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Literature summary for 3.4.21.95 extracted from

  • Kisiel, W.; Canfield, W.M.
    Snake venom proteases that activate blood-coagulation factor V (1981), Methods Enzymol., 80, 275-285.
    View publication on PubMed
Search for more literature for 3.4.21.95

General Stability

General Stability Organism
stable to repeated freezing and thawing Daboia russelii

Inhibitors

Inhibitors Comment Organism Structure
diisopropyl fluorophosphate
-
 Daboia russelii
diisopropylfluorophosphate
-
 Daboia russelii

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Daboia russelii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ mediates the interaction of factor V to factor Va Daboia russelii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27200
-
 x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions Daboia russelii
27200
-
 1 * 27200, Vipera russelli, sedimentation equilibrium under denaturing conditions Daboia russelii
28000
-
 x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions Daboia russelii
29000
-
 x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions Daboia russelii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Clotting factor V + H2O Daboia russelii
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Daboia russelii
-
 Russell's viper
-
Daboia russelii
-
 factor V activator is separated from factor X activator by gel filtration
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 6% carbohydrate Daboia russelii

Purification (Commentary)

Purification (Comment) Organism
-
 Daboia russelii

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Daboia russelii
-
venom lyophilized Daboia russelii
-

Storage Stability

Storage Stability Organism
-70°C to 50°C, procoagulant activity stable Daboia russelii
4°C, 50 mM Tris-HCl, pH 7.5, 0.02% NaN3, protein concentration 0.5-1.5 mg/ml Daboia russelii
4°C, 50 mM Tris-HCl, pH 7.5, containing 0.02% NaN3 at protein concentration of 0.2 mg/ml, procoagulant activity remains constant for several months Daboia russelii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Benzoyl-L-Arg ethyl ester + H2O
-
 Daboia russelii Benzoyl-L-Arg + ethanol
-
 ?
Clotting factor V + H2O clotting factor V of human and bovine origin, no other protein substrate, not rabbit clotting factor V Daboia russelii Clotting factor Va cleavage of a single peptide bond, Va is composed of a heavy chain of MW 230000 and a light chain of MW 80000 ?
Clotting factor V + H2O
-
 Daboia russelii ?
-
 ?
Factor V + H2O cleavage of a single internal peptide bond, human and bovine factor V, not: rabbit factor V, human or bovine factor VIII, bovine fibrinogen, bovine prothrombin Daboia russelii Factor Va composed of a heavy chain, MW 230000, and a light chain, MW 80000. The heavy chain and the light chain are noncovalently associated in solution ?
L-Phe-pipecolyl-L-Arg 4-nitroanilide + H2O
-
 Daboia russelii L-Phe-pipecolyl-L-Arg + 4-nitrolaniline
-
 ?
additional information hydrolyzes arginine esters, such as benzoyl-Arg ethyl ester and tosyl-Arg methyl ester Daboia russelii ?
-
 ?
Tosyl-L-Arg methyl ester + H2O
-
 Daboia russelii Tosyl-L-Arg + methanol
-
 ?

Subunits

Subunits Comment Organism
? x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions Daboia russelii
monomer 1 * 27200, Vipera russelli, sedimentation equilibrium under denaturing conditions Daboia russelii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-70 50
-
 Daboia russelii
85
-
 60 min, 50% loss of activity Daboia russelii
85
-
 60 min, enzyme retains approximately 50% of its coagulant and esterase activity Daboia russelii