Literature summary 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.

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.24.87	Homo sapiens	Q76LX8	recombinant	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.4.24.87	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	?	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
3.4.24.87	ADAMTS13	-	Homo sapiens

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Release 2023.1 (January 2023)