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Literature summary for 3.2.1.166 extracted from

  • Pikas, D.S.; Li, J.P.; Vlodavsky, I.; Lindahl, U.
    Substrate specificity of heparanases from human hepatoma and platelets (1998), J. Biol. Chem., 273, 18770-18777.
    View publication on PubMed
Search for more literature for 3.2.1.166

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y251
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Source Tissue

Source Tissue Comment Organism Textmining
blood platelet
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 Homo sapiens
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SK-HEP-1 cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heparin octasaccharide + H2O cleavage of the single beta-D-glucuronidic linkage in a heparin-derived octasaccharide with high affinity for antithrombin Homo sapiens ?
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additional information a capsular polysaccharide from Escherichia coli K5, with the same (-GlcUA-(beta-1,4)-GlcNAc-(alpha-1,4)-)n structure as the unmodified backbone of heparan sulfate, resists heparanase degradation in its native state as well as after chemical N-deacetylation/N-sulfation or partial enzymatic C-5 epimerization of beta-D-GlcUA to alpha-L-idopyranuronic acid. By contrast, a chemically O-sulfated (but still N-acetylated) K5 derivative is susceptible to heparanase cleavage. O-Sulfate groups, but not N-sulfate or alpha-L-idopyranuronic acid residues are essential for substrate recognition by the heparanase. Selective O-desulfation of the heparin octasaccharide implicates a 2-O-sulfate group on a hexuronic acid residue located two monosaccharide units from the cleavage site, toward the reducing end Homo sapiens ?
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