoma
Estrogen sulfotransferase (SULT1E1) expression in benign and malignant human bone tumors.
Osteosarcoma
Proteomic profiling of osteosarcoma cells identifies ALDOA and SULT1A3 as negative survival markers of human osteosarcoma.
Osteosarcoma
Thermostable (SULT1A1) and thermolabile (SULT1A3) phenol sulfotransferases in human osteosarcoma and osteoblast cells.
Ovarian Neoplasms
Clinical significance of the estrogen-modifying enzymes steroid sulfatase and estrogen sulfotransferase in epithelial ovarian cancer.
Ovarian Neoplasms
SULT1E1 and ID2 genes as candidates for inherited predisposition to breast and ovarian cancer in Jewish women.
Pancreatic Neoplasms
Genomic characteristics of pancreatic squamous cell carcinoma, an investigation by using high throughput sequencing after in-solution hybrid capture.
Pancreatic Neoplasms
Inhibition of SCAMP1 suppresses cell migration and invasion in human pancreatic and gallbladder cancer cells.
Pancreatic Neoplasms
Interaction of the cytochrome P4501A2, SULT1A1 and NAT gene polymorphisms with smoking and dietary mutagen intake in modification of the risk of pancreatic cancer.
Pheochromocytoma
Human pheochromocytoma phenol sulfotransferase: biochemical properties and activities of thermolabile and thermostable forms.
Polycystic Kidney Diseases
Decreased sulfotransferase SULT1C2 gene expression in DPT-induced polycystic kidney.
Polycystic Ovary Syndrome
Variants in SULT2A1 Affect the DHEA Sulphate to DHEA Ratio in Patients With Polycystic Ovary Syndrome But Not the Hyperandrogenic Phenotype.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Polymorphisms in CYP1B1, CYP3A5, GSTT1, and SULT1A1 Are Associated with Early Age Acute Leukemia.
Primary Ovarian Insufficiency
The significance of polymorphism and expression of oestrogen metabolism-related genes in Chinese women with premature ovarian insufficiency.
Prolactinoma
Erythrocyte catechol-O-methyltransferase, platelet monoamine oxidase, and platelet phenol sulfotransferase activities in patients with prolactin-secreting pituitary adenomas.
Prostatic Neoplasms
Association of SULT1A1 phenotype and genotype with prostate cancer risk in African-Americans and Caucasians.
Prostatic Neoplasms
Association of SULT2A1 allelic variants with plasma adrenal androgens and prostate cancer in African American men.
Prostatic Neoplasms
Further evidence for null association of phenol sulfotransferase SULT1A1 polymorphism with prostate cancer risk: a case-control study of familial prostate cancer in a Japanese population.
Prostatic Neoplasms
Inherited Variants in SULT1E1 and Response to Abiraterone Acetate by Men with Metastatic Castration Refractory Prostate Cancer.
Prostatic Neoplasms
Phenol sulphotransferase SULT1A1 polymorphism in prostate cancer: lack of association.
Prostatic Neoplasms
Sulfotransferase 1A1 Arg(213)His polymorphism and prostate cancer risk.
Prostatic Neoplasms
Transfection of human prostate cancer CA-HPV-10 cells with cytosolic sulfotransferase SULT1E1 affects estrogen signaling and gene transcription.
Pulmonary Disease, Chronic Obstructive
Alternative splicing events implicated in carcinogenesis and prognosis of colorectal cancer.
Pulmonary Edema
The proteome of Hypobaric Induced Hypoxic Lung: Insights from Temporal Proteomic Profiling for Biomarker Discovery.
Rectal Neoplasms
[A case-control study on the association between the genetic polymorphism of sulfotransferase 1A1, diet and susceptibility of colorectal cancer]
Reperfusion Injury
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases.
s-(hydroxymethyl)glutathione dehydrogenase deficiency
Use of genetically manipulated Salmonella typhimurium strains to evaluate the role of human sulfotransferases in the bioactivation of nitro- and aminotoluenes.
Sarcoma
Studies of the decrease of tyrosine-O-sulphated proteins in Rous sarcoma-virus-transformed rat embryo fibroblasts, line 3Y1. Examination of the sulphate activation and tyrosyl-protein sulphotransferase systems.
Sarcoma, Ewing
Estrogen sulfotransferase (SULT1E1) expression in benign and malignant human bone tumors.
Sepsis
Estrogen sulfotransferase in the metabolism of estrogenic drugs and in the pathogenesis of diseases.
