Enzymes
| UniProtKB help_outline | 8 proteins |
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- Name help_outline L-thyroxine Identifier CHEBI:58448 Charge 0 Formula C15H11I4NO4 InChIKeyhelp_outline XUIIKFGFIJCVMT-LBPRGKRZSA-N SMILEShelp_outline [NH3+][C@@H](Cc1cc(I)c(Oc2cc(I)c(O)c(I)c2)c(I)c1)C([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 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 125 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-thyroxine sulfate Identifier CHEBI:176512 Charge -1 Formula C15H10I4NO7S InChIKeyhelp_outline QYXIJUZWSSQICT-LBPRGKRZSA-M SMILEShelp_outline [NH3+][C@@H](CC1=CC(I)=C(OC2=CC(I)=C(OS([O-])(=O)=O)C(I)=C2)C(I)=C1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 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 159 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:83575 | RHEA:83576 | RHEA:83577 | RHEA:83578 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3',5-triiodothyronine as the substrate.
Li X., Clemens D.L., Cole J.R., Anderson R.J.
Sulfotransferase 1A1 (SULT1A1) (thermostable phenol sulfotransferase, TS PST1, P-PST) is important in the metabolism of thyroid hormones. SULT1A1 isolated from human platelets displays wide individual variations not only in the levels of activity, but also in thermal stability. The activity of the ... >> More
Sulfotransferase 1A1 (SULT1A1) (thermostable phenol sulfotransferase, TS PST1, P-PST) is important in the metabolism of thyroid hormones. SULT1A1 isolated from human platelets displays wide individual variations not only in the levels of activity, but also in thermal stability. The activity of the allelic variant or allozyme SULT1A1*1, which possesses an arginine at amino acid position 213 (Arg213) has been shown to be more thermostable than the activity of the SULT1A1*2 allozyme which possesses a histidine at this position (His213) when using p-nitrophenol as the substrate. We isolated a SULT1A1*1 cDNA from a human liver cDNA library and expressed both SULT1A1*1 and SULT1A1*2 in eukaryotic cells. The allozymes were assayed using iodothyronines as the substrates and their biochemical properties were compared. SULT1A1*1 activity was more thermostable and more sensitive to NaCl than was SULT1A1*2 activity when assayed with 3,5,3'-triiodothyronine (T(3)). Sensitivities to 2,6-dichloro-4-nitrophenol (DCNP) and apparent K(m) values for SULT1A1*1 and for SULT1A1*2 with iodothyronines were similar. Based on K(m) values, the preferences of these SULT1A1 allozymes for iodothyronine substrates were the same (3,3'-diiodothyronine (3,3'-T(2))>3', 5',3-triiodothyronine (rT(3))>T(3)>thyroxine (T(4))>>3,5-diiodothyronine (3,5-T(2))). SULT1A1*1 activity was significantly higher than the SULT1A1*2 activity with T(3) as the substrate. Potential differences in thyroid hormone sulfation between individuals with predominant SULT1A1*1 versus SULT1A1*2 allozymes are most likely due to differences in catalytic activity rather than substrate specificity. << Less
J Endocrinol 171:525-532(2001) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Characterization of thyroid hormone sulfotransferases.
Visser T.J., Kaptein E., Glatt H., Bartsch I., Hagen M., Coughtrie M.W.
Sulfation is an intriguing pathway of thyroid hormone metabolism since it facilitates the degradation of the hormone by the type I deiodinase (D1). This study reports the preliminary characterization of iodothyronine sulfotransferase activities of rat and human liver cytosol and recombinant rSULT1 ... >> More
Sulfation is an intriguing pathway of thyroid hormone metabolism since it facilitates the degradation of the hormone by the type I deiodinase (D1). This study reports the preliminary characterization of iodothyronine sulfotransferase activities of rat and human liver cytosol and recombinant rSULT1C1 and hSULT1A1 isoenzymes. All these enzyme preparations catalyzed the sulfation of--in decreasing order of efficiency--3,3'-diiodothyronine (3,3'-T2) > 3,3',5-triiodothyronine (T3) approximately 3,3',5'-triiodothyronine (rT3) > thyroxine (T4). 3,3'-T2 sulfotransferase activity was found to be higher in male than in female rat liver, which has also been shown by others for the expression of rSULT1A1 and rSULT1C1. No sulfation of iodothyronines was observed with rSULT1A1. Different phenol derivatives were found to be potent inhibitors of the sulfation of 3,3'-T2 by native and recombinant sulfotransferases, with pentachlorophenol and 2,4,6-tribromophenol being the most potent. The inhibitions exerted by the different phenols on 3,3'-T2 sulfation by rSULT1C1 correlated better with the effects observed in male than with those in female liver. A strong correlation was also observed between the inhibition profiles of human liver cytosol and hSUL1T1A1. These results suggest that: (1) rSULT1C1 is an important isoenzyme for the sulfation of thyroid hormone in male rat liver; (2) another isoenzyme with similar properties, perhaps rSULT1B1, is responsible for thyroid hormone sulfation in female rat liver and may also contribute to this process in male rat liver; and (3) hSULT1A1 is an important isoenzyme for thyroid hormone sulfation in human liver. << Less
Chem Biol Interact 109:279-291(1998) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.