Biology:ADAMTS13 endopeptidase
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Short description: Class of enzymes
| ADAMTS13 endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.87 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
ADAMTS13 endopeptidase (EC 3.4.24.87, ADAMTS VWF cleaving metalloprotease, ADAMTS-13, ADAMTS13, vWF-cleaving protease, VWF-CP, vWF-degrading protease, Upshaw factor, von Willebrand factor cleaving protease, ADAMTS13 peptidase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- The enzyme cleaves the von Willebrand factor at bond Tyr842-Met843 within the A2 domain
This enzyme belong in the peptidase family M12.
References
- ↑ "Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family". Blood 98 (6): 1662–6. September 2001. doi:10.1182/blood.v98.6.1662. PMID 11535495.
- ↑ "ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions". Blood 100 (12): 4033–9. December 2002. doi:10.1182/blood-2002-05-1401. PMID 12393397.
External links
- ADAMTS13+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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