Sjogren's Syndrome
Decreased salivary sulphotransferase activity correlated with inflammation and autoimmunity parameters in Sjogren's syndrome patients.
Squamous Cell Carcinoma of Head and Neck
A case-control study investigating the role of sulfotransferase 1A1 polymorphism in head and neck cancer.
Squamous Cell Carcinoma of Head and Neck
Sulfotransferase 1A1 haplotypes associated with oral squamous cell carcinoma susceptibility in male Taiwanese.
Stomach Neoplasms
Polymorphisms in metabolic genes, their combination and interaction with tobacco smoke and alcohol consumption and risk of gastric cancer: a case-control study in an Italian population.
Stomach Neoplasms
Sulfotransferase 1A1 polymorphism and gastric cancer risk: a pilot case-control study.
Stomach Neoplasms
The Interaction of Smoking with Gene Polymorphisms on Four Digestive Cancers: A Systematic Review and Meta-Analysis.
Stroke
Probing Estrogen Sulfotransferase-Mediated Inflammation with [11C]-PiB in the Living Human Brain.
Tension-Type Headache
Platelet 3H-imipramine binding and sulphotransferase activity in primary headache.
Tension-Type Headache
Platelet sulphotransferase activity, plasma sulphate levels and sulphation capacity in patients with migraine and tension headache.
Thrombosis
Spontaneous fetal loss caused by placental thrombosis in estrogen sulfotransferase-deficient mice.
Thyroid Diseases
Human thyroid phenol sulfotransferase enzymes 1A1 and 1A3: activities in normal and diseased thyroid glands, and inhibition by thyroid hormones and phytoestrogens.
Urinary Bladder Neoplasms
Association between the SULT1A1 Arg213His polymorphism and the risk of bladder cancer: a meta-analysis.
Urinary Bladder Neoplasms
Association of genotypes of carcinogen-metabolizing enzymes and smoking status with bladder cancer in a Japanese population.
Urinary Bladder Neoplasms
Bladder cancer risk from the perspective of genetic polymorphisms in the carcinogen metabolizing enzymes.
Urinary Bladder Neoplasms
Bladder cancer, GSTs, NAT1, NAT2, SULT1A1, XRCC1, XRCC3, XPD genetic polymorphisms and coffee consumption: a case-control study.
Urinary Bladder Neoplasms
Combined effects of NQO1 Pro187Ser or SULT1A1 Arg213His polymorphism and smoking on bladder cancer risk: Two meta-analyses.
Urinary Bladder Neoplasms
Expression and prognostic value of SULT1A2 in bladder cancer.
Urinary Bladder Neoplasms
Fruit consumption reduces the effect of smoking on bladder cancer risk. The Belgian case control study on bladder cancer.
Urinary Bladder Neoplasms
GST, NAT, SULT1A1, CYP1B1 genetic polymorphisms, interactions with environmental exposures and bladder cancer risk in a high-risk population.
Urinary Bladder Neoplasms
Sulfotransferase 1A1 (SULT1A1) polymorphism and bladder cancer risk: a case-control study.
Urinary Bladder Neoplasms
SULT1A1 Arg213His polymorphism is associated with bladder cancer risk: a meta-analysis.
Urinary Bladder Neoplasms
[Steroid and xenobiotic receptor (SXR), multidrug resistance gene (MDR1) and GSTs, SULTs and CYP polymorphism expression in invasive bladder cancer, analysis of their expression and correlation with other prognostic factors]
Urogenital Neoplasms
Case-control study and meta-analysis of SULT1A1 Arg213His polymorphism for gene, ethnicity and environment interaction for cancer risk.
Vaccinia
PXR phosphorylated at Ser350 transduces a glucose signal to repress the estrogen sulfotransferase gene in human liver cells and fasting signal in mouse livers.
Xeroderma Pigmentosum
Impact of Occupational Exposures and Genetic Polymorphisms on Recurrence and Progression of Non-Muscle-Invasive Bladder Cancer.
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Pacifici, G.M.; Franchi, M.; Giuliani, L.
Characterization of sulphotransferase in human ileum and colon
Pharmacology
38
146-150
1989
Homo sapiens
brenda
Rein, G.; Glover, V.; Sandler, M.
Multiple forms of phenolsulphotransferase in human tissues: selective inhibition by dichloronitrophenol
Biochem. Pharmacol.
31
1893-1897
1982
Homo sapiens
brenda
Roth, J.A.; Rivett, J.; Renskers, K.
