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Literature summary extracted from

  • Gao, W.; Anderson, P.J.; Sadler, J.E.
    Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity (2008), Blood, 112, 1713-1719.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.87 delQ1624-R1641 mutation minimally affects the rate of cleavage Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.87 von Willebrand factor + H2O Homo sapiens ADAMTS13 efficiently cleaves only the Tyr842-Met843 bond within the central A2 domain of multimeric von Willebrand factor (i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275) ?
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Organism

EC Number Organism UniProt Comment Textmining
3.4.24.87 Homo sapiens Q76LX8 recombinant
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.87 von Willebrand factor + H2O ADAMTS13 efficiently cleaves only the Tyr842-Met843 bond within the central A2 domain of multimeric von Willebrand factor (i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275) Homo sapiens ?
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 ?
3.4.24.87 von Willebrand factor + H2O ADAMTS13 efficiently cleaves only the Tyr842-Met843 bond within the central A2 domain of multimeric von Willebrand factor (i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275). This specificity depends in part on binding of the noncatalytic ADAMTS13 spacer domain to the C-terminal alpha-helix of von Willebrand factor domain A2. By kinetic analysis of recombinant ADAMTS13 constructs, it is shown that the first thrombospondin-1, Cys-rich, and spacer domains of ADAMTS13 interact with segments of von Willebrand factor domain A2 between Gln1624 and Arg1668 (in von Willebrand factor UniProt Id P04275), and together these exosite interactions increase the rate of substrate cleavage by at least approximately 300fold. Specific recognition of von Willebrand factor depends on cooperative, modular contacts between several ADAMTS13 domains and discrete segments of von Willebrand factor domain A2. Specification of the cleavage site depends on sequences flanking the scissile bond between positions P9 (Arg1597) and P18' (Ile1623) Homo sapiens ?
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Synonyms

EC Number Synonyms Comment Organism
3.4.24.87 ADAMTS13
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 Homo sapiens