Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of disintegrin domain mutants by site-directed mutagenesis, that exhibit dramatically reduced activity toward the von Willebrand factor fragment VWF115, comprising amino acid residues 1554-1668 of von Willebrand factor. The isolated metalloprotease domain of ADAMTS13 alone is ineffective in cleaving, but if the various noncatalytic domains are incrementally added back, proteolytic activity is gradually restored | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of ADAMTS13 disintegrin domain mutants with substrate VWF115, overview | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Homo sapiens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | required, three active sites His and catalytic residues Glu coordinate a catalytic Zn2+ ion | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
von Willebrand factor + H2O | Homo sapiens | - |
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | ADAMTS13 is a multidomain glycoprotein | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
plasma | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the positively charged Arg349 on ADAMTS13 appears to directly interact with the negatively charged Asp1614 on the von Willebrand factor-A2 domain. This seemingly weak interaction between the disintegrin and VWF-A2 appears to be essential for efficient catalysis of von Willebrand factor under static/denaturing conditions. Molecular modeling of the involvement of the disintegrin domain of ADAMTS13 in von Willebrand factor processing, overview | Homo sapiens | ? | - |
? | |
von Willebrand factor + H2O | - |
Homo sapiens | von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment | - |
? | |
von Willebrand factor + H2O | binding of all the proximal noncatalytic domains of ADAMTS13 to von Willebrand factor is necessary to position the active site of ADAMTS13 to the scissile bond, Tyr1605-Met1606, on von Willebrand factor, resulting in productive cleavage. The metalloprotease domain of ADAMTS13 alone is ineffective in cleaving von Willebrand factor, linear relationship between the domains of ADAMTS13 and von Willebrand factor proteolysis. All the proximal noncatalytic domains of ADAMTS13 are required for productive engagement with von Willebrand factor-A2 domain at least under static/denaturing conditions | Homo sapiens | von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment | - |
? | |
VWF115 + H2O | a von Willebrand factor-derived peptide substrate, comprising amino acid residues 1554-1668 of von Willebrand factor | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | ADAMTS13 is a multidomain glycoprotein. It consists of numerous domains including a metalloprotease domain, a disintegrin domain, first thrombospondin type 1 repeat, i.e. TSP1, a cysteine-rich domain, and a spacer domain, schematic domain structure model of ADAMTS13, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
ADAMTS13 | ADAMTS13 is a member of the a disintegrin and metalloprotease with thrombospondin type 1 repeats, i.e. ADAMTS, family | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | thrombotic thrombocytopenic purpura is a potentially fatal illness caused primarily by the absence of plasma ADAMTS13 proteolytic activity, as a result of ADAMTS13 mutations or acquired autoantibodies against ADAMTS13 enzyme | Homo sapiens |