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Information on EC 2.8.2.1 - aryl sulfotransferase and Organism(s) Homo sapiens and UniProt Accession O75897

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.2 Sulfotransferases
                2.8.2.1 aryl sulfotransferase
IUBMB Comments
A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: O75897
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sult1a1, sult2a1, sult1e1, sulphotransferase, sult1a3, phenol sulfotransferase, cytosolic sulfotransferase, sult4a1, sult1b1, sult1a2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-naphthol phenol sulfotransferase
-
-
-
-
2-naphtholsulfotransferase
-
-
-
-
4-nitrocatechol sulfokinase
-
-
-
-
arylsulfotransferase
-
-
-
-
ASTIV
-
-
-
-
catecholamine-sulfating phenol sulfotransferase
-
-
-
-
cytosolic sulfotransferase
DOPA/tyrosine sulfotransferase
-
-
-
-
dopamine sulfotransferase
H-PST
-
i.e. hippocampal phenol sulfotransferase
HAST1/HAST2
-
-
-
-
HAST3
-
-
-
-
hippocampal phenol sulfotransferase
-
-
-
-
M-PST
minoxidil sulfotransferase
-
-
-
-
monoamine sulfotransferase
-
-
-
-
monoamine-form phenol sulfotransferase
-
-
neuronal SULT
-
p-nitrophenol sulfotransferase
-
-
-
-
P-PST
PAPS-sulfotransferase
-
-
phenol sulfokinase
-
-
-
-
phenol sulfotransferase
phenol sulfotransferase 1
-
-
phenol sulfotransferase 1A1
phenol sulfotransferase 1A3
-
-
phenol/aryl sulfotransferase
-
-
-
-
Pst
-
-
-
-
PST-P
-
-
ritodrine sulfotransferase
-
-
-
-
ST1A2
-
-
-
-
ST1A3
-
-
-
-
ST1A4
-
-
-
-
sulfokinase
-
-
-
-
sulfotransferase
-
-
sulfotransferase 1A1
sulfotransferase 1A3
sulfotransferase, aryl
-
-
-
-
sulfotransferase, monoamine-preferring
-
-
-
-
sulphotransferase
-
SULT1A1
SULT1A1*2
-
-
SULT1A2
SULT1A3
SULT1B1
SULT1C1
-
-
SULT1C2
-
-
SULT1C3
-
-
SULT1E1
-
-
SULT2A1
-
-
SULT4A1
thermolabile phenol sulfotransferase
-
-
-
-
thermostable phenol sulfotransferase
-
-
-
-
TL-PST
-
-
-
-
TS-PST
-
-
-
-
tyrosine-ester sulfotransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
mechanism
3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:phenol sulfotransferase
A number of aromatic compounds can act as acceptors. Organic hydroxylamines are not substrates (cf. EC 2.8.2.9 tyrosine-ester sulfotransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
9026-09-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
-
-
r
3'-phosphoadenylyl sulfate + doxorubicin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + epirubicin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + rotigotine
adenosine 3',5'-bisphosphate + rotigotine 1-O-sulfate
show the reaction diagram
i.e. (6S)-6-[propyl[2-(thiophen-2-yl)ethyl]amino]-5,6,7,8-tetrahydronaphthalen-1-ol, non-ergoline dopamine agonist
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
show the reaction diagram
SULT1C2
-
-
?
2 3'-phosphoadenylyl sulfate + 2 dopamine
2 adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + dopamine 4-O-sulfate
show the reaction diagram
SULT1A3
NMR product structure analysis, dopamine 3-O-sulfate is the main product, overview
-
?
3'-phosphoadenosine 5'-phosphosulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 1-hydroxypyrene
adenosine 3',5'-bisphosphate + 1-hydroxypyrene sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 17alpha-ethinylestradiol
?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
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
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2,3,5,5',6-pentachlorobiphenyl-4'-yl
adenosine 3',5'-bisphosphate + 2,2',3,3',5'-pentachlorobiphenyl-4'-yl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2,6-dichloro-4-nitrophenol
adenosine 3',5'-bisphosphate + 2,6-dichloro-4-nitrophenyl sulfate
show the reaction diagram
low activity, inhibitory
-
-
?
3'-phosphoadenylyl sulfate + 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2-amino-3-methyl-9H-pyrido[2,3-b]indole
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2-amino-9H-pyrido[2,3-b]indole
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2-aminophenol
adenosine 3',5'-bisphosphate + 2-aminophenyl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 2-methoxyestradiol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 3',4',5-trichlorobiphenyl-2-yl
adenosine 3',5'-bisphosphate + 3',4',5-trichlorobiphenyl-2-yl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3-amino-1-methyl-5H-pyrido[4,3-b]indole
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3-cyano-7-hydroxycoumarin
?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3-nitro-L-tyrosine
adenosine 3',5'-bisphosphate + 3-nitro-O-sulfo-L-tyrosine
show the reaction diagram
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
show the reaction diagram
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 + 3-nitrobenzanthrone
adenosine 3',5'-bisphosphate + N-sulfoxy-3-aminobenzanthrone
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3alpha-hydroxytibolone
adenosine 3',5'-bisphosphate + 3alpha-sulfooxytibolone O-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 3beta-hydroxytibolone
adenosine 3',5'-bisphosphate + 3beta-sulfooxytibolone O-sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 4-chlorobiphenyl-3'-ol
adenosine 3',5'-bisphosphate + 4'-chlorobiphenyl-3-yl sulfate
show the reaction diagram
low activity
-
-
?
3'-phosphoadenylyl sulfate + 4-chlorobiphenyl-4'-ol
adenosine 3',5'-bisphosphate + 4'-chlorobiphenyl-4-yl sulfate
show the reaction diagram
low activity
-
-
?
3'-phosphoadenylyl sulfate + 4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + 4-(sulfooxy)tamoxifen
show the reaction diagram
3'-phosphoadenylyl sulfate + 4-methylumbelliferone
adenosine 3',5'-bisphosphate + 4-methylumbelliferyl sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 5-amino-2-(4-amino-3-fluorophenyl)-6,8-difluoro-7-methyl-4H-1-benzopyran-4-one
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + 5-chloro-7-iodo-8-quinolinol
adenosine 3',5'-bisphosphate + 5-chloro-7-iodo-8-quinolinyl sulfate
show the reaction diagram
-
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 + ?
show the reaction diagram
i.e. proluciferin substrate UGT-Glo substrate A, GSA
-
-
?
