Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
- Name help_outline 3'-phosphoadenylyl sulfate Identifier CHEBI:58339 Charge -4 Formula C10H11N5O13P2S InChIKeyhelp_outline GACDQMDRPRGCTN-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OS([O-])(=O)=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 106 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-nitrophenol Identifier CHEBI:57917 (Beilstein: 3589511) help_outline Charge -1 Formula C6H4NO3 InChIKeyhelp_outline BTJIUGUIPKRLHP-UHFFFAOYSA-M SMILEShelp_outline [O-]c1ccc(cc1)[N+]([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-nitrophenyl sulfate Identifier CHEBI:140994 Charge -1 Formula C6H4NO6S InChIKeyhelp_outline JBGHTSSFSSUKLR-UHFFFAOYSA-M SMILEShelp_outline C1=C(C=CC(=C1)[N+](=O)[O-])OS([O-])(=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline adenosine 3',5'-bisphosphate Identifier CHEBI:58343 Charge -4 Formula C10H11N5O10P2 InChIKeyhelp_outline WHTCPDAXWFLDIH-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 140 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:66548 | RHEA:66549 | RHEA:66550 | RHEA:66551 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| Reactome help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases.
Fujita K., Nagata K., Ozawa S., Sasano H., Yamazoe Y.
Human and rat cDNAs encoding thyroid hormone sulfotransferases have been isolated from their liver cDNA libraries. The isolated sulfotransferases, termed rat ST1B1 and human ST1B2, share 77 and 74% homologies at nucleotide and deduced amino acid levels. These forms showed less than 36 and 56% homo ... >> More
Human and rat cDNAs encoding thyroid hormone sulfotransferases have been isolated from their liver cDNA libraries. The isolated sulfotransferases, termed rat ST1B1 and human ST1B2, share 77 and 74% homologies at nucleotide and deduced amino acid levels. These forms showed less than 36 and 56% homologies to hydroxysteroid and aryl sulfotransferases, indicating that they constitute a new gene subfamily of aryl sulfotransferase. Expression of ST1B1 and ST1B2 in COS-1 cells resulted in the appearance of 33.0 and 32.5 kDa proteins, respectively, whose mobilities were identical with proteins detected in rat and human livers in Western blots using antibodies raised against ST1B1 and ST1B2 produced in Escherichia coli. The recombinant forms catalyzed sulfation of p-nitrophenol, 3,3',5-triiodothyronine (T3) and dopamine, but not of beta-estradiol and dehydroepiandrosterone. ST1B1 and ST1B2 showed higher affinities for formation of T3 sulfate (apparent Km 40.2 and 63.5 microM, respectively) than did thermostable phenol sulfotransferase ST1A3 (apparent Km 413 microM) or thermolabile phenol sulfotransferase ST1A5 (apparent Km 180 microM). These data indicate that the newly characterized sulfotransferases constitute a distinct ST1 subfamily of enzymes catalyzing the sulfation of T3 as a typical endogenous substrate in rats and humans. << Less
J. Biochem. 122:1052-1061(1997) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
-
A novel sulfotransferase abundantly expressed in the dauer larvae of Caenorhabditis elegans.
Hattori K., Inoue M., Inoue T., Arai H., Tamura H.O.
We have isolated a gene (clone Y113G7A.11) from Caenorhabditis elegans (C. elegans), that we have designated as ceST1, and which is the only member of the cytosolic sulfotransferase (SULT) gene family present in the genome of this organism. We identified the SULT motifs of ceST1 based upon their d ... >> More
We have isolated a gene (clone Y113G7A.11) from Caenorhabditis elegans (C. elegans), that we have designated as ceST1, and which is the only member of the cytosolic sulfotransferase (SULT) gene family present in the genome of this organism. We identified the SULT motifs of ceST1 based upon their deduced amino acid sequence, and subsequently expressed the ceST1 cDNA in Escherichia coli and characterized its enzymatic properties. The recombinant protein showed sulfation activity for 4-nitrophenol and 2-naphthol substrates, but did not catalyze the sulfation of either monoamines or hydroxysteroids. Another compound sulfated by ceST1 is bisphenol A, which is known to stimulate germ cell proliferation in C. elegans. SULT activity was not detected in the cytosol of C. elegans, probably due to heat labile inhibitors. The ceST1 protein was detectable in the cytosol of C. elegans using anti-sera raised against recombinant ceST1, and transcripts could also be detected throughout the developmental stages. Moreover, high levels of ceST1 expression were evident at both the embryonic and adult stages and were augmented in dauer larva. These findings suggest that this sulfotransferase either forms part of a defence system against xenobiotics or regulates germ cell proliferation in C. elegans. << Less
J. Biochem. 139:355-362(2006) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.