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Literature summary for 3.4.21.74 extracted from
- Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom (2015), Biochimie, 109, 78-87 .
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | in standard experimental conditions 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(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination and analysis | Vipera ammodytes ammodytes |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Vipera ammodytes ammodytes | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vipera ammodytes ammodytes | A0A0B4U9L8 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme is a single-chain glycoprotein. Two consensus N-glycosylation sites are present in the sequence of VaF1, but the extent of its glycosylation is low, only 5.2% of the total molecular mass. Deglycosylation by peptide N-glycosidase F | Vipera ammodytes ammodytes |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from venom by cation exchange chromatography, dialysis, and anion exchange chromatography | Vipera ammodytes ammodytes |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| venom | - |
Vipera ammodytes ammodytes | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Collagen IV + H2O | partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? |  |
| factor X + H2O | low activity, the heavy chain of factor X is more susceptible to hydrolysis by VaF1 than the light chain whose hydrolysis is observed only after prolonged incubation, partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? | |
| Fibronectin + H2O | partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? | |
| Insulin B-chain + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| additional information | enzyme VaF1 degrades collagen IV, nidogen and fibronectin, components of the extracellular matrix in vitro, although with low efficacy and narrow specificity. Although VaF1 possesses a collagen-binding sequence in its disintegrin-like domain, VaF1 displays no effect on collagen-induced platelet aggregation in vitro. The two major coagulation factors, FX and prothrombin, and the fibrinolysis factor, plasminogen, are only partially hydrolysed by VaF1 in vitro. FX and plasminogen are degraded also very slowly. None of the degradation products detected by SDS-PAGE analysis has the same apparent molecular mass as the heavy chains of the activated factors, FXa, alpha-thrombin and plasmin, overview. No activity with laminin | Vipera ammodytes ammodytes | ? | - |
? | |
| plasminogen + H2O | low activity, partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? | |
| prothrombin + H2O | low activity, partial hydrolysis | Vipera ammodytes ammodytes | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 49700, about, mass spectrometry | Vipera ammodytes ammodytes |
| More | the typical P-IIIa subclass snake venom metalloproteinase VaF1 is composed of metalloproteinase domain, disintegrin-like domain, and cysteine-rich domain. Enzyme protein Edman sequencing and mass spectrometry | Vipera ammodytes ammodytes |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| metalloproteinase 1 | UniProt | Vipera ammodytes ammodytes |
| VaF1 | - |
Vipera ammodytes ammodytes |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Vipera ammodytes ammodytes |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Vipera ammodytes ammodytes |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Vipera ammodytes ammodytes | isoelectric focusing | - |
5.8 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | enzyme VaF1 is a high molecular mass metalloproteinase with alpha-fibrinogenolytic activity from nose-horned viper (Vipera ammodytes ammodytes) venom | Vipera ammodytes ammodytes |
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