3'-phosphoadenylyl sulfate + 6-hydroxydopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + 7-hydroxyserotonin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + 7-methylimidazo[1,2-a:5,4-b']dipyridin-2-amine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 9-(4'-aminophenyl)-9H-pyrido[3,4-b]indole
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + acetaminophen
adenosine 3',5'-bisphosphate + 4-(acetylamino)phenylsulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + acetaminophen
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + apigenin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + beta-estradiol
adenosine 3',5'-bisphosphate + beta-estradiol 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + butylparaben
adenosine 3',5'-bisphosphate + butylparaben sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + catechol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + chrysin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
substrate of allozyme SULT1A1*1
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + dextrorphan
adenosine 3',5'-bisphosphate + dextrorphan sulfate
show the reaction diagram
i.e. active metabolite of the antitussive dextromethorphan
-
-
?
3'-phosphoadenylyl sulfate + DL-3-hydroxyphenylalanine
adenosine 3',5'-bisphosphate + DL-3-(sulfooxy)phenylalanine
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopaminyl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + epicatechin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + epigallocatechin gallate
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol sulfate
show the reaction diagram
-
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 + ?
show the reaction diagram
as fenoterol hydrobromide
-
-
?
3'-phosphoadenylyl sulfate + genistein
adenosine 3',5'-bisphosphate + genistein 4'-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + imidazo[1,2-a:5,4-b']dipyridin-2-amine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + isoproterenol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
as isoproterenol hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + isoproterenol
adenosine 3',5'-bisphosphate + isoproterenol sulfate
show the reaction diagram
as isoproterenol hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + L-DOPA
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + L-triiodothyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + L-tyrosine
adenosine 3',5'-bisphosphate + O-sulfo-L-tyrosine
show the reaction diagram
low activity
-
-
?
3'-phosphoadenylyl sulfate + minoxidil
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + morphine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
show the reaction diagram
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl-4-amine
show the reaction diagram
SULT1C*2
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxyaristolactam I
adenosine 3',5'-bisphosphate + N-hydroxyaristolactam I sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + O-desmethyl tramadol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + p-nitrophenol
adenosine 3',5'-bisphosphate + p-nitrophenyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + pentachlorophenol
adenosine 3',5'-bisphosphate + pentachlorophenyl sulfate
show the reaction diagram
low activity, inhibitory
-
-
?
3'-phosphoadenylyl sulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + quercetin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
allozyme SULT1A1*1
-
-
?
3'-phosphoadenylyl sulfate + resveratrol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + resveratrol
adenosine 3',5'-bisphosphate + trans-resveratrol-3-O sulfate
show the reaction diagram
3,4',5-trihydroxy-trans-stilbene
-
-
?
3'-phosphoadenylyl sulfate + ritodrine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
as ritodrine hydrochloride
-
-
?
3'-phosphoadenylyl sulfate + rotigotine
adenosine 3',5'-bisphosphate + rotigotine 1-O-sulfate
show the reaction diagram
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 + ?
show the reaction diagram
as salbutamol hemisulfate
-
-
?
3'-phosphoadenylyl sulfate + serotonin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + tapentadol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + terbutaline
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
as terbutaline hemisulfate
-
-
?
3'-phosphoadenylyl sulfate + trans-4-hydroxytamoxifen
adenosine 3',5'-bisphosphate + trans-4-(sulfooxy)tamoxifen
show the reaction diagram
substrate of the allozymes SULT1A1*2 and SULT1A1*1
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + (+/-)isoproterenol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + (+/-)metoprolol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + (+/-)salbutamol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + (+/-)sotalol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 2-amino-4'-hydroxy-1-methyl-6-phenylimidazo[4,5-b]pyridine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 2-ethylphenol
adenosine 3',5'-bisphosphate + 2-ethylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 2-methylphenol
adenosine 3',5'-bisphosphate + 2-methylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthylsulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 3,3',5'-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 3,3',5-triiodo-D-thyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 3,3',5-triiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 3,3'-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 3,4-dihydroxyphenylacetate
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 3,5-diiodo-L-thyronine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 3-ethylphenol
adenosine 3',5'-bisphosphate + 3-ethylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 3-hydroxybenzo[a]pyrene
adenosine 3',5'-bisphosphate + benzo[a]pyrene 3-sulfate
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 3-methylphenol
adenosine 3',5'-bisphosphate + 3-methylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-chlorocatechol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 4-chlorophenol
adenosine 3',5'-bisphosphate + 4-chlorophenyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 4-ethylphenol
adenosine 3',5'-bisphosphate + 4-ethylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-hydroxy-3-methoxyphenylglycol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 4-isopropylcatechol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 4-methoxytyramine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + 4-methylcatechol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 4-methylphenol
adenosine 3',5'-bisphosphate + 4-methylphenyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 4-methylumbelliferone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + 4-n-amylphenol
adenosine 3',5'-bisphosphate + 4-n-amylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-n-butylphenol
adenosine 3',5'-bisphosphate + 4-n-butylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-n-propylphenol
adenosine 3',5'-bisphosphate + 4-n-propylphenyl sulfate
show the reaction diagram
-
SULT1A1/2
-
-
?
3'-phosphoadenylylsulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 4-nonylphenol
adenosine 3',5'-bisphosphate + 4-nonylphenyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 4-octylphenol
adenosine 3',5'-bisphosphate + 4-octylphenyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + 5,7-dihydroxyflavanone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 5-(hydroxyphenyl)-5-(p-tolyl)-hydantoin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 5-hydroxyindole
adenosine 3',5'-bisphosphate + 5-indoxyl sulfate
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 5-hydroxytryptophol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + 6-hydroxymelatonin
adenosine 3',5'-bisphosphate + melatonin 6-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + acebutolol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + acetaminophen
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
M-PST and P-PST
-
-
?
3'-phosphoadenylylsulfate + benzyl alcohol
adenosine 3',5'-bisphosphate + benzyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + beta-estradiol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + bisphenol A
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + bupivacaine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + catechol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + D-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + D-tyrosine
adenosine 3',5'-bisphosphate + D-tyrosyl sulfate
show the reaction diagram
M-PST
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 4'-sulfate
show the reaction diagram
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + daidzein
adenosine 3',5'-bisphosphate + daidzein 7-sulfate + daidzein 4'-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + daidzein 4'-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
show the reaction diagram
3'-phosphoadenylylsulfate + daidzein 7-sulfate
adenosine 3',5'-bisphosphate + daidzein 4',7-disulfate
show the reaction diagram
3'-phosphoadenylylsulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + dexamethasone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + DL-propanolol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST, not M-PST
-
-
?