Characterization of human brain phenol sulfotransferase
Phenolsulfotransferase, Ment. Health Res. (Sandler, M. , Usdin, E. Eds. ) Macmillan
London
74-85
1981
Homo sapiens
-
brenda
Weinshilboum, R.M.
Phenol sulfotransferase in humans: properties, regulation, and function
Fed. Proc.
45
2223-2228
1986
Homo sapiens
brenda
Veronese, M.E.; Burgess, W.; Zhu, X.; McManus, M.E.
Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies
Biochem. J.
302
497-502
1994
Homo sapiens
brenda
Whittemore, R.M.; Pearce, L.B.; Roth, J.A.
Purification and kinetic characterization of a phenol-sulfating form of phenol sulfotransferase from human brain
Arch. Biochem. Biophys.
249
464-471
1986
Homo sapiens
brenda
Falany, C.N.; Vazquez, M.E.; Heroux, J.A.; Roth, J.A.
Purification and characterization of human liver phenol-sulfating phenol sulfotransferase
Arch. Biochem. Biophys.
278
312-318
1990
Homo sapiens
brenda
Whittemore, R.M.; Pearce, L.B.; Roth, J.A.
Purification and kinetic characterization of a dopamine-sulfating form of phenol sulfotransferase from human brain
Biochemistry
24
2477-2482
1985
Homo sapiens
brenda
Wood, T.C.; Aksoy, I.A.; Aksoy, S.; Weinshilboum, R.M.
Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization
Biochem. Biophys. Res. Commun.
198
1119-1127
1994
Homo sapiens
brenda
Falany, C.N.; Zhuang, W.; Falany, J.L.
Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability
Chem. Biol. Interact.
92
57-66
1994
Homo sapiens
brenda
Kudlacek, P.E.; Clemens, D.L.; Anderson, R.J.
Characterization of recombinant human liver thermolabile phenol sulfotransferase with minoxidil as the substrate
Biochem. Biophys. Res. Commun.
210
363-369
1995
Homo sapiens
brenda
Ganguly, T.C.; Krasnykh, V.; Falany, C.N.
Bacterial expression and kinetic characterization of the human monoamine-sulfating form of phenol sulfotransferase
Drug Metab. Dispos.
23
945-950
1995
Homo sapiens
brenda
Hwang, S.R.; Palkovits, M.; Hook, V.Y.
High level expression and characterization of recombinant human hippocampus phenol sulfotransferase: a novel phenol-sulfating form of phenol sulfotransferase
Protein Expr. Purif.
11
125-134
1997
Homo sapiens
brenda
Dajani, R.; Hood, A.M.; Coughtrie, M.W.H.
A single amino acid, Glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3
Mol. Pharmacol.
54
942-948
1998
Homo sapiens, Homo sapiens (P50225)
brenda
Sakakibara, Y.; Yanagisawa, K.; Takami, Y.; Nakayama, T.; Suiko, M.; Liu, M.C.
Molecular cloning, expression, and functional characterization of novel mouse sulfotransferases
Biochem. Biophys. Res. Commun.
247
681-686
1998
Homo sapiens (O43704), Homo sapiens
brenda
Dajani, R.; Sharp, S.; Graham, S.; Bethell, S.S.; Cooke, R.M.; Jamieson, D.J.; Coughtrie, M.W.
Kinetic properties of human dopamine sulfotransferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: comparison with the recombinant enzyme purified from Escherichia coli
Protein Expr. Purif.
16
11-18
1999
Homo sapiens (P0DMM9), Homo sapiens
brenda
Dajani, R.; Cleasby, A.; Neu, M.; Wonacott, A.J.; Jhoti, H.; Hood, A.M.; Modi, S.; Hersey, A.; Taskinen, J.; Cooke, R.M.; Manchee, G.R.; Coughtrie, M.W.
X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity
J. Biol. Chem.
274
37862-37868
1999
Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens
brenda
Liu, M.C.; Suiko, M.; Sakakibara, Y.
Mutational analysis of the substrate binding/catalytic domains of human M form and P form phenol sulfotransferases
J. Biol. Chem.
275
13460-13464
2000
Homo sapiens
brenda
Suiko, M.; Sakakibara, Y.; Liu, M.C.
Sulfation of environmental estrogen-like chemicals by human cytosolic sulfotransferases
Biochem. Biophys. Res. Commun.
267
80-84
2000
Homo sapiens
brenda
Harris, R.M.; Waring, R.H.; Kirk, C.J.; Hughes, P.J.
