Cloned (Comment) | Organism |
---|---|
cloning from venom gland cDNA library, DNA and amino acid sequence determination and analysis | Macrovipera lebetina |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diisopropylfluorophosphate | - |
Macrovipera lebetina | |
PMSF | - |
Macrovipera lebetina |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Macrovipera lebetina | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
factor V + H2O | Macrovipera lebetina | activation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Macrovipera lebetina | Q9PT41 | turanica | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
venom | toxin profile, overview | Macrovipera lebetina | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Benzoylarginine ethyl ester + H2O | - |
Macrovipera lebetina | ? | - |
? | |
factor V + H2O | activation | Macrovipera lebetina | ? | - |
? | |
additional information | enzyme VLFVA hydrolyses several synthetic arginine ester substrates, such as benzoylarginine ethyl ester (BAEE), tosylarginine methyl ester (TAME) and amide substrates such as Pro-Phe-Arg-MCA | Macrovipera lebetina | ? | - |
? | |
Pro-Phe-Arg-7-amido-4-methyl coumarin + H2O | - |
Macrovipera lebetina | Pro-Phe-Arg + 7-amino-4-methyl coumarin | - |
? | |
tosylarginine methyl ester + H2O | - |
Macrovipera lebetina | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 28400, SDS-PAGE | Macrovipera lebetina |
Synonyms | Comment | Organism |
---|---|---|
Factor V activator | - |
Macrovipera lebetina |
VLFVA | - |
Macrovipera lebetina |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Macrovipera lebetina | above | - |
9.3 |
General Information | Comment | Organism |
---|---|---|
evolution | the amino acid sequence of VLFVA shows significant homology with snake venom and mammalian serine proteinases. The other sequences (VLP2, VLP3 and VLP4) are homologous to VLFVA, but have two principal discrepancies in the translated protein sequence in comparison with snake venom serine protease structures: in the active site triad Ser195 is replaced by Asn195 and His57 by Arg57. Sequences of VLP3 and VLP4 represent combinations of VLFVA and VLP2 clones | Macrovipera lebetina |
metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina |
physiological function | the enzyme VLFVA has the ability to activate factor V | Macrovipera lebetina |