3'-phosphoadenylylsulfate + DL-tyrosine
adenosine 3',5'-bisphosphate + DL-tyrosyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + dobutamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + epinephrine
adenosine 3',5'-bisphosphate + epinephrine sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 4'-sulfate
show the reaction diagram
-
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + genistein
adenosine 3',5'-bisphosphate + genistein 7-sulfate + genistein 4'-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + genistein 4'-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
show the reaction diagram
3'-phosphoadenylylsulfate + genistein 7-sulfate
adenosine 3',5'-bisphosphate + genistein 4',7-disulfate
show the reaction diagram
3'-phosphoadenylylsulfate + harmol
adenosine 3',5'-bisphosphate + harmol sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + L-3,4-dihydroxyphenylalanine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + L-thyroxine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + L-tyrosine
adenosine 3',5'-bisphosphate + L-tyrosyl O4-sulfate
show the reaction diagram
M-PST
-
-
?
3'-phosphoadenylylsulfate + lidocaine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
P-PST and M-PST
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + naringenin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + norepinephrine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
enzyme form SULT1A3
-
-
?
3'-phosphoadenylylsulfate + norepinephrine
adenosine 3',5'-bisphosphate + norepinephrine sulfate
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + normetanephrine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + phentolamine
adenosine 3',5'-bisphosphate + phentolamine sulfate
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + ritodrine
adenosine 3',5'-bisphosphate + ritodrine sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + sakuranetin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + salicylamide
adenosine 3',5'-bisphosphate + 2-sulfooxybenzamide
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
3'-phosphoadenylylsulfate + serotonin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylylsulfate + troglitazone
adenosine 3',5'-bisphosphate + troglitazone sulfate
show the reaction diagram
-
ST1A3, not ST1A5
-
-
?
3'-phosphoadenylylsulfate + tyramine
adenosine 3',5'-bisphosphate + tyramine O-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + tyrosylglycine
?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylylsulfate + umbelliferone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
ST1A3 and ST1A5
-
-
?
adenosine 3',5'-bisphosphate + 4-methylumbelliferyl sulfate
3'-phosphoadenylyl sulfate + 4-methylumbelliferone
show the reaction diagram
-
-
-
-
r
adenosine 3',5'-bisphosphate + dopamine sulfate
3'-phosphoadenylyl sulfate + dopamine
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 3'-phosphoadenylyl sulfate + 2 dopamine
2 adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + dopamine 4-O-sulfate
show the reaction diagram
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 17alpha-ethinylestradiol
?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
?
show the reaction diagram
-
-
-
-
?
3'-phosphoadenylyl sulfate + 17beta-estradiol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2-methoxyestradiol
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 2-naphthylamine
adenosine 3',5'-bisphosphate + 2-naphthylamine sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3,4-dihydroxyphenylacetic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + 3-nitro-L-tyrosine
adenosine 3',5'-bisphosphate + 3-nitro-O4-sulfo-L-tyrosine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
a potent inducer of apoptosis in breast tumor cell lines
-
-
?
3'-phosphoadenylyl sulfate + 4-nitrophenol
adenosine 3',5'-bisphosphate + 4-nitrophenyl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + 5-amino-2-(4-amino-3-fluorophenyl)-6,8-difluoro-7-methyl-4H-1-benzopyran-4-one
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
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
show the reaction diagram
-
isoform SULT1A3 is responsible for the 5-chloro-7-iodo-8-quinolinol sulfation in human jejunum
-
-
?
3'-phosphoadenylyl sulfate + 6-hydroxydopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + 7-hydroxyserotonin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
3'-phosphoadenylyl sulfate + acetaminophen
adenosine 3',5'-bisphosphate + 4-(acetylamino)phenylsulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + aristolochic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
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
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + caffeic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + dehydroepiandrosterone
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + desipramine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopamine sulfate
show the reaction diagram
-
-
-
-
r
3'-phosphoadenylyl sulfate + dopamine
adenosine 3',5'-bisphosphate + dopaminyl sulfate
show the reaction diagram
-
specific substrate for isoform SULT1A3
-
-
?
3'-phosphoadenylyl sulfate + estradiol
adenosine 3',5'-bisphosphate + estradiol sulfate
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + minoxidil
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + N-hydroxy-4-aminobiphenyl
adenosine 3',5'-bisphosphate + N-(sulfooxy)biphenyl 4-amine
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + phenol
adenosine 3',5'-bisphosphate + phenyl sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + serotonin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylyl sulfate + xanthurenic acid
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + dopamine
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
accounts for approximately 10% of the enzymic activity directed towards catabolism of dopamine
-
-
?
