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Literature summary for 3.2.1.166 extracted from
- Multi-faceted substrate specificity of heparanase (2013), Matrix Biol., 32, 223-227.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| heparan sulfate + H2O | Mammalia | heparanase is a strict endo-beta-glucuronidase with no exolytic glucuronidase activity. The enzyme only cleaves the glycosidic bond in the middle of the substrate. Heparan sulfate is a polysaccharide that has the disaccharide repeating unit of glucuronic acid or iduronic acid and glucosamine. Certain parts of heparan sulfate are occupied by the repeating disaccharide of -GlcA-GlcNAc-, known as the lowly sulfated domain. Other parts of HS are dominated by the highly sulfated disaccharide repeating unit of GlcA-GlcNS3S6S-IdoA2SGlcNS6S-, known as highly sulfated domain, overview | ? | - |
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Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mammalia | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| heparan sulfate + H2O | heparanase is a strict endo-beta-glucuronidase with no exolytic glucuronidase activity. The enzyme only cleaves the glycosidic bond in the middle of the substrate. Heparan sulfate is a polysaccharide that has the disaccharide repeating unit of glucuronic acid or iduronic acid and glucosamine. Certain parts of heparan sulfate are occupied by the repeating disaccharide of -GlcA-GlcNAc-, known as the lowly sulfated domain. Other parts of HS are dominated by the highly sulfated disaccharide repeating unit of GlcA-GlcNS3S6S-IdoA2SGlcNS6S-, known as highly sulfated domain, overview | Mammalia | ? | - |
? | |
| heparan sulfate + H2O | isolated from Escherichia coli K5 strain. heparanase is a strict endo-beta-glucuronidase with no exolytic glucuronidase activity. The enzyme only cleaves the glycosidic bond in the middle of the substrate. Second, heparanase not only cleaves the linkages of -GlcA-GlcNS6S-, but also degrades the linkage of -GlcA-GlcNAc6S. Third, the enzyme does not uniformly cleave the linkages of -GlcA-GlcNS6S-. Depending on the trisaccharide sequence at the nonreducing end of the nonasaccharide substrates, heparanase is able to choose to cleave the subsequent nonreducing end linkage of -GlcA-GlcNS6S- in the substrate or leave it intact. This unique observation suggests that heparanase displays two cleavage modes: consecutive cleavage and gapped cleavage. In the consecutive mode, heparanase cleaves the nonreducing trisaccharide at Step 1 digestion, and then cleaves the linkage between Residues 5 and 6 at Step 2 digestion. In the gapped cleavage, heparanase also cleaves the trisaccharide from the nonreducing end at Step 1 digestion, and then cleaves the linkage between Residues 7 and 9 | Mammalia | ? | - |
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General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | each cell has a dynamic control over the exact sequence of heparan sulfate and can change the way they respond to growth factors by altering the structure of the heparan sulfate on their surfaces. To accommodate those structural variations in heparan sulfate, heparanase adapts itself to recognize the overall structure of heparan sulfate, especially those highly sulfated domains in heparan sulfate.The substrate specificity plays a critical role in dissecting the biological functions of heparanase and heparan sulfate. Heparanase is capable of varying its substrate specificities depending on the saccharide structures around the cleavage site, overview. Potential regulating role of the surrounding saccharide sequences in controlling the cleavage site and the degradation extent by the enzyme | Mammalia |
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