Sulfation of 'estrogenic' alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases
J. Biol. Chem.
275
159-166
2000
Homo sapiens
brenda
Dubin, R.L.; Hall, C.M.; Pileri, C.L.; Kudlacek, P.E.; Li, X.Y.; Yee, J.A.; Johnson, M.L.; Anderson, R.J.
Thermostable (SULT1A1) and thermolabile (SULT1A3) phenol sulfotransferases in human osteosarcoma and osteoblast cells
Bone
28
617-624
2001
Homo sapiens
brenda
Li, X.; Clemens, D.L.; Cole, J.R.; Anderson, R.J.
Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3',5-triiodothyronine as the substrate
J. Endocrinol.
171
525-532
2001
Homo sapiens (P50225), Homo sapiens
brenda
Honma, W.; Kamiyama, Y.; Yoshinari, K.; Sasano, H.; Shimada, M.; Nagata, K.; Yamazoe, Y.
Enzymatic characterization and interspecies difference of phenol sulfotransferases, ST1A forms
Drug Metab. Dispos.
29
274-281
2001
Homo sapiens, Mus musculus, Mus musculus BALB/c, Mus musculus ST1a4, Oryctolagus cuniculus (Q9XT99), Oryctolagus cuniculus, Oryctolagus cuniculus ST1A8 (Q9XT99), Rattus norvegicus
brenda
Tabrett, C.A.; Coughtrie, M.W.
Phenol sulfotransferase 1A1 activity in human liver: kinetic properties, interindividual variation and re-evaluation of the suitability of 4-nitrophenol as a probe substrate
Biochem. Pharmacol.
66
2089-2097
2003
Homo sapiens
brenda
Pai, T.G.; Ohkimoto, K.; Sakakibara, Y.; Suiko, M.; Sugahara, T.; Liu, M.C.
Manganese stimulation and stereospecificity of the Dopa (3,4-dihydroxyphenylalanine)/tyrosine-sulfating activity of human monoamine-form phenol sulfotransferase. Kinetic studies of the mechanism using wild-type and mutant enzymes
J. Biol. Chem.
277
43813-43820
2002
Homo sapiens
brenda
Chen, G.; Chen, X.
Arginine residues in the active site of human phenol sulfotransferase (SULT1A1)
J. Biol. Chem.
278
36358-36364
2003
Homo sapiens (P50225), Homo sapiens
brenda
Yeh, C.T.; Yen, G.C.
Effects of phenolic acids on human phenolsulfotransferases in relation to their antioxidant activity
J. Agric. Food Chem.
51
1474-1479
2003
Homo sapiens
brenda
Sugahara, T.; Pai, T.G.; Suiko, M.; Sakakibara, Y.; Liu, M.C.
Differential roles of human monoamine (M)-form and simple phenol (P)-form phenol sulfotransferases in drug metabolism
J. Biochem.
133
259-262
2003
Homo sapiens
brenda
Duffel, M.W.; Marshall, A.D.; McPhie, P.; Sharma, V.; Jakoby, W.B.
Enzymatic aspects of the phenol (aryl) sulfotransferases
Drug Metab. Rev.
33
369-395
2001
Bos taurus, Homo sapiens, Homo sapiens (O00338), Homo sapiens (O43704), Homo sapiens (O75897), Mus musculus, Mus musculus (Q3UZZ6), Mus musculus (Q80VR3), Mus musculus (Q9QWG7), Rattus norvegicus, Rattus norvegicus (P50237), Rattus norvegicus (P52847), Rattus norvegicus (Q9WUW8), Rattus norvegicus (Q9WUW9), Oryctolagus cuniculus (O46503), Oryctolagus cuniculus (Q9XT99), Macaca fascicularis (P52846), Canis lupus familiaris (Q29476), Oryctolagus cuniculus ST1A8 (Q9XT99), Oryctolagus cuniculus ST1C5 (O46503), Mus musculus ST1c4 (Q80VR3), Macaca fascicularis ST1A9 (P52846), Mus musculus ST1a4
brenda
Lu, J.H.; Li, H.T.; Liu, M.C.; Zhang, J.P.; Li, M.; An, X.M.; Chang, W.R.
Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate
Biochem. Biophys. Res. Commun.
335
417-423
2005
Homo sapiens (P50225), Homo sapiens
brenda
Chen, G.
Histidine residues in human phenol sulfotransferases
Biochem. Pharmacol.
67
1355-1361
2004
Homo sapiens
brenda
Nakano, H.; Ogura, K.; Takahashi, E.; Harada, T.; Nishiyama, T.; Muro, K.; Hiratsuka, A.; Kadota, S.; Watabe, T.
