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Literature summary for 3.4.24.73 extracted from

  • Moura-da-Silva, A.M.; Ramos, O.H.; Baldo, C.; Niland, S.; Hansen, U.; Ventura, J.S.; Furlan, S.; Butera, D.; Della-Casa, M.S.; Tanjoni, I.; Clissa, P.B.; Fernandes, I.; Chudzinski-Tavassi, A.M.; Eble, J.A.
    Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases (2008), Biochimie, 90, 484-492.
    View publication on PubMed
Search for more literature for 3.4.24.73

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bothrops jararaca
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is a P-III snake venom metalloproteinase Bothrops jararaca

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Fibrinogen + H2O Bothrops jararaca
-
 ?
-
 ?
additional information Bothrops jararaca the enzyme is a hemorrhagic P-III snake venom metalloproteinase, collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases, the multidomain enzyme binds to collagen via disintegrin-like and cysteine-rich domains allocate motifs that enable catalytic degradation of extracellular matrix components leading to disruption of capillary vessels ?
-
 ?
Type I collagen + H2O Bothrops jararaca
-
 ?
-
 ?
von Willebrand factor + H2O Bothrops jararaca
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bothrops jararaca P30431
-
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Bothrops jararaca
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fibrinogen + H2O
-
 Bothrops jararaca ?
-
 ?
Fibrinogen + H2O bovine substrate Bothrops jararaca ?
-
 ?
additional information the enzyme is a hemorrhagic P-III snake venom metalloproteinase, collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases, the multidomain enzyme binds to collagen via disintegrin-like and cysteine-rich domains allocate motifs that enable catalytic degradation of extracellular matrix components leading to disruption of capillary vessels Bothrops jararaca ?
-
 ?
additional information the enzyme inhibits collagen-induced platelet aggregation with an IC50 value of 300 nM Bothrops jararaca ?
-
 ?
Type I collagen + H2O
-
 Bothrops jararaca ?
-
 ?
Type I collagen + H2O bovine and chicken substrates, the enzyme binds with high affinity to the intact triple helix collagen structure affecting the collagen suprastructure Bothrops jararaca ?
-
 ?
von Willebrand factor + H2O
-
 Bothrops jararaca ?
-
 ?

Subunits

Subunits Comment Organism
More three-dimensional structure of jararhagin, structure-function relationship, molecular modeling and dynamics, comparison to berythractivase, overview Bothrops jararaca

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bothrops jararaca

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Bothrops jararaca