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Literature summary for 3.4.24.87 extracted from

  • de Groot, R.; Lane, D.A.; Crawley, J.T.
    The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity (2010), Blood, 116, 3064-3072.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.87

Protein Variants

Protein Variants Comment Organism
D187A the mutant shows 10fold reduced catalytic efficiency against von Willebrand factor 115 compared to the wild type enzyme Homo sapiens
D252N the ADAMTS13 VR2 single-point mutant is secreted as the wild type enzyme Homo sapiens
E184A the mutant exhibits wild type activity Homo sapiens
E184A/L185A/D187A/R190A the proteolytic function of the mutant is severely affected Homo sapiens
E184A/L185A/D187A/R190A/Q191A/V192N/R193A the mutant has abolished activity against von Willebrand factor 115 Homo sapiens
L185A the mutant exhibits wild type activity Homo sapiens
L218A the ADAMTS13 VR2 single-point mutant is secreted poorly Homo sapiens
Q191A the mutant exhibits wild type activity Homo sapiens
Q197A the mutant exhibits wild type activity Homo sapiens
R190A the mutant shows 2fold reduced catalytic efficiency against von Willebrand factor 115 compared to the wild type enzyme Homo sapiens
R193A the mutant shows 4fold reduced catalytic efficiency against von Willebrand factor 115 compared to the wild type enzyme Homo sapiens
R257A the ADAMTS13 VR2 single-point mutant is secreted as the wild type enzyme Homo sapiens
S251A the ADAMTS13 VR2 single-point mutant is secreted poorly Homo sapiens
T196A the mutant exhibits wild type activity Homo sapiens
T260A the ADAMTS13 VR2 single-point mutant is secreted as the wild type enzyme Homo sapiens
V192N the mutant exhibits wild type activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00065
-
 von Willebrand factor 115 wild type enzyme, in 20 mM Tris-HCl (pH 7.8), 150 mM NaCl, 5 mM CaCl2, at 37°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the active site contains zinc Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
von Willebrand factor 115 + H2O Homo sapiens von Willebrand factor is cleaved at the Tyr1605-Met1606 bond in the von Willebrand factor A2 domain 10000 Da fragment of von Willebrand factor 115 + 7000 Da fragment of von Willebrand factor 115
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
von Willebrand factor 115 + H2O von Willebrand factor is cleaved at the Tyr1605-Met1606 bond in the von Willebrand factor A2 domain Homo sapiens 10000 Da fragment of von Willebrand factor 115 + 7000 Da fragment of von Willebrand factor 115
-
 ?

Synonyms

Synonyms Comment Organism
ADAMTS13
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.52
-
 von Willebrand factor 115 wild type enzyme, in 20 mM Tris-HCl (pH 7.8), 150 mM NaCl, 5 mM CaCl2, at 37°C Homo sapiens

General Information

General Information Comment Organism
physiological function ADAMTS13 modulates von Willebrand factor platelet-tethering function by proteolysis Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
821
-
 von Willebrand factor 115 wild type enzyme, in 20 mM Tris-HCl (pH 7.8), 150 mM NaCl, 5 mM CaCl2, at 37°C Homo sapiens