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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.

TPST1,2 transfer SO4(2-) from PAPS to PODXL2

PODXL2 + 2 PAPS → OSulf-Y97,118-PODXL2 + 2 PAP

Reactome: R-HSA-8954262
Compartment: Golgi lumen · Golgi membrane
Rhea: None recorded

Inputs

PODXL2R-HSA-8954248, Golgi lumen
2 PAPSCHEBI:58339, C10H11N5O13P2S, Golgi lumen

Outputs

OSulf-Y97,118-PODXL2R-HSA-8954273, Golgi lumen
2 PAPCHEBI:58343, C10H11N5O10P2, Golgi lumen

Catalysed by

protein-tyrosine sulfotransferase activity of TPST1,2 [Golgi membrane]EC 2.8.2.20

Literature

Endoglycan, a member of the CD34 family, functions as an L-selectin ligand through modification with tyrosine sulfation and sialyl Lewis x J. Biol. Chem., 2003
Endoglycan, a member of the CD34 family of sialomucins, is a ligand for the vascular selectins J. Immunol., 2008
Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2 J. Am. Soc. Mass Spectrom., 2008
Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction Nat Commun, 2013
Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins Proc. Natl. Acad. Sci. U.S.A., 1998