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Literature summary for 3.4.21.95 extracted from

  • Siigur, J.; Aaspollu, A.; Siigur, E.
    Biochemistry and pharmacology of proteins and peptides purified from the venoms of the snakes Macrovipera lebetina subspecies (2019), Toxicon, 158, 16-32 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloning from venom gland cDNA library, DNA and amino acid sequence determination and analysis Macrovipera lebetina

Inhibitors

Inhibitors Comment Organism Structure
diisopropylfluorophosphate
-
Macrovipera lebetina
PMSF
-
Macrovipera lebetina

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Macrovipera lebetina
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor V + H2O Macrovipera lebetina activation ?
-
?

Organism

Organism UniProt Comment Textmining
Macrovipera lebetina Q9PT41 turanica
-

Source Tissue

Source Tissue Comment Organism Textmining
venom toxin profile, overview Macrovipera lebetina
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 28400, SDS-PAGE Macrovipera lebetina

Synonyms

Synonyms Comment Organism
Factor V activator
-
Macrovipera lebetina
VLFVA
-
Macrovipera lebetina

pI Value

Organism Comment pI Value Maximum pI Value
Macrovipera lebetina above
-
9.3

General Information

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