Regioselective monosulfation and disulfation of the phytoestrogens daidzein and genistein by human liver sulfotransferases
Drug Metab. Pharmacokinet.
19
216-226
2004
Homo sapiens
brenda
Yeh, C.T.; Shih, P.H.; Yen, G.C.
Synergistic effect of antioxidant phenolic acids on human phenolsulfotransferase activity
J. Agric. Food Chem.
52
4139-4143
2004
Homo sapiens
brenda
Yeh, C.T.; Huang, S.M.; Yen, G.C.
Induction of phenolsulfotransferase expression by phenolic acids in human hepatoma HepG2 cells
J. Agric. Food Chem.
53
4766-4773
2005
Homo sapiens (P50225), Homo sapiens
brenda
Barnett, A.C.; Tsvetanov, S.; Gamage, N.; Martin, J.L.; Duggleby, R.G.; McManus, M.E.
Active site mutations and substrate inhibition in human sulfotransferase 1A1 and 1A3
J. Biol. Chem.
279
18799-18805
2004
Homo sapiens (P50225), Homo sapiens
brenda
Novakova, S.; Van Dyck, S.; Glatz, Z.; Van Schepdael, A.; Hoogmartens, J.
Study of enzyme kinetics of phenol sulfotransferase by electrophoretically mediated microanalysis
J. Chromatogr. A
1032
319-326
2004
Homo sapiens
brenda
Ebmeier, C.C.; Anderson, R.J.
Human thyroid phenol sulfotransferase enzymes 1A1 and 1A3: activities in normal and diseased thyroid glands, and inhibition by thyroid hormones and phytoestrogens
J. Clin. Endocrinol. Metab.
89
5597-5605
2004
Homo sapiens
brenda
Nishimuta, H.; Tsujimoto, M.; Ogura, K.; Hiratsuka, A.; Ohtani, H.; Sawada, Y.
Inhibitory effects of various beverages on ritodrine sulfation by recombinant human sulfotransferase isoforms SULT1A1 and SULT1A3
Pharm. Res.
22
1406-1410
2005
Homo sapiens
brenda
Davies, E.; Tsang, C.W.; Ghazali, A.R.; Harris, R.M.; Waring, R.H.
Effects of culture with TNF-alpha, TGF-beta and insulin on sulphotransferase (SULT 1A1 and 1A3) activity in human colon and neuronal cell lines
Toxicol. In Vitro
18
749-754
2004
Homo sapiens
brenda
Yasuda, S.; Idell, S.; Liu, M.C.
Generation and release of nitrotyrosine O-sulfate by HepG2 human hepatoma cells upon SIN-1 stimulation: identification of SULT1A3 as the enzyme responsible
Biochem. J.
401
497-503
2007
Homo sapiens (P0DMM9), Homo sapiens
brenda
Riches, Z.; Bloomer, J.C.; Coughtrie, M.W.
Comparison of 2-aminophenol and 4-nitrophenol as in vitro probe substrates for the major human hepatic sulfotransferase, SULT1A1, demonstrates improved selectivity with 2-aminophenol
Biochem. Pharmacol.
74
352-358
2007
Homo sapiens (O43704), Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens
brenda
Itaeaho, K.; Alakurtti, S.; Yli-Kauhaluoma, J.; Taskinen, J.; Coughtrie, M.W.; Kostiainen, R.
Regioselective sulfonation of dopamine by SULT1A3 in vitro provides a molecular explanation for the preponderance of dopamine-3-O-sulfate in human blood circulation
Biochem. Pharmacol.
74
504-510
2007
Homo sapiens (P0DMM9), Homo sapiens
brenda
Najmanovich, R.J.; Allali-Hassani, A.; Morris, R.J.; Dombrovsky, L.; Pan, P.W.; Vedadi, M.; Plotnikov, A.N.; Edwards, A.; Arrowsmith, C.; Thornton, J.M.
Analysis of binding site similarity, small-molecule similarity and experimental binding profiles in the human cytosolic sulfotransferase family
Bioinformatics
23
e104-e109
2007
Homo sapiens (P0DMM9), Homo sapiens
brenda
Nishimuta, H.; Ohtani, H.; Tsujimoto, M.; Ogura, K.; Hiratsuka, A.; Sawada, Y.
Inhibitory effects of various beverages on human recombinant sulfotransferase isoforms SULT1A1 and SULT1A3
Biopharm. Drug Dispos.
