Application | Comment | Organism |
---|---|---|
medicine | in standard experimental conditions, enzyme VaF1 is not recognised by antiserum against the whole venom, so it can contribute to postserotherapy complications, such as ineffective blood coagulation, in the envenomed patient | Vipera ammodytes ammodytes |
Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis | Vipera ammodytes ammodytes |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | pre-incubation of the enzyme with EDTA blocks the fibrinogenolytic activity | Vipera ammodytes ammodytes | |
additional information | pefabloc, an inhibitor of serine proteases, has no effect on the enzyme proteolytic activity | Vipera ammodytes ammodytes |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Vipera ammodytes ammodytes | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
49735 | - |
1 * 49735, mass spectrometry, SDS-PAGE and native PAGE | Vipera ammodytes ammodytes |
49740 | - |
mass spectrometry, SDS-PAGE and native PAGE | Vipera ammodytes ammodytes |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
factor X + H2O | Vipera ammodytes ammodytes | partial hydrolysis | ? | - |
? | |
Human fibrinogen + H2O | Vipera ammodytes ammodytes | - |
? | - |
? | |
additional information | Vipera ammodytes ammodytes | hydrolysis of fibrinogen, factor X, prothrombin and plasminogen, plasma proteins involved in blood coagulation | ? | - |
? | |
plasminogen + H2O | Vipera ammodytes ammodytes | partial hydrolysis | ? | - |
? | |
prothrombin + H2O | Vipera ammodytes ammodytes | partial hydrolysis | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vipera ammodytes ammodytes | A0A0B4U9L8 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | the enzyme contains two consensus N-glycosylation sites, the extent of its glycosylation is 5.2% of the total molecular mass. Deglycosylation by peptide N-glycosidase F. Deglycosylation reduces the molecular weight by 3.0 kDa | Vipera ammodytes ammodytes |
Purification (Comment) | Organism |
---|---|
native enzyme by several steps including cation exchange chromatography, dialysis and anion exchange chromatography | Vipera ammodytes ammodytes |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Cleavage of the Lys413-/-Leu414 bond of alpha-chain of human fibrinogen. Cleavage of Ala14-/-Leu15 and Tyr16-/-Leu17 in insulin B chain. Non-hemorrhagic proteinase | no cleavage of fibrin, fibrinogen beta-chain or fibrinogen gamma-chain | Vipera ammodytes ammodytes |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
venom | - |
Vipera ammodytes ammodytes | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
bovine factor X + H2O | slow degradation. The heavy chain offactor X is more susceptible to hydrolysis by the enzyme than the light chain whose hydrolysis is observed only after prolonged incubation | Vipera ammodytes ammodytes | ? | - |
? | |
bovine fibronectin + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
bovine plasminogen + H2O | slow degradation. Very limited proteolysis, giving rise to multiple products with molecular masses between 40 and 60 kDa | Vipera ammodytes ammodytes | ? | - |
? | |
bovine prothrombin + H2O | slow degradation. Two major cleavage products, of 60 and 28 kDa, accumulate after extended incubation. N-terminal sequencing shows them to be prethrombin-1 and fragment 1, indicating the cleavage of prothrombin at the Ser157-/-Gly158 bond | Vipera ammodytes ammodytes | ? | - |
? | |
factor X + H2O | partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? | |
Human fibrinogen + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
human fibrinogen alpha-chain + H2O | cleavage of the Lys413-/-Leu414 bond of alpha-chain of fibrinogen. Fibrinogen beta- and gamma-chains remain intact even after 3 h incubation | Vipera ammodytes ammodytes | ? | - |
? | |
human type collagen IV + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
insulin B chain + H2O | cleavage of two peptide bonds is detected, Ala14-/-Leu15 and Tyr16-/-Leu17 | Vipera ammodytes ammodytes | ? | - |
? | |
additional information | hydrolysis of fibrinogen, factor X, prothrombin and plasminogen, plasma proteins involved in blood coagulation | Vipera ammodytes ammodytes | ? | - |
? | |
additional information | non-hemorrhagic proteinase. No degradation of fibrin. Laminin resists hydrolysis by the enzyme, even after 24 h incubation | Vipera ammodytes ammodytes | ? | - |
? | |
Nidogen + H2O | hydrolysis at the Ser322-/-Phe323 bond | Vipera ammodytes ammodytes | ? | - |
? | |
plasminogen + H2O | partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? | |
prothrombin + H2O | partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 49735, mass spectrometry, SDS-PAGE and native PAGE | Vipera ammodytes ammodytes |
Synonyms | Comment | Organism |
---|---|---|
VaF1 | - |
Vipera ammodytes ammodytes |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Vipera ammodytes ammodytes |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Vipera ammodytes ammodytes |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Vipera ammodytes ammodytes | isoelectric focussing | - |
5.8 |