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EC Tree
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).
The taxonomic range for the selected organisms is: Bos taurus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sult1a1, sult2a1, sult1e1, sulphotransferase, sult1a3, phenol sulfotransferase, cytosolic sulfotransferase, sult4a1, sult1b1, sult1a2,
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phenol sulfotransferase
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1-naphthol phenol sulfotransferase
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2-naphtholsulfotransferase
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4-nitrocatechol sulfokinase
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arylsulfotransferase
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catecholamine-sulfating phenol sulfotransferase
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DOPA/tyrosine sulfotransferase
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dopamine sulfotransferase
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hippocampal phenol sulfotransferase
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minoxidil sulfotransferase
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monoamine sulfotransferase
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p-nitrophenol sulfotransferase
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phenol sulfokinase
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phenol sulfotransferase
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phenol/aryl sulfotransferase
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ritodrine sulfotransferase
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sulfotransferase, aryl
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sulfotransferase, monoamine-preferring
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thermolabile phenol sulfotransferase
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thermostable phenol sulfotransferase
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tyrosine-ester sulfotransferase
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3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate
mechanism
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sulfate group transfer
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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).
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3'-phosphoadenylyl sulfate + 7-hydroxycoumarin
adenosine 3',5'-bisphosphate + 7-hydroxycoumarin sulfate
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
3'-phosphoadenylylsulfate + 2-naphthol
adenosine 3',5'-bisphosphate + 2-naphthyl sulfate
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ST1A6
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?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
additional information
?
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3'-phosphoadenylyl sulfate + 7-hydroxycoumarin
adenosine 3',5'-bisphosphate + 7-hydroxycoumarin sulfate
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?
3'-phosphoadenylyl sulfate + 7-hydroxycoumarin
adenosine 3',5'-bisphosphate + 7-hydroxycoumarin sulfate
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?
3'-phosphoadenylyl sulfate + 7-hydroxycoumarin
adenosine 3',5'-bisphosphate + 7-hydroxycoumarin sulfate
SULT molecular dynamic, substrate 3'-phosphoadenylyl sulfate, i.e. PAPS, induces a structural change, overview
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?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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?
3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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r
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
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?
3'-phosphoadenylylsulfate + 1-naphthol
adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
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highest activity among simple phenols tested
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?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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enzyme may be considered as detoxification enzyme which catalyzes the conjugation of xenobiotics containing a phenol group or of phenolic compounds generated by endogenous oxidation
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?
additional information
?
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tyrosine and its derivatives
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?
additional information
?
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different enzyme forms show overlapping substrate specificities, overview
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?
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3'-phosphoadenylyl sulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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?
3'-phosphoadenylylsulfate + a phenol
adenosine 3',5'-bisphosphate + an aryl sulfate
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enzyme may be considered as detoxification enzyme which catalyzes the conjugation of xenobiotics containing a phenol group or of phenolic compounds generated by endogenous oxidation
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?
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CoA
reversible covalent inhibition, the inactivation of the dimeric enzyme is stoichiometric, binding structure and mechanism, overview
2,6-Dichloro-4-nitrophenol
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pyridoxal 5'-phosphate
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50% inhibition at 0.001 mM, excess of 2-naphthol protects
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0.000815 - 0.00524
3'-phosphoadenylyl sulfate
0.000526 - 0.003
7-hydroxycoumarin
additional information