3'-phosphoadenylylsulfate + minoxidil
adenosine 3',5'-bisphosphate + minoxidil sulfate
show the reaction diagram
adenosine 3',5'-bisphosphate + dopamine sulfate
3'-phosphoadenylyl sulfate + dopamine
show the reaction diagram
-
-
-
-
r
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
activates
NaCl
activates
additional information
-
no effect: Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-catechin
-
(-)-epicatechin
(-)-epicatechin gallate
(-)-epigallocatechin
(-)-epigallocatechin gallate
1-hydroxy-4-ethylbenzene
-
-
17alpha-ethinylestradiol
-
potent inhibitor, 17alpha-ethinylestradiol binds and inhibits isoform SULT1A1 activity toward 4-nitrophenol and 2-naphthol at low nanomolar concentrations, whereas the compound is not sulfated until significantly higher concentrations are reached
2,3',4,6-tetrachlorobiphenyl-4'-ol
i.e. 4'-OH-CB69
2,3,3',5,5',6-hexachlorobiphenyl-4'-ol
i.e. 4'-OH-CB165, a mixed, noncompetitive-uncompetitive inhibitor
2,3,3',5,6-pentachlorobiphenyl-4'-ol
i.e. 4'-OH-CB112
2,3-Butanedione
2,6-Dichloro-4-nitrophenol
2,6-dichloro-4-nitrophenyl phosphate
i.e. DCNP
2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
mixed competitive-noncompetitive type inhibition of SULT1A1 versus 17beta-estradiol
2-Aminophenol
substrate inhibition of SULT1A1
2-Ethylphenol
-
inhibits SULT1A1/2 and SULT1A3
2-n-propylphenol
-
inhibits SULT1A1/2, but not SULT1A3
2-sec-Butylphenol
-
inhibits SULT1A1/2, but not SULT1A3
2-sec-propylphenol
-
inhibits SULT1A1/2 and SULT1A3
2-tert-butylphenol
-
inhibits SULT1A1/2, but not SULT1A3
3',4,5'-trichlorobiphenyl-4'-ol
i.e. 4'-OH-CB39
3'-phosphoadenylylsulfate
-
substrate inhibition
3,3',4-trichlorobiphenyl-6'-ol
i.e. 6'-OH-CB35
3,3',5',6-tetrachlorobiphenyl-4'-ol
i.e. 4'-OH-CB72
3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide
-
DBHM
3,5-dibromo-4-hydroxybenzoic acid (6,8-dichloro-4-oxo-4H-chromen-3-ylmethylene) hydrazide
-
DBHD
4-aminobiphenyl
i.e. 4-ABP, mixed competitive-noncompetitive type inhibition of SULT1A1 versus 17beta-estradiol
4-chlorobiphenyl-3'-ol
i.e. 3'-OH-CB3, inhibitory effects on different SULT1A1 genotypes, overview
4-chlorobiphenyl-4'-ol
i.e. 4'-OH-CB3
4-n-amylphenol
-
inhibits SULT1A1/2, but not SULT1A3
4-n-heptylphenol
-
inhibits SULT1A1/2, but not SULT1A3
4-n-nonylphenol
-
inhibits SULT1A1/2, but not SULT1A3
4-n-octylphenol
-
inhibits SULT1A1/2, but not SULT1A3
4-nitrophenol
5,7-dichlorokynurenic acid
-
5-chloro-7-iodo-8-quinolinol
-
inhibits isoform SULT1A3-mediated sulfation of dopamine in a dose-dependent manner
6',7'-dihydroxybergamottin
6-Hydroxydopamine
competiitve versus dopamine, complete inhibition at about 1 mM
7-hydroxyserotonin
competitive versus serotonin, complete inhibition at about 1 mM
Acetylsalicylate
binds near enough to the substrate site to prevent catalysis but does not affect dissociation of the substrate-enzyme complex
Acetylsalicylic acid
-
adenosine 3',5'-bisphosphate
adenosine 5'-(beta,gamma-imido) triphosphate
-
i.e. AMP-PNP, a non-hydrolysable ATP analogue
apigenin
antagonizes aminoflavone by inhibiting SULT1A1
bergamottin
caffeic acid
-
inhibition of P-PST and M-PST
chlorogenic acid
-
inhibition of P-PST and M-PST
Cu2+
-
M-PST and P-PST, strong inhibition
daidzein
diethyldicarbonate
-
His108 is critical for activity
dopamine
dopamine 3-O-sulfate
35-85% product inhibition of SULT1A3
dopamine 4-O-sulfate
40-80% product inhibition of SULT1A3
epigallocatechin gallate
-
highly specific inhibitor of isoform SULT1A1
Fe2+
-
M-PST, not P-PST
gavestinel
i.e. 4,6-dichloro-3-[(1E)-3-oxo-3-(phenylamino)-1-propenyl]-1H-indole-2-carboxylic acid sodium salt
genistein
Hg2+
-
M-PST and P-PST, strong inhibition
Ibuprofen
-
indomethacin
-
Kynurenic acid
-
L689,560
i.e. trans-2-carboxy-5,7-dichloro-4-phenylaminocarboxylamino-1,2,3,4-tetrahydroquinoline
L701,324
i.e. 7-chloro-4-hydroxy-3(3-phenoxy)phenyl-2(H)-quinolinone
meclofenamate
binds near enough to the substrate site to prevent catalysis but does not affect dissociation of the substrate-enzyme complex
Mefenamic acid
N-Hydroxy-4-aminobiphenyl
i.e. N-OH-4-ABP, mixed competitive-noncompetitive type inhibition of SULT1A1 versus 17beta-estradiol
naringenin
naringin
inhibition of SULT1A3
nimesulide
binds near enough to the substrate site to prevent catalysis but not affect dissociation of the substrate-enzyme complex
nobiletin
Pentachlorophenol
Phenylglyoxal
-
-
piroxicam
-
protocatechuic acid
-
inhibition of P-PST and M-PST
punicalagin
-
-
pyridoxal 5'-phosphate
-
a competitive inhibitor for sulfotransferases
quercetin
resveratrol
substrate inhibition
salicylate
-
Sinapic acid
-
inhibition of P-PST and M-PST
syringic acid
-
inhibition of P-PST and M-PST
tangeretin
theaflavin
thearubigin
vanillic acid
-
inhibition of P-PST and M-PST
Zn2+
-
P-PST and M-PST
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ferulic acid
-
activation of M-PST
gallic acid
-
activation of P-PST and M-PST
gentisic acid
-
activation of P-PST and M-PST
m-coumaric acid
-
activation of P-PST
morpholinosydnonimine
i.e. SIN-1, a peroxynitrite generator, activates SULT1A3 in vivo in Hep-G2 cells
o-coumaric acid
-
activation of P-PST
p-coumaric acid
-
activation of P-PST
p-hydroxybenzoic acid
-
activation of P-PST and M-PST
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1191
rotigotine
pH 7.0, 37°C
0.000022
1-hydroxypyrene
wild-type, initial rate value, pH 7.5, 25°C
0.00099
1-naphthol
isoform Sult1a1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C
0.0024
17beta-estradiol
-
pH not specified in the publication, at 37°C
0.009 - 0.223
2-Aminophenol
0.00158 - 0.00388
3'-phosphoadenylyl sulfate
0.00035 - 0.51
3'-phosphoadenylylsulfate
0.036 - 0.05
3,3',5'-triiodo-L-thyronine
0.084 - 0.126
3,3',5-triiodo-L-thyronine
0.00051 - 0.00063
3,3'-diiodo-L-thyronine
0.02
3-cyano-7-hydroxycoumarin
