Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.87 extracted from

  • Muia, J.; Zhu, J.; Gupta, G.; Haberichter, S.L.; Friedman, K.D.; Feys, H.B.; Deforche, L.; Vanhoorelbeke, K.; Westfield, L.A.; Roth, R.; Tolia, N.H.; Heuser, J.E.; Sadler, J.E.
    Allosteric activation of ADAMTS13 by von Willebrand factor (2014), Proc. Natl. Acad. Sci. USA, 111, 18584-18589.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.87

Activating Compound

Activating Compound Comment Organism Structure
additional information antibodies that recognize domains T67, T8, and CUB domains have additive effects. Binding activates ADAMTS13 up to 4.2fold at pH 7.4, but antibodies have markedly decreased effects on ADAMTS13 activity at pH 6 Homo sapiens
von Willebrand factor binding to substrate von Willebrand factor D4 allosterically activates ADAMTS13, increasing its catalytic activity. Binding also positions ADAMTS13 on the substrate where it can act rapidly when shear stress exposes the scissile bond in the adjacent A2 domain Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q76LX8
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FRETS-rVWF71 + H2O substrate based on von Willebrand factor residues Gln1599-Arg1668, with an N-terminal Gly and with mutations N1610C and K1617R. The N-terminus is modified with IRDye QC-1 Nhydroxysuccinimide ester, and Cys1610 is modified with DyLight 633 maleimide Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
physiological function the distal T8-CUB2 domains markedly inhibit substrate cleavage, and binding of von Willebrand factor or monoclonal antibodies to distal ADAMTS13 domains relieves this autoinhibition. Distal T-CUB domains interact with proximal MDTCS domains. ADAMTS13 is regulated by substrate-induced allosteric activation, which may optimize von Willebrand factor cleavage under fluid shear stress in vivo Homo sapiens