28
491-500
2007
Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens
brenda
Meng, L.H.; Shankavaram, U.; Chen, C.; Agama, K.; Fu, H.Q.; Gonzalez, F.J.; Weinstein, J.; Pommier, Y.
Activation of aminoflavone (NSC 686288) by a sulfotransferase is required for the antiproliferative effect of the drug and for induction of histone gamma-H2AX
Cancer Res.
66
9656-9664
2006
Homo sapiens (P50225), Homo sapiens
brenda
Wang, L.Q.; Lehmler, H.J.; Robertson, L.W.; James, M.O.
Polychlorobiphenylols are selective inhibitors of human phenol sulfotransferase 1A1 with 4-nitrophenol as a substrate
Chem. Biol. Interact.
159
235-246
2006
Homo sapiens (O43704), Homo sapiens (P50225), Homo sapiens
brenda
King, R.S.; Ghosh, A.A.; Wu, J.
Inhibition of human phenol and estrogen sulfotransferase by certain non-steroidal anti-inflammatory agents
Curr. Drug Metab.
7
745-753
2006
Homo sapiens (P50225), Homo sapiens
brenda
Ung, D.; Nagar, S.
Variable sulfation of dietary polyphenols by recombinant human sulfotransferase (SULT) 1A1 genetic variants and SULT1E1
Drug Metab. Dispos.
35
740-746
2007
Homo sapiens (P50225), Homo sapiens
brenda
Furimsky, A.M.; Green, C.E.; Hunt Sharp, L.E.; Catz, P.; Adjei, A.A.; Parman, T.; Kapetanovic, I.M.; Weinshilboum, R.M.; Iyer, L.V.
Effect of resveratrol on 17{beta}-estradiol sulfation by human hepatic and jejunal S9 and recombinant SULT1E1
Drug Metab. Dispos.
36
129-136
2008
Homo sapiens
brenda
Ohtake, E.; Kakihara, F.; Matsumoto, N.; Ozawa, S.; Ohno, Y.; Hasegawa, S.; Suzuki, H.; Kubota, T.
Frequency distribution of phenol sulfotransferase 1A1 activity in platelet cells from healthy Japanese subjects
Eur. J. Pharm. Sci.
28
272-277
2006
Homo sapiens (P50225), Homo sapiens
brenda
Hempel, N.; Gamage, N.; Martin, J.L.; McManus, M.E.
Human cytosolic sulfotransferase SULT1A1
Int. J. Biochem. Cell Biol.
39
685-689
2007
Homo sapiens (P50225), Homo sapiens
brenda
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 (P50225), Homo sapiens
brenda
Yasuda, S.; Liu, M.Y.; Suiko, M.; Sakakibara, Y.; Liu, M.C.
Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3
J. Neurochem.
103
2679-2689
2007
Homo sapiens (P0DMM9), Homo sapiens
brenda
Bian, H.S.; Ngo, S.Y.; Tan, W.; Wong, C.H.; Boelsterli, U.A.; Tan, T.M.
Induction of human sulfotransferase 1A3 (SULT1A3) by glucocorticoids
Life Sci.
81
1659-1667
2007
Homo sapiens (P0DMM9), Homo sapiens
brenda
Nagar, S.; Walther, S.; Blanchard, R.L.
Sulfotransferase (SULT) 1A1 polymorphic variants *1, *2, and *3 are associated with altered enzymatic activity, cellular phenotype, and protein degradation
Mol. Pharmacol.
69
2084-2092
2006
Homo sapiens
brenda
Nowell, S.; Falany, C.N.
Pharmacogenetics of human cytosolic sulfotransferases
Oncogene
25
1673-1678
2006
Homo sapiens (P50225)
brenda
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
-
brenda
Wang, M.; Ebmeier, C.C.; Olin, J.R.; Anderson, R.J.
Sulfation of tibolone metabolites by human postmenopausal liver and small intestinal sulfotransferases (SULTs)
Steroids
71
343-351
2006
Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens
brenda
Yasuda, S.; Idell, S.; Fu, J.; Carter, G.; Snow, R.; Liu, M.C.
Cigarette smoke toxicants as substrates and inhibitors for human cytosolic SULTs
Toxicol. Appl. Pharmacol.
221
13-20
2007
Homo sapiens (O00338), Homo sapiens (O43704), Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens (P50226), Homo sapiens (Q9BR01), Homo sapiens
brenda
Prusakiewicz, J.J.; Harville, H.M.; Zhang, Y.; Ackermann, C.; Voorman, R.L.
