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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.

Heparanase (HPSE) cleaves heparan sulfate from its proteoglycan (lysosome)

H2O + HS/HPIN-PGs → IdoA-GlcN6S-IdoA2S-GlcN3S- group + GlcA-Gal-Gal-Xyl-HS proteins

Reactome: R-HSA-1667005
Compartment: lysosomal lumen
Rhea: None recorded

Inputs

H2OCHEBI:15377, H2O, lysosomal lumen
HS/HPIN-PGsR-HSA-2090050, lysosomal lumen

Outputs

IdoA-GlcN6S-IdoA2S-GlcN3S- groupCHEBI:747403, C47H68N2O56S5, lysosomal lumen
GlcA-Gal-Gal-Xyl-HS proteinsR-HSA-2076551, Golgi lumen

Catalysed by

heparanase activity of HPSE dimer [lysosomal lumen]EC 3.2.1.166

Literature

Human heparanase is localized within lysosomes in a stable form Exp Cell Res, 2002
Heterodimer formation is essential for heparanase enzymatic activity Biochem Biophys Res Commun, 2003
Structural recognition by recombinant human heparanase that plays critical roles in tumor metastasis. Hierarchical sulfate groups with different effects and the essential target disulfated trisaccharide sequence J Biol Chem, 2002
Human heparanase. Purification, characterization, cloning, and expression J Biol Chem, 1999