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Literature summary for 3.4.24.87 extracted from

  • Pruss, C.M.; Notley, C.R.; Hegadorn, C.A.; OBrien, L.A.; Lillicrap, D.
    ADAMTS13 cleavage efficiency is altered by mutagenic and, to a lesser extent, polymorphic sequence changes in the A1 and A2 domains of von Willebrand factor (2008), Br. J. Haematol., 143, 552-558.
    View publication on PubMed

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
von Willebrand factor + H2O all alterations examined in the Y1605-M1606 cleavage site greatly reduce the cleavability of von Willebrand factor by ADAMTS13. Greatest cleavage resistance is observed in Y1605A/M1606A. Y1605H and M1606L show a loss of cleavability in the recombinant full-length von Willebrand factor assay, suggesting that an aromatic ring at 1605 is critical for ADAMTS13 recognition. The G1643S polymorphism shows increased cleavage, suggesting a type 2A von Willebrand factor phenotype, while D1472H, Q1571H and P1601T show slightly decreased ADAMTS13 cleavage. A-domain changes in von Willebrand factor alter ADAMTS13-mediated proteolysis Homo sapiens ?
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Synonyms

Synonyms Comment Organism
ADAMTS13
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Homo sapiens