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Literature summary for 3.4.21.95 extracted from

  • Nakayama, D.; Ben Ammar, Y.; Takeda, S.
    Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell’s viper venom (2009), Acta Crystallogr. Sect. F, 65, 1306-1308.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with Pefabloc or D-Phe-Pro-Arg-chloromethylketone, sitting drop vapor diