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Literature summary extracted from

  • Raman, K.; Kuberan, B.
    Differential effects of heparitinase I and heparitinase III on endothelial tube formation in vitro (2010), Biochem. Biophys. Res. Commun., 398, 191-193.
    View publication on PubMedView publication on EuropePMC

Organism

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

EC Number Source Tissue Comment Organism Textmining
4.2.2.7 additional information propagated in bovine lung microvascular endothelial cells Pedobacter heparinus
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4.2.2.8 additional information propagated in bovine lung microvascular endothelial cells Pedobacter heparinus
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Synonyms

EC Number Synonyms Comment Organism
4.2.2.7 Hep III
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 Pedobacter heparinus
4.2.2.7 heparin lyase
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 Pedobacter heparinus
4.2.2.7 heparitinase III
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 Pedobacter heparinus
4.2.2.8 Hep I
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 Pedobacter heparinus
4.2.2.8 heparin lyase
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 Pedobacter heparinus
4.2.2.8 heparitinase I
-
 Pedobacter heparinus

General Information

EC Number General Information Comment Organism
4.2.2.7 physiological function differential effects of heparitinase I, EC 4.2.2.8, and heparitinase III on endothelial tube formation. The enzymes inhibit tube formation and reduce tumor-derived neovascularization in vivo by reducing bFGF binding and subsequent signaling, HepIII has a stronger effect than Hep I. Heparitinases, isolated from Flavobacterium heparinum, cleave heparan sulfate chains at defined locations, Hep III cleaves near sulfated iduronic acid residues and at highly sulfated regions. Hep III therefore may disrupt the growth factor binding domains that are important for angiogenesis Pedobacter heparinus
4.2.2.8 physiological function differential effects of heparitinase I and heparitinase III, EC 4.2.2.7, on endothelial tube formation. The enzymes inhibit tube formation and reduce tumor-derived neovascularization in vivo by reducing bFGF binding and subsequent signaling, HepIII has a stronger effect than Hep I. Heparitinases, isolated from Flavobacterium heparinum, cleave heparan sulfate chains at defined locations, Hep I cleaves heparin sulfate chains containing glucuronic acid residues adjacent to glucosamine residues containing either N-acetyl or N-sulfate groups. Hep I generates fragments that retain their growth factor binding capability and therefore still potentiate tube formation Pedobacter heparinus