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Literature summary extracted from

  • 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 (2007), PLoS Biol., 5, 1063-1078.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.2.1 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 Homo sapiens
2.8.2.2 purified SULT1B1 is crystallized in the presence of 2 mM PAP using the hanging drop method at 20°C by mixing for SULT1B1: 0.002 ml of the protein solution with 0.002 ml of the reservoir solution containing 0.1 M Bis-Tris, pH 6.5, 0.2 M ammonium sulfate and 16%-20% PEG 4000 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.2.1 3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide DBHM Homo sapiens
2.8.2.1 3,5-dibromo-4-hydroxybenzoic acid (6,8-dichloro-4-oxo-4H-chromen-3-ylmethylene) hydrazide DBHD Homo sapiens
2.8.2.1 adenosine 5'-(beta,gamma-imido) triphosphate i.e. AMP-PNP, a non-hydrolysable ATP analogue Homo sapiens
2.8.2.1 additional information isoprenaline is poor inhibitor of SULT1B1 Homo sapiens
2.8.2.1 pyridoxal 5'-phosphate a competitive inhibitor for sulfotransferases Homo sapiens
2.8.2.1 quercetin a potent inhibitor of SULT1A1 Homo sapiens
2.8.2.2 3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide DBHM Homo sapiens
2.8.2.2 3,5-dibromo-4-hydroxybenzoic acid (6,8-dichloro-4-oxo-4H-chromen-3-ylmethylene) hydrazide DBHD Homo sapiens
2.8.2.2 adenosine 5'-(beta,gamma-imido) triphosphate i.e. AMP-PNP, a non-hydrolysable ATP analogue Homo sapiens
2.8.2.2 additional information isoprenaline is poor inhibitor of SULT1B1 Homo sapiens
2.8.2.2 pyridoxal 5'-phosphate a competitive inhibitor for sulfotransferases Homo sapiens
2.8.2.4 3,5-dibromo-4-hydroxy-benzoic acid (6-chloro-4-oxo-4H-chromen-3-ylmethylene)-hydrazide DBHM Homo sapiens
2.8.2.4 3,5-dibromo-4-hydroxybenzoic acid (6,8-dichloro-4-oxo-4H-chromen-3-ylmethylene) hydrazide DBHD Homo sapiens
2.8.2.4 adenosine 5'-(beta,gamma-imido) triphosphate i.e. AMP-PNP, a non-hydrolysable ATP analogue Homo sapiens
2.8.2.4 pyridoxal 5'-phosphate a competitive inhibitor for sulfotransferases Homo sapiens
2.8.2.4 quercetin a potent inhibitor of SULT1E1 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.8.2.1 cytosol
-
 Homo sapiens 5829
-
2.8.2.2 cytosol
-
 Homo sapiens 5829
-
2.8.2.4 cytosol
-
 Homo sapiens 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.2.1 additional information Homo sapiens SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview ?
-
 ?
2.8.2.2 additional information Homo sapiens SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview ?
-
 ?
2.8.2.4 additional information Homo sapiens SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.2.1 Homo sapiens
-
-
-
2.8.2.2 Homo sapiens O00204
-
-
2.8.2.4 Homo sapiens P49888
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.2.1 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate random bi-bi mechanism catalytic mechanism of SULTs, many family members have distinct, but overlapping substrate specificities, the enzymes have a sequential catalytic mechanism that is susceptible to substrate inhibition Homo sapiens
a
2.8.2.2 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate random bi-bi mechanism catalytic mechanism of SULTs, many family members have distinct, but overlapping substrate specificities, the enzymes have a sequential catalytic mechanism that is susceptible to substrate inhibition Homo sapiens
a
2.8.2.4 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate random bi-bi mechanism catalytic mechanism of SULTs, many family members have distinct, but overlapping substrate specificities, the enzymes have a sequential catalytic mechanism that is susceptible to substrate inhibition Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.2.1 brain SULT4A1, an orphan member of the SULT family expressed primarily in the brain Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.1 3'-phosphoadenylyl sulfate + 1-naphthol SULT1B1 Homo sapiens adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
 ?
2.8.2.1 additional information SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview Homo sapiens ?
-
 ?
2.8.2.1 additional information role for 3'-phosphoadenylyl sulfate in priming the conformation of substrate binding loops, overview, substrate specificities and binding structures of SULT1B1, SULT1A1, SULT1A3, SULT1C1, SULT1C2, and SULT1C3, overview Homo sapiens ?
-
 ?
2.8.2.2 3'-phosphoadenylyl sulfate + 1-naphthol SULT1B1 Homo sapiens adenosine 3',5'-bisphosphate + 1-naphthyl sulfate
-
 ?
2.8.2.2 additional information SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview Homo sapiens ?
-
 ?
2.8.2.2 additional information role for 3'-phosphoadenylyl sulfate in priming the conformation of substrate binding loops, overview, substrate specificity and binding structure of SULT1B1, overview Homo sapiens ?
-
 ?
2.8.2.4 additional information SULTs play a role in the metabolism of regulatory hormones, drugs, and carcinogens, they catalyze the sulfonation of simple phenols, estradiol, and thyroid hormones, as well as environmental xenobiotics and drugs, overview Homo sapiens ?
-
 ?
2.8.2.4 additional information role for 3'-phosphoadenylyl sulfate in priming the conformation of substrate binding loops, overview, substrate specificity and binding structure of SULT1E1, overview Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.2.1 More detailed structural analysis and comparison of SULT family enzymes, comparison of substrate binding structures of SULT1B1, SULT1A1, SULT1A3, SULT1C1, SULT1C2, and SULT1C3, overview, chemical library preparation and ligand binding screens Homo sapiens
2.8.2.2 More detailed structural analysis and comparison of SULT family enzymes, comparison of substrate binding structures of SULT1B1, overview, chemical library preparation and ligand binding screens Homo sapiens
2.8.2.4 More detailed structural analysis and comparison of SULT family enzymes, comparison of substrate binding structures, overview, chemical library preparation and ligand binding screens Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.8.2.1 cytosolic sulfotransferase
-
 Homo sapiens
2.8.2.1 SULT
-
 Homo sapiens
2.8.2.1 SULT1A1
-
 Homo sapiens
2.8.2.1 SULT1A2
-
 Homo sapiens
2.8.2.1 SULT1A3
-
 Homo sapiens
2.8.2.1 SULT1B1
-
 Homo sapiens
2.8.2.1 SULT1C1
-
 Homo sapiens
2.8.2.1 SULT1C2
-
 Homo sapiens
2.8.2.1 SULT1C3
-
 Homo sapiens
2.8.2.1 SULT4A1
-
 Homo sapiens
2.8.2.2 cytosolic sulfotransferase
-
 Homo sapiens
2.8.2.2 SULT
-
 Homo sapiens
2.8.2.2 SULT1B1
-
 Homo sapiens
2.8.2.4 cytosolic sulfotransferase
-
 Homo sapiens
2.8.2.4 SULT
-
 Homo sapiens
2.8.2.4 SULT1E1
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.2.1 37
-
 assay at Homo sapiens
2.8.2.2 37
-
 assay at Homo sapiens
2.8.2.4 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.2.1 7.5
-
 assay at Homo sapiens
2.8.2.2 7.5
-
 assay at Homo sapiens
2.8.2.4 7.5
-
 assay at Homo sapiens