additional information
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kinetics
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0.000815
3'-phosphoadenylyl sulfate
wild-type, pH 7.4, temperature not specified in the publication
0.001394
3'-phosphoadenylyl sulfate
mutant W53Y, pH 7.4, temperature not specified in the publication
0.00519
3'-phosphoadenylyl sulfate
mutant W53L, pH 7.4, temperature not specified in the publication
0.00524
3'-phosphoadenylyl sulfate
mutant W53A, pH 7.4, temperature not specified in the publication
0.000526
7-hydroxycoumarin
wild-type, pH 7.4, temperature not specified in the publication
0.00187
7-hydroxycoumarin
mutant W53A, pH 7.4, temperature not specified in the publication
0.00208
7-hydroxycoumarin
mutant W53Y, pH 7.4, temperature not specified in the publication
0.003
7-hydroxycoumarin
mutant W53L, pH 7.4, temperature not specified in the publication
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0.069 - 0.18
3'-phosphoadenylyl sulfate
0.069
3'-phosphoadenylyl sulfate
mutant W53A, pH 7.4, temperature not specified in the publication
0.125
3'-phosphoadenylyl sulfate
mutant W53L, pH 7.4, temperature not specified in the publication
0.141
3'-phosphoadenylyl sulfate
wild-type, pH 7.4, temperature not specified in the publication
0.18
3'-phosphoadenylyl sulfate
mutant W53Y, pH 7.4, temperature not specified in the publication
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13 - 173
3'-phosphoadenylyl sulfate
13
3'-phosphoadenylyl sulfate
mutant W53A, pH 7.4, temperature not specified in the publication
24
3'-phosphoadenylyl sulfate
mutant W53L, pH 7.4, temperature not specified in the publication
129
3'-phosphoadenylyl sulfate
mutant W53Y, pH 7.4, temperature not specified in the publication
173
3'-phosphoadenylyl sulfate
wild-type, pH 7.4, temperature not specified in the publication
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0.023
pyridoxal 5'-phosphate
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additional information
additional information
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0.0021 - 0.0028
CoA
pH 7.4, 25°C, recombinant SULT1A1, method B
0.00573
CoA
pH 7.4, 25°C, recombinant SULT1A1, method A
additional information
additional information
inhibition kinetics
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additional information
additional information
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inhibition kinetics
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SwissProt
brenda
isoform SULT1A1
SwissProt
brenda
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brenda
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brenda
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brenda
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brenda
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ST1A1_BOVIN
295
0
34184
Swiss-Prot
other Location (Reliability: 1 )
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additional information
molecular modeling of the enzyme structure using the crystal structure PDB ID 1LS6
additional information
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molecular modeling of the enzyme structure using the crystal structure PDB ID 1LS6
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homology modeling of the active site. Two phenylalanyl and one tyrosinyl group help create a hydrophobic pocket for phenolic acceptor substrates. Two arginyl and one lysyl residues, plus other groups, aid in the binding of 3'-phosphoadenosine-5'-phospho(sulfate) via electrostatic forces and H-bonding. The conserved histidine serves as the general base to initiate phenoxide anion stabilization and attack on the 3'-phosphoadenosine-5'-phosphosulfate sulfuryl group
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W53A
mutation decreases thermal stabilizations by 3'-phosphoadenosine-5'-phosphate plus pentachlorophenol
W53L
mutation decreases thermal stabilizations by 3'-phosphoadenosine-5'-phosphate plus pentachlorophenol
W53Y
mutation decreases thermal stabilizations by 3'-phosphoadenosine-5'-phosphate plus pentachlorophenol
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42 - 45
30 min, 50% inactivation, wild-type and mutants
45
melting temperature, wild-type peaks at 45°C, with a domain-suggestive shoulder at 49°C
60
melting temperature, wild-type in presence of 3'-phosphoadenosine-5'-phosphate plus pentachlorophenol
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DEAE-cellulose column chromatography
recombinant SULT1A1 from Escherichia coli strain DH5alpha by anion exchange chromatography and gel filtration
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expression of pTrc99A-bSULT1A1 in Escherichia coli DH5alpha
SULT1A1, expression in Escherichia coli strain DH5alpha
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Bartzatt, R.; Beckmann, J.D.
Inhibition of phenol sulfotransferase by pyridoxal phosphate
Biochem. Pharmacol.
47
2087-2095
1994
Bos taurus
brenda
Fernando, P.H.P.; Sakakibara, Y.; Nakatsu, S.; Suiko, M.; Han, J.R.; Liu, M.C.
Isolation and characterization of a novel microsomal membrane-bound phenol sulfotransferase from bovine liver
Biochem. Mol. Biol. Int.
30
433-441
1993
Bos taurus
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
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Chodavarapu, S.; Hertema, H.; Huynh, T.; Odette, J.; Miller, R.; Fullerton, A.; Alkirwi, J.; Hartsfield, D.; Padmanabhan, K.; Woods, C.; Beckmann, J.D.
Reversible covalent inhibition of a phenol sulfotransferase by coenzyme A
Arch. Biochem. Biophys.
457
197-204
2007
Bos taurus (P50227), Bos taurus
brenda
Beckmann, J.; Chodavarapu, S.; Doyle, B.
Evaluation of a conserved tryptophanyl residue in donor substrate binding and catalysis by a phenol sulfotransferase (SULT1A1)
Arch. Biochem. Biophys.
695
108621
2020
Bos taurus (P50227), Bos taurus
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