Parabens inhibit human skin estrogen sulfotransferase activity: possible link to paraben estrogenic effects
Toxicology
232
248-256
2007
Homo sapiens
brenda
Murias, M.; Miksits, M.; Aust, S.; Spatzenegger, M.; Thalhammer, T.; Szekeres, T.; Jaeger, W.
Metabolism of resveratrol in breast cancer cell lines: Impact of sulfotransferase 1A1 expression on cell growth inhibition
Cancer Lett.
261
172-182
2008
Homo sapiens (P50225), Homo sapiens
brenda
Senggunprai, L.; Yoshinari, K.; Yamazoe, Y.
Inhibitory effects of kynurenic acid, a tryptophan metabolite, and its derivatives on cytosolic sulfotransferases
Biochem. J.
422
455-462
2009
Mus musculus, Mus musculus (Q9QWG7), Homo sapiens (P0DMM9), Homo sapiens (P50225)
brenda
James, M.O.; Sacco, J.C.; Faux, L.R.
Effects of food natural products on the biotransformation of PCBs
Environ. Toxicol. Pharmacol.
25
211-217
2008
Homo sapiens
brenda
Saruwatari, A.; Okamura, S.; Nakajima, Y.; Narukawa, Y.; Takeda, T.; Tamura, H.
Pomegranate juice inhibits sulfoconjugation in Caco-2 human colon carcinoma cells
J. Med. Food
11
623-628
2008
Homo sapiens
brenda
Yeo, M.; Na, Y.M.; Kim, D.K.; Kim, Y.B.; Wang, H.J.; Lee, J.A.; Cheong, J.Y.; Lee, K.J.; Paik, Y.K.; Cho, S.W.
The loss of phenol sulfotransferase 1 in hepatocellular carcinogenesis
Proteomics
10
266-276
2010
Homo sapiens
brenda
Lu, L.Y.; Hsu, Y.C.; Yang, Y.S.
Spectrofluorometric assay for monoamine-preferring phenol sulfotransferase (SULT1A3)
Anal. Biochem.
404
241-243
2010
Homo sapiens
brenda
Rohn, K.J.; Cook, I.T.; Leyh, T.S.; Kadlubar, S.A.; Falany, C.N.
Potent inhibition of human sulfotransferase 1A1 by 17alpha-ethinylestradiol: role of 3-phosphoadenosine 5-phosphosulfate binding and structural rearrangements in regulating inhibition and activity
Drug Metab. Dispos.
40
1588-1595
2012
Homo sapiens
brenda
Berger, I.; Guttman, C.; Amar, D.; Zarivach, R.; Aharoni, A.
The molecular basis for the broad substrate specificity of human sulfotransferase 1A1
PLoS ONE
6
e26794
2011
Homo sapiens (P50225), Homo sapiens
brenda
Yoshinari, K.; Sakamoto, M.; Senggunprai, L.; Yamazoe, Y.
Clioquinol is sulfated by human jejunum cytosol and SULT1A3, a human-specific dopamine sulfotransferase
Toxicol. Lett.
206
229-233
2011
Homo sapiens
brenda
Yu, X.; Dhakal, I.B.; Beggs, M.; Edavana, V.K.; Williams, S.; Zhang, X.; Mercer, K.; Ning, B.; Lang, N.P.; Kadlubar, F.F.; Kadlubar, S.
Functional genetic variants in the 3-untranslated region of sulfotransferase isoform 1A1 (SULT1A1) and their effect on enzymatic activity
Toxicol. Sci.
118
391-403
2010
Homo sapiens
brenda
Wang, T.; Cook, I.; Leyh, T.S.
Isozyme specific allosteric regulation of human sulfotransferase 1A1
Biochemistry
55
4036-4046
2016
Homo sapiens
brenda
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 (P0DMM9), Homo sapiens
brenda
Bairam, A.F.; Rasool, M.I.; Alherz, F.A.; Abunnaja, M.S.; El Daibani, A.A.; Kurogi, K.; Liu, M.C.
Effects of human SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of acetaminophen and opioid drugs by the cytosolic sulfotransferase SULT1A3
Arch. Biochem. Biophys.
648
44-52
2018
Homo sapiens (P0DMM9), Homo sapiens
brenda
Arlt, V.M.; Meinl, W.; Florian, S.; Nagy, E.; Barta, F.; Thomann, M.; Mrizova, I.; Krais, A.M.; Liu, M.; Richards, M.; Mirza, A.; Kopka, K.; Phillips, D.H.; Glatt, H.; Stiborova, M.; Schmeiser, H.H.
