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Literature summary extracted from

  • Wei, Z.; Lyon, M.; Gallagher, J.T.
    Distinct substrate specificities of bacterial heparinases against N-unsubstituted glucosamine residues in heparan sulfate (2005), J. Biol. Chem., 280, 15742-15748.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.7 Pedobacter heparinus
-
-
-
4.2.2.8 Pedobacter heparinus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.7 additional information heparinase I does not cleave at GlcNH3+ residues in partially de-N-sulfated forms of heparin Pedobacter heparinus ?
-
 ?
4.2.2.7 partially de-N-sulfated forms of heparin heparinase II Pedobacter heparinus (DELTA4,5-unsaturated hexuronic acid)-(N-unsubstituted glucosamine(6S)) + (DELTA4,5-unsaturated hexuronic acid(2S))-(N-unsubstituted glucosamine) + (DELTA4,5-unsaturated hexuronic acid(2S))-(N-unsubstituted glucosamine(6S))
-
 ?
4.2.2.8 partially de-N-sulfated forms of heparin heparinase III Pedobacter heparinus (DELTA4,5-unsaturated hexuronic acid)-(N-unsubstituted glucosamine)
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.2.7 heparinase I
-
 Pedobacter heparinus
4.2.2.7 heparinase II
-
 Pedobacter heparinus
4.2.2.8 heparinase III
-
 Pedobacter heparinus