wild type enzyme, in 50 mM HEPES, pH 7.5, 7 mM MgCl2, and 1.5 mM dithiothreitol, at 22°C
0.1305 - 0.1641
3-nitro-L-tyrosine
0.00018
3alpha-tibolone
pH 7.5, 37°C, postmenopausal liver enzyme
0.00042
3beta-tibolone
pH 7.5, 37°C, postmenopausal liver enzyme
0.00036 - 1.47
4-nitrophenol
0.019
6-Hydroxydopamine
pH 7.0, 37°C, SULT1A3
0.018 - 0.065
6-hydroxymelatonin
0.04
7-hydroxyserotonin
pH 7.0, 37°C, SULT1A3
0.43 - 4.5
acetaminophen
0.00172 - 0.00264
apigenin
0.0026
beta-estradiol
isoform Sult1a1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C
0.0025
chrysin
pH 6.5, 37°C, allozyme SULT1A1*1
0.00047 - 0.407
daidzein
0.0443 - 0.0516
daidzein 4'-sulfate
0.0435 - 0.0699
daidzein 7-sulfate
0.015
dobutamine
-
M-PST, pH 7.0, 37°C
0.00065 - 11.3
dopamine
0.065 - 0.419
epicatechin
0.00051 - 0.371
genistein
0.0114 - 0.0266
genistein 4'-sulfate
0.03 - 0.0316
genistein 7-sulfate
0.101 - 0.208
L-thyroxine
0.2
minoxidil
-
P-PST, pH 7.0, 37°C
3.8 - 10
morphine
0.27 - 0.8
O-desmethyl tramadol
-
0.0351
quercetin
pH 6.5, 37°C, allozyme SULT1A1*1
0.0005 - 0.0023
resveratrol
0.438 - 3.08
ritodrine
0.0291 - 0.0807
rotigotine
0.133
serotonin
pH 7.0, 37°C, SULT1A3
0.09 - 0.84
tapentadol
-
0.0066 - 0.0161
trans-resveratrol-3-O sulfate
0.833
tyrosylglycine
-
pH 8.5
0.0433
xanthurenic acid
isoform Sult1a1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
1-hydroxypyrene
wild-type, initial rate value, pH 7.5, 25°C
0.00033 - 0.1065
daidzein
0.00183 - 0.063
daidzein 4'-sulfate
0.00016 - 0.076
daidzein 7-sulfate
0.0015 - 0.124
genistein
0.0067 - 0.035
genistein 4'-sulfate
0.00116 - 0.06
genistein 7-sulfate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.149 - 1.2
3-cyano-7-hydroxycoumarin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0123
1-hydroxy-4-ethylbenzene
-
SULT1A1/2, pH 7.0, 37°C
0.0000089 - 0.000019
17alpha-ethinylestradiol
0.0018
2,3,3',5,5',6-hexachlorobiphenyl-4'-ol
pH 7.0, 37°C, SULT1A1
0.108
2-Aminophenol
SULT1A1, pH 7.4, 37°C
0.00035
3'-phosphoadenylylsulfate
-
P-PST, pH 8.5
0.0151
4-n-amylphenol
-
SULT1A1/2, pH 7.0, 37°C
0.0052 - 0.034
4-nitrophenol
0.0014 - 0.0024
Acetylsalicylate
0.00026 - 0.00751
Acetylsalicylic acid
0.00007
adenosine 3',5'-bisphosphate
-
M-PST, pH 7.0, 37°C
0.18
ATP
-
M-PST, pH 7.0, 37°C
0.174
dopamine
-
at pH 7.0 and 37°C
0.000045 - 0.000056
meclofenamate
0.000027 - 0.000148
Mefenamic acid
0.00071 - 0.00099
nimesulide
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00101 - 0.1
2,3',4,6-tetrachlorobiphenyl-4'-ol
0.00051 - 0.1
2,3,3',5,5',6-hexachlorobiphenyl-4'-ol
0.00054 - 0.1
2,3,3',5,6-pentachlorobiphenyl-4'-ol
0.00017 - 0.52
2,6-Dichloro-4-nitrophenol
0.00196 - 0.1
3',4,5'-trichlorobiphenyl-4'-ol
0.0117 - 0.0351
3,3',4-trichlorobiphenyl-6'-ol
0.00041 - 0.1
3,3',5',6-tetrachlorobiphenyl-4'-ol
0.00026 - 0.0082
4-chlorobiphenyl-3'-ol
0.0062 - 0.1
4-chlorobiphenyl-4'-ol
0.0137 - 0.0208
5,7-dichlorokynurenic acid
0.0279
5-chloro-7-iodo-8-quinolinol
Homo sapiens
-
using dopamine as substrate, in 0.1 M potassium phosphate buffer (pH 7.4), 1 mM dithiothreitol, 5 mM MgCl2, at 37°C
1.3
Acetylsalicylate
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
0.0106 - 146
gavestinel
1.9
Ibuprofen
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
0.0188 - 0.022
Kynurenic acid
0.117 - 0.25
L689,560
0.00011
meclofenamate
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
0.0149 - 0.0304
Mefenamic acid
62.5 - 178.7
NaCl
1.7
naproxen
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
0.0012
nimesulide
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
0.38 - 0.39
piroxicam
0.045
punicalagin
Homo sapiens
-
in 10 mM phosphate buffer (pH 7.4), at 37°C
0.001 - 0.064
quercetin
0.038 - 0.074
resveratrol
0.15
salicylic acid
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
3.8
sulindac
Homo sapiens
pH 7.4, 37°C, versus 4-nitrophenol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00185
substrate doxorubicin, pH 7.0, 37°C
0.00504
substrate epirubicin, pH 7.0, 37°C
11.8
pH 7.0, 37°C
0.0000000009
-
reaction of EC 2.8.2.4, estrone sulfotransferase, SULT1A2
0.0000000023
-
reaction of EC 2.8.2.4, estrone sulfotransferase, SULT1A1*2
0.0000007
-
purified SULT1C1, substrate 4-nitrophenol
0.00001
SULT1A3, substrate L-DOPA
0.00009 - 0.00452
SULT activities with 3-naphthylamine, overview
0.00014 - 0.00052
SULT activities with N-hydroxy-4-aminobiphenyl, overview
0.00031 - 0.01201
SULT activities with caffeic acid, overview
0.00069
isoform SULT1A3, at pH 7.0 and 37°C
0.00085
SULT1A3, substrate DL-3-hydroxyphenylalanine
0.0019
-
purified SULT1C2, substrate 4-octylphenol
0.00194
substrate dextrorphan, pH 7.0, 37°C
0.002
-
purified P-PST, substrate 4-nonylphenol
0.00206
SULT1A3, substrate L-tyrosine
0.00211
SULT1A3, substrate 3-nitro-L-tyrosine
0.0024
-
purified P1-PST
0.0028
-
purified M-PST, substrate dopamine
0.00293
substrate 4-nitrophenol, pH 7.0, 37°C
0.0066 - 0.0166
SULT activities with catechol, overview
0.0077
-
purified M-PST
0.01592
SULT1A3, substrate dopamine
0.054
-
purified recombinant H-PST
0.059
-
purified M-PST mutantD86A, substrate dopamine
0.063
-
purified M-PST mutantD86A, substrate dopamine + Mn2+
0.0781
substrate dopamine, pH 7.0, 37°C
0.106
-
M-PST, substrate dobutamine
0.121
purified SULT1A1, substrate 2-aminophenol
0.147
-
P-PST, substrate (+/-)isoproterenol
0.2
purified recombinant SULT1A3
0.34
-
purified PI-PST
0.5
-
purified M-PST wild-type enzyme, substrate dopamine
1.13
-
purified M-PST wild-type enzyme, substrate dopamine + Mn2+
14.2
pH 7.0, 37°C
29.1
pH 7.0, 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
with substrate serotonin
6.2
assay at
6.5 - 10.5
SULT1A3, broad optimum with substrate dopamine
7.2
-
SULT1A1
8 - 9
with substrates dopamine and 6-hydroxydopamine
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
about 65% activity at pH 6.5 and about 50% activity at pH 8.5
additional information