Impact of genetic modulation of SULT1A enzymes on DNA adduct formation by aristolochic acids and 3-nitrobenzanthrone
Arch. Toxicol.
91
1957-1975
2017
Homo sapiens (P50225), Homo sapiens (P50226), Homo sapiens
brenda
Chevereau, M.; Glatt, H.; Zalko, D.; Cravedi, J.P.; Audebert, M.
Role of human sulfotransferase 1A1 and N-acetyltransferase 2 in the metabolic activation of 16 heterocyclic amines and related heterocyclics to genotoxicants in recombinant V79 cells
Arch. Toxicol.
91
3175-3184
2017
Homo sapiens (P50225), Homo sapiens
brenda
Tibbs, Z.; Falany, C.
An engineered heterodimeric model to investigate SULT1B1 dependence on intersubunit communication
Biochem. Pharmacol.
115
123-133
2016
Homo sapiens (O43704)
brenda
Yamamoto, A.; Kurogi, K.; Schiefer, I.T.; Liu, M.Y.; Sakakibara, Y.; Suiko, M.; Liu, M.C.
Human cytosolic sulfotransferase SULT1A3 mediates the sulfation of dextrorphan
Biol. Pharm. Bull.
39
1432-1436
2016
Homo sapiens (P0DMM9), Homo sapiens
brenda
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 (Q9BR01), Homo sapiens
brenda
Hashimoto, K.; Zaitseva, I.N.; Bonala, R.; Attaluri, S.; Ozga, K.; Iden, C.R.; Johnson, F.; Moriya, M.; Grollman, A.P.; Sidorenko, V.S.
Sulfotransferase-1A1-dependent bioactivation of aristolochic acid I and N-hydroxyaristolactam I in human cells
Carcinogenesis
37
647-655
2016
Homo sapiens (P50225), Homo sapiens
brenda
Idris, M.; Mitchell, D.J.; Gordon, R.; Sidharthan, N.P.; Butcher, N.J.; Minchin, R.F.
Interaction of the brain-selective sulfotransferase SULT4A1 with other cytosolic sulfotransferases effects on protein expression and function
Drug Metab. Dispos.
48
337-344
2020
Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens (Q9BR01), Homo sapiens
brenda
Yoshitake, S.; McKay-Daily, M.; Tanaka, M.; Huang, Z.
Quantification of sulfotransferases 1A1 and 1A3/4 in tissue Fractions and cell lines by multiple reaction monitoring mass spectrometry
Drug Metab. Lett.
11
35-47
2017
Homo sapiens (P0DMM9), Homo sapiens (P0DMN0), Homo sapiens (P50225), Homo sapiens
brenda
Luo, L.; Zhou, C.; Hui, Y.; Kurogi, K.; Sakakibara, Y.; Suiko, M.; Liu, M.C.
Human cytosolic sulfotransferase SULT1C4 mediates the sulfation of doxorubicin and epirubicin
Drug Metab. Pharmacokinet.
31
163-166
2016
Homo sapiens (O75897), Homo sapiens
brenda
Wang, T.; Cook, I.; Leyh, T.S.
The NSAID allosteric site of human cytosolic sulfotransferases
J. Biol. Chem.
292
20305-20312
2017
Homo sapiens (P50225), Homo sapiens
brenda
Shimohira, T.; Kurogi, K.; Hashiguchi, T.; Liu, M.C.; Suiko, M.; Sakakibara, Y.
Regioselective production of sulfated polyphenols using human cytosolic sulfotransferase-expressing Escherichia coli cells
J. Biosci. Bioeng.
124
84-90
2017
Homo sapiens (O75897), Homo sapiens (P0DMM9), Homo sapiens
brenda
Jia, C.; Luo, L.; Kurogi, K.; Yu, J.; Zhou, C.; Liu, M.-C.
Identification of the human SULT enzymes involved in the metabolism of rotigotine
J. Clin. Pharmacol.
56
754-760
2016
Homo sapiens (O75897), Homo sapiens (P0DMM9), Homo sapiens (P50225), Homo sapiens (P50226), Homo sapiens
brenda
Cook, I.; Wang, T.; Girvin, M.; Leyh, T.S.
The structure of the catechin-binding site of human sulfotransferase 1A1
Proc. Natl. Acad. Sci. USA
113
14312-14317
2016
Homo sapiens (P50225), Homo sapiens
brenda