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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

3,5,3'-triiodothyronine + PAPS => 3,5,3'-triiodothyronine 4-sulfate + PAP

T3 + PAPS → 3,5,3'-triiodothyronine 4-sulfate + PAP

Reactome: R-HSA-176585
Compartment: cytosol
Rhea: None recorded

Inputs

T3CHEBI:533015, C15H12I3NO4, cytosol
PAPSCHEBI:58339, C10H11N5O13P2S, cytosol

Outputs

3,5,3'-triiodothyronine 4-sulfateCHEBI:35432, C15H12I3NO7S, cytosol
PAPCHEBI:58343, C10H11N5O10P2, cytosol

Catalysed by

aryl sulfotransferase activity of SULT dimers (T3) [cytosol]EC 2.8.2.1

Literature

Characterization of human iodothyronine sulfotransferases J Clin Endocrinol Metab, 1999
Characterization of human liver thermostable phenol sulfotransferase (SULT1A1) allozymes with 3,3',5-triiodothyronine as the substrate J Endocrinol, 2001
Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver Mol Pharmacol, 1998
Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization Gene, 2002
Sulfation of iodothyronines by human sulfotransferase 1C1 (SULT1C1)* Biochem Pharmacol, 2000
Sulfation of iodothyronines by recombinant human liver steroid sulfotransferases Biochem Biophys Res Commun, 1999