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3.4.24.87: ADAMTS13 endopeptidase

This is an abbreviated version!
For detailed information about ADAMTS13 endopeptidase, go to the full flat file.

Word Map on EC 3.4.24.87

Reaction

The enzyme cleaves the von Willebrand factor at bond Tyr842-/-Met843 within the A2 domain =

Synonyms

a disintegrin and metalloprotease with thrombospondin motifs 13, a disintegrin and metalloprotease with thrombospondin type 1 repeats 13, a disintegrin and metalloprotease with thrombospondin-13, a disintegrin and metalloproteinase with a thrombonspondin type 1 motif member 13, a disintegrin and metalloproteinase with a thrombospondin motif repeats 13, a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13, a disintegrin-like and metalloprotease with thrombospondin type I repeats – 13, a disintegrin-like and metalloprotease with thrombospondin type-1 motifs 13, a disintegrin-like and metalloproteinase domain with thrombospondin type I motifs 13, a disintegrin-like and metalloproteinase with thrombospondin type-1 motifs 13, a disintegrin-like domain and metalloprotease with thrombospondin type I motif, a thrombospondin type 1 motif, member 13, ADAMTS 13, ADAMTS VWF cleaving metalloprotease, ADAMTS-13, ADAMTS13, ADAMTS13 metalloprotease, M12.241, metalloprotease ADAMTS-13, More, plasma metalloprotease ADAMTS13, plasma von Willebrand factor cleaving activity, Upshaw factor, van Willebrand factor processing activity, von Willebrand cleavage protease, von Willebrand cleavaging protease, von Willebrand factor cleaving protease, von Willebrand factor specific cleaving protease, von Willebrand factor-cleaving metalloprotease, von Willebrand factor-cleaving protease, von Willebrand factor-cleaving proteinase, von-Willebrand factor cleaving protease, von-Willebrand factor degrading protease, von-Willebrand-factor-cleaving protease, VWF cleaving metalloprotease, VWF cleaving protease, vWF protease, VWF-cleaving metalloprotease, vWF-cleaving protease, VWF-CP, vWF-degrading protease, VWFCP, xWF-CP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.87 ADAMTS13 endopeptidase

Inhibitors

Inhibitors on EC 3.4.24.87 - ADAMTS13 endopeptidase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
activity can be restored by Ca2+
Ca2+
enzyme catalytic activity in blood plasma is tuned by varying buffer calcium, with lower divalent ion concentrations enhancing cleavage
citrate
-
weak
Cl-
-
Chloride ions inhibit von Willebrand factor hydrolysis by ADAMTS-13 of the A1-A2-A3 and A1-A2 domains in the presence of either urea or high shear stress, whereas this effect is either absent or negligible when using A2 and A2-A3 domains
CoCl2
-
an increasing concentration of CoCl2 inhibits ADAMTS13 activity
H2O2
treatment with 25 nM myeloperoxidase plus 50 microM H2O2 reduces ADAMTS13 activity by >85%. Residues Met249, Met331, and Met496 in important functional domains of ADAMTS13 are oxidized to methionine sulfoxide in an HOCl concentration-dependent manner
heparin
-
inhibits ADAMTS13 activity through inhibition of enzyme binding to endothelial cell surfaces, overview
HOCl
-
HOCl can oxidize methionine to methionine sulfoxide and tyrosine to chlorotyrosine, oxidation of VWF A2 peptide, at Met1606 and Tyr1605, markedly impairs ADAMTS13 cleavage. Oxidative modification by myeloperoxidase/H2O2 is similar to that produced by HOCl
Mn2+
-
ADAMTS13 activity is decreased in the presence of 0.9 mM Ni2+
MnSO4
-
an increasing concentration of MnSO4 inhibits ADAMTS13 activity
N-ethylmaleimide
-
slow and weak inhibition
Ni2+
-
ADAMTS13 activity is markedly decreased in the presence of 0.9 mM Ni2+
NiSO4
-
an increasing concentration of NiSO4 inhibits ADAMTS13 activity
peroxynitrite
-
formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13 a prothrombotic mechanism in diseases associated with oxidative stress, overview. Oxidation by peroxynitrite of purified VWF multimers inhibits ADAMTS-13 hydrolysis, but does not alter their electrophoretic pattern nor their ability to induce platelet agglutination by ristocetin. In vitro treatment of ADAMTS-13 with peroxynitrite over a concentration ranging from 0.050 to 0.250 mM causes a complete inhibition of the protease activity of the enzyme
plasma from patients with thrombotic thrombocytopenic purpurea
-
-
-
Pro-1645-Lys-1668 fragment of von Willebrand factor 73
-
-
-
Trypsin
-
inhibits ADAMTS13 activity through inhibition of enzyme binding to endothelial cell surfaces, overview
-
VWFA2 domain
-
a C-terminal 32 kDa fragment of VWF, soluble VWFA2 domain effectively inhibits the binding of ADAMTS13 to immobilized VWFA2, and completely inhibits the interaction between ADAMTS13 and immobilized 64 kDa VWFA1A2A3 fragment
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W688X6-1
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the monoclonal antibody W688X6-1 shows dose-dependent inhibitory activity toward ADAMTS13-mediated hydrolysis
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WH2-22-1A
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the monoclonal antibody WH2-22-1A shows dose-dependent inhibitory activity toward ADAMTS13-mediated hydrolysis
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Z-Phe-Phe-CHN2
-
best peptidyl diazomethyl ketone inhibitor
additional information
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