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 45
-
about 60% activity at 30°C and about 90% activity at 45°C, no activity at 50°C
additional information
-
incubation at 37°C causes a selective decrease in activity towards dopamine compared with phenol
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
pulmonary, endothelial cell
Manually annotated by BRENDA team
-
recombinant SULT1A1 expressed in insect Sf9 cells
Manually annotated by BRENDA team
primary pulmonary artery endothelial cells and lung microvascular endothelial cells
Manually annotated by BRENDA team
-
cell lines SaOS-2, U2-OS, PR, and HOS-TE85
Manually annotated by BRENDA team
-
SULT1A1 alozymes 1 and 2, but no SULT1B1 expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
M-PST
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ST1C4_HUMAN
302
0
35520
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
250000
-
isozyme M-PST, gel filtration
32000
-
2 * 32000, SDS-PAGE
33000
-
x * 33000, recombinant M-PST
34000
-
2 * 34000, recombinant H-PST, SDS-PAGE
34300
-
MALDI-TOF mass spectrometry
35500
-
x * 35500, recombinant TL-PST, SDS-PAGE
38000
gel filtration, mutant K266E
60000
gel filtration, mutant E275K
60000 - 65000
-
H-PST, gel filtration
68000
-
isozyme P-PST, gel filtration
77000
gel filtration, wild-type
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with adenosine 3',5'-bisphosphate, purified recombinant SULT1A3 at 10 mg/ml, sitting drop method at 20°C, protein solution: 50 mM Tris-HCl, pH 7.4, 1 mM 2-mercaptoethanol, 4 mM adenosine 3',5'-bisphosphate, precipitant solution: 0.65 M ammonium sulfate, 0.1 M sodium citrate, pH 5.1, 10 mM 2-mercaptoethanol, equal volumes, 4 days, X-ray diffraction structure determination and analysis
crystal structure of SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate, at 2.6 A resolution. Space group: P2(1)2(1)2. Unit cell dimension: a = 79.3 A, b = 123.6 A, c = 73.1 A, alpha = 90.0°, beta = 90°, gamma = 90°
homology modeling in complex with 3'-phosphoadenylyl sulfate
in complex with adenosine 3',5'-bisphosphate alone, with adenosine 3',5'-bisphosphate and 3-cyano-7-hydroxycumarin and with adenosine 3',5'-bisphosphate and 2-naphthol, vapor diffusion method
purified SULT1B1, SULT1C1, and SULT1C3 are crystallized in the presence of 2 mM PAP using the hanging drop method at 20°C by mixing for SULT1B1: 0.002 ml of the protein solution with 0.002 ml of the reservoir solution containing 0.1 M Bis-Tris, pH 6.5, 0.2 M ammonium sulfate and 16%-20% PEG 4000, for SULT1C1: 0.002 ml of the protein solution with 0.002 ml of the reservoir solution containing 0.1 M K2HPO4 and 12%-16% PEG 3350, and for SULT1C3: 0.002 ml of the protein solution with 0.002 ml of the reservoir solution containing 18% PEG 3350, 0.2 M ammonium formate, 0.1 M Bis-Tris (pH 6.5), to obtain crystals of SULT1C2-PAP-PCP ternary complex, 10 mg/ml of purified SULT1C2 is mixed with 2 mM PAP and 2 mM PCP in 20 mM MES-NaOH buffer, pH 6.5, and incubated on ice for 30 min, SULT1C2-PAP-PCP complex is crystallized using the sitting drop method at 20°C by mixing 0.0008 ml of the protein-cofactor-inhibitor mix with 0.0008 ml of the reservoir solution containing 25% PEGl 3350, 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 6.5, SULT4A1 and SULT1C2 crystals are obtained by using the hanging drop method at 20°C by mixing 0.002 ml of the protein solution with 0.002 ml of the reservoir solution containing 20% PEG 4000, 0.2 M ammonium tartrate, and 14%-20% PEG 3350, 0.2 M lithium citrate, 0.1 M sodium citrate, pH 4.6, respectively
-
structure of the catechin-binding site of SULT1A1 bound to epigallocatechin gallate, using a spin-label triangulation method. The allosteric pocket resides in a dynamic region of the protein that enables epigallocatechin gallate to control opening and closure of the enzyme's active-site cap
structure of the Mefenamic acid-binding site of SULT1A1, using spin-label triangulation NMR
SULT1A1 complexed with 3'-phosphoadenosine-5'-phosphate and two molecules of 4-nitrophenol, X-ray diffraction structure analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A146E
-
P-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, highly increased activity wih 4-nitrophenol
A86D/I89E
-
P-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, highly increased activity wih 4-nitrophenol
A86D/I89E/A146E
-
P-PST mutant by site-directed mutagenesis, no activity
C70S
-
mutation has no effect on enzymic activity, but the mutant is more thermosensitive than the wild-type
D249G
the mutant shows higher specific activity towards 3-cyano-7-hydroxycumarin (0.1 mM and above) compared to the wild type enzyme. The mutant is less heat stable than the wild type enzyme
D86A/E89I
-
M-PST mutant by site-directed mutagenesis, reduced activity
D86A/E89I/E146A
-
M-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, and highly increased activity with 4-nitrophenol
E146A
E275K
generation of a targeted point mutation of the KxxxTVxxxE dimerization motif to KxxxTVxxxK (E275K) or ExxxTVxxxE (K266E). The heterodimer exhibits wild-type-like activity with regards to native size, thermal integrity, phosphoadenosine 5'-phosphate affinity, and phosphoadenosine 5'-phosphosulfate Km value. Substitution of the dysfunctional subunits for fully active subunits yields dimeric SULT1B1 with 50% the activity of the fully competent dimer
E89I
-
M-PST mutant by site-directed mutagenesis, reduced activity
F247L
unlike wild-type enzyme SULT1A1 the mutant enzyme shows substrate inhibition with dopamine at high concentrations
G148C
naturally occuring mutation of the SULt1A1 gene, frequency is 0.49% in the Japanese population, the mutant shows reduced enzyme activity with substrate trans-4-hydroxytamoxifen compared to the wild-type enzyme
H108A
H109Y
