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Literature summary for 3.2.1.166 extracted from
- Chemical shift assignments and secondary structure of the surrogate domain for drug discovery studies of human heparanase (2014), Biomol. NMR Assign., 9, 15-19.
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is a very attractive target in drug discovery | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of an N-terminally His-tagged truncated enzyme form, residues 36-543, containing a TEV protease cleavage site, in Escherichia coli strain BL21-CodonPlus (DE3)-RIL | Homo sapiens |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 8000 | - |
1 * 45000, glycosylated subunit formed by residues Lys158-Ile543, + 1 * 8000, formed by residues Gln36-Glu109, SDS-PAGE | Homo sapiens |
| 45000 | - |
1 * 45000, glycosylated subunit formed by residues Lys158-Ile543, + 1 * 8000, formed by residues Gln36-Glu109, SDS-PAGE | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His-tagged truncated enzyme form from Escherichia coli strain BL21-CodonPlus (DE3)-RIL by nickel affinity chromatography and dialysis | Homo sapiens |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | 1 * 45000, glycosylated subunit formed by residues Lys158-Ile543, + 1 * 8000, formed by residues Gln36-Glu109, SDS-PAGE | Homo sapiens |
| More | chemical shift assignments, secondary structure and chemical shift deviations from random coil of the domain of human heparanase comprising residues Lys158-Lys417, overview | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | residues Glu225 and Glu343 are critical in its catalytic mechanism. Two heparan sulfate binding sites are formed by Lys158-Asp171 and Gln270-Lys280 | Homo sapiens |
| physiological function | heparanase is an endoglycosidase that specifically degrades heparan sulfate, one of the main components of the extracellular matrix. Heparanase is implicated in cancer processes such as tumour formation, angiogenesis and metastasis | Homo sapiens |
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