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3.4.21.95: Snake venom factor V activator

This is an abbreviated version!
For detailed information about Snake venom factor V activator, go to the full flat file.

Word Map on EC 3.4.21.95

Reaction

Fully activates human clotting factor V by a single cleavage at the Trp-Tyr-Leu-Arg1545!Ser-Asn-Asn-Gly bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2 =

Synonyms

blood coagulation factor V-activating proteinase, coagulant serine proteinase, Factor V activator, Factor V-activating enzyme, Factor V-activating proteinase alpha, Factor V-activating proteinase gamma, FV activating enzymes, Human blood coagulation Factor V activating enzymes, LVV-V, Russell's viper venom factor V (FV) activator, Russell's viper venom factor V activator, RVV-V, RVV-Vgamma, Snake venom factor V activator alpha, Snake venom factor V activator gamma, VLCII, VLFVA, VSPF5

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.95 Snake venom factor V activator

Molecular Weight

Molecular Weight on EC 3.4.21.95 - Snake venom factor V activator

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26172
-
x * 26182, enzyme RVV-Valpha, x * 26172, enzyme RVV-Vgamma, six disulfide bridges, of which Cys74-Cys234 is unique to snake venom serine proteases, amino acid sequence
26182
-
x * 26182, enzyme RVV-Valpha, x * 26172, enzyme RVV-Vgamma, six disulfide bridges, of which Cys74-Cys234 is unique to snake venom serine proteases, amino acid sequence
27200
28000
-
x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
28400
-
gel filtration, MALDI-TOF mass spectrometry
29000
30000
-
1 * 30000, SDS-PAGE