mutation negatively affects 3'-phosphoadenosine 5'-phosphate binding by approximately 10fold and completely abolishes activity
H143Y
H143Y/E146A
site-directed mutagenesis, reduced activity with dopamine and increased activity with 4-nitrophenol compared to wild-type SULT1A3, switch of specificity to wild-type SULT1A1
I89A
mutation does not show any significant effect on substrate inhibition pattern with dopamine or 4-nitrophenol, enzyme form SULT1A1
I89E
-
P-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, highly increased activity wih 4-nitrophenol
I89E/A146E
-
P-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, no activity wih 4-nitrophenol
K234N
missense SNP for the SULT1A3 gene
K266E
generation of a targeted point mutation of the KxxxTVxxxE dimerization motif to KxxxTVxxxK (E275K) or ExxxTVxxxE (K266E). The heterodimer exhibits wild-type-like activity with regards to native size, thermal integrity, phosphoadenosine 5'-phosphate affinity, and phosphoadenosine 5'-phosphosulfate Km value. Substitution of the dysfunctional subunits for fully active subunits yields dimeric SULT1B1 with 50% the activity of the fully competent dimer
K48M
-
P-PST and M-PST mutants by site-directed mutagenesis, no activity
K48M/H108A
-
M-PST mutant by site-directed mutagenesis, no activity
L67V/A101S/Q177K/V211L/F222K/F247I
the mutant is more heat stable than the wild type enzyme
M223V
-
the mutation is associated with decreased platelet enzymatic activity and thermostability
N235T
missense SNP for the SULT1A3 gene
N85K
-
M-PST mutant by site-directed mutagenesis, reduced activity
N85K/D86A
-
M-PST mutant by site-directed mutagenesis, reduced activity with dopamine, unaltered activity wih 4-nitrophenol
N85K/E89I
-
M-PST mutant by site-directed mutagenesis, reduced activity
P101H
missense SNP for the SULT1A3 gene
P101L
missense SNP for the SULT1A3 gene
P10L
missense SNP for the SULT1A3 gene
P19L
missense SNP for the SULT1A3 gene
Q56E/A101S/T117S/H213R/F222L/V243L/T266N/L111P/Y240C
the mutant is more heat stable than the wild type enzyme
Q56E/A101S/T117S/Q177K/M223I/V243L
the mutant shows higher specific activity towards 3-cyano-7-hydroxycumarin (0.1 mM and above) compared to the wild type enzyme. The mutant is more heat stable than the wild type enzyme
Q56E/L67V/A101S/T117S/H213R/F222L/V243I/D249G
the mutant shows higher specific activity towards 3-cyano-7-hydroxycumarin (0.1 mM and above) compared to the wild type enzyme. The mutant is more heat stable than the wild type enzyme
R130A
site-directed mutagenesis, SULT1A1 mutant, unaltered activity
R130E
site-directed mutagenesis, SULT1A1 mutant, slightly increased activity
R144C
missense SNP for the SULT1A3 gene
R213E
site-directed mutagenesis, SULT1A1 mutant, unaltered activity
R213H
R257A
site-directed mutagenesis, SULT1A1 mutant, no activity
R257E
site-directed mutagenesis, SULT1A1 mutant, no activity
R258K
mutation renders the isoform unable to bind 3'-phosphoadenosine 5'-phosphate at detectible levels
R78A
site-directed mutagenesis, SULT1A1 mutant, unaltered activity
R78E
site-directed mutagenesis, SULT1A1 mutant, no activity
R9C
missense SNP for the SULT1A3 gene
S290T
missense SNP for the SULT1A3 gene
S8P
missense SNP for the SULT1A3 gene
T7P
missense SNP for the SULT1A3 gene
V15M
missense SNP for the SULT1A3 gene
V18F
missense SNP for the SULT1A3 gene
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
the wild type enzyme remains stable up to 40°C and then rapidly loses activity being completely inactive at temperatures of 42°C and above
37
-
H-PST, inactivation after 15 min
37.6
-
liver TL-PST, 50% inactivation at
38.3
-
SULT1A3, 50% inactivation within 15 min
39
-
15 min, 50% of the activity remains, enzyme form SULT1A3
40.4
-
liver TS-PST, 50% inactivation at
43
-
SULT1A1, 50% inactivation within 15 min
44.5
50% inactivation, SULT1A1 allozymes 2
45
wild-type, stable for at least 90 min. The K266E mutant loses almost all activity after a 90 minute 45°C incubation, the E275K mutant loses 30% of its sulfation activity. A mutants K266E/E275K heterodimer retains most of its activity after 45°C incubation for 90 min
46.9
50% inactivation, SULT1A1 allozymes 1
47
-
SULT1A1, inactivation within 15 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the recombinant SULT1A1*2 protein has a shorter half-life than the recombinant SULT1A1*1 protein
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, liver cytosol, 50 mM Tris-HCl, pH 7.8, 0.25 M sucrose, 0.5 mM EDTA, 0.1 mM DTT, and 0.02 mM BHT, no loss of activity during storage
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
389fold
-
557fold
-
DEAE-Sepharose column chromatography and amylose affinity column chromatography
-
monoamine-sulfating form, M-PST
-
Ni-NTA agarose column chromatography
Ni-NTA resin column chromatography
nickel chelating Sepharose chromatography and glutathione Sepharose column chromatography
-
one-step column chromatography, His-binding metal chelation resin column
partial
-
phenol-sulfating form, P-PST
-
recombinant enzyme as maltose-binding fusion protein from Escherichia coli
recombinant enzyme, enzyme form SULT1A3
-
recombinant from Escherichia coli
recombinant H-PST from Escherichia coli, 14.5fold
-
recombinant His-tagged SULT1A1 from Escherichia coli by nickel affinity chromatography
recombinant His-tagged SULT1A1*1, *2, and *3 from Spodoptera frugiperda Sf9 cells by metal affinity chromatography
-
recombinant His-tagged SULT1A3 from Escherichia coli by nickel affinity chromatography
recombinant SULT1A3 from Escherichia coli strain by ammonium sulfate fractionation, anion exchange and adenosine 3',5'-bisphosphate affinity chromatography
recombinant SULT1A3 from Escherichia coli, to homogeneity
recombinant wild-type P-PST and M-PST and chimeric mutants
recombinant wild-type SULT1A3 and mutants from Escherichia coli
TL-PST
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
DNA and amino acid sequence determination, expression of P-PST in COS cells and Escherichia coli XL1-Blue
-
DNA sequence determination and analysis, expression of SULT1A3 in several expression systems: Escherichia coli, Saccharomyces cerevisiae, COS-7 cells, V79 cells, overview
expressed in Escherichia coli as fusion protein with maltose-binding protein
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli M15 as His-tagged protein
-
expression in Escherichia coli, enzyme form SULT1A3
-
expression in HeLa cell, SKN-MC cell, and SH-SY5Y cell
expression of His-tagged sulfotransferase in Escherichia coli BL21-DE3
expression of His-tagged SULT1A1 in Escherichia coli
expression of His-tagged SULT1A3 in Escherichia coli
expression of His6-Rv3117 in Escherichia coli BL21-DE3
expression of simple phenol sulfating P-PST and monoamine sulfating M-PST in COS-7 cells as HAST1 and HAST3
-
expression of SULT1A1 allozymes 1 and 2 in COS-1 cells, amino acid sequence determination
expression of SULT1A1 in Escherichia coli, expression analysis
expression of SULT1A1 in TB1 cells as maltose-binding-protein fusion protein
expression of SULT1A1 wild-type and mutants as maltose-binding fusion protein in Escherichia coli XL1-Blue
expression of SULT1B1 in Escherichia coli
expression of SULT1B1 in Escherichia coli, expression analysis
expression of SULTs in Escherichia coli strain BL21 DE3, in Salmonella typhimurium strain TA1538, and in chinese hamster V79 cells, and application of aristolochic acid, mutagenicity with expression of different SULT isozymes and allozymes of SULT1A1, detailed overview, analysis of the expression of SULT1A1
expression of wild-type M-PST and mutant D86A in Escherichia coli BL21
-
expression of wild-type P-PST and M-PST and chimeric mutants bearing parts of both enzyme forms in Escherichia coli
expression of wild-type P-PST and M-PST and diverse mutants of both in Escherichia coli XL1-Blue
-
genetic polymorphisms in the SULT1A1 gene define three alleles, SULT1A1*1, *2, and *3, stable expression of the allozymes in MCF-7 cells, allele-specific antiestrogenic response to 4-hydroxytamoxifen, expression of His-tagged SULT1A1*1, *2, and *3 in Spodoptera frugiperda Sf9 cells via liposome transfection
-
M-PST, functional expression in Escherichia coli
-
overexpression of H-PST in Escherichia coli BL21(DE3)
-
overexpression of SULT1A1 in Escherichia coli strain XL-1 Blue cytosol
recombinant expression of SULT1A1*2
-
SULT1A1, DNA and amino acid sequence determination and analysis, genotyping, determination and sequence analysis of putative transcription factor binding sites, SULT1A1 promoter haplotype frequencies in African-American, Caucasian, and Chinese individuals, overview
SULT1A1, DNA and amino acid sequence determination and analysis, sequence determination and distribution analysis of mutations other than SULT1A1*2 in the SULT1A1 gene, overview, expression of SULT1A1*1 and SULT1A1*2 allozymes
SULT1A1, DNA sequence determination and analysis, expression in Escherichia coli
SULT1A3 and SULT1A1, expression analysis in Hep-G2 cells in response to glucocorticoids prednisolone and dexamethasone
SULT1A3, expression in Escherichia coli
SULT1A3, wild-type and mutants, expression in Escherichia coli
the human SULT1A1 gene has common single nucleotide polymorphisms that define three allozymes, SULT1A1*1, *2, and *3, stable expression of the allozymes in MCF-7 cells and expression of His-tagged SULT1A1 allozymes using a baculoviral-Spodoptera frugiperda Sf9 cell system
TL-PST, DNA and amino acid sequence determination, in vitro transcription and translation, and expression in COS-1 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pomegranate juice shows no effects on the expression of the sulfotransferase SULT1A family of genes (SULT1A1 and SULT1A3) in Caco-2 cells
-
SULT1A1 is down-regulated in hepatocellular carcinoma
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
isoforms SULT1A1, 1A2, 1A3, 1B1, 1C4, 1E1 display significant sulfating activities toward rotigotine. Of the 6 human organ samples tested, small intestine and liver cytosols display considerably higher rotigotine-sulfating activity than brain, lung, and kidney. Sulfation of rotigotine occurs in HepG2 cells and Caco-2 cells under metabolic conditions
synthesis
Escherichia coli cells expressing human isoform SULT1A3 produce preferentially genistein 4'-sulfate, Escherichia coli cells expressing isoform SULT1C4 produce preferentially genistein 7-sulfate. Presence of glucose, SO42-, and incubation temperature are key factors that affect the efficiency of the production
analysis
medicine
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pacifici, G.M.; Franchi, M.; Giuliani, L.
Characterization of sulphotransferase in human ileum and colon
Pharmacology
38
146-150
1989
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Weinshilboum, R.M.
Phenol sulfotransferase in humans: properties, regulation, and function
Fed. Proc.
45
2223-2228
1986
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chen, G.
Histidine residues in human phenol sulfotransferases
Biochem. Pharmacol.
67
1355-1361
2004
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Nowell, S.; Falany, C.N.
Pharmacogenetics of human cytosolic sulfotransferases
Oncogene
25
1673-1678
2006
Homo sapiens (P50225)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Wang, T.; Cook, I.; Leyh, T.S.
Isozyme specific allosteric regulation of human sulfotransferase 1A1
Biochemistry
55
4036-4046
2016
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Tibbs, Z.; Falany, C.
An engineered heterodimeric model to investigate SULT1B1 dependence on intersubunit communication
Biochem. Pharmacol.
115
123-133
2016
Homo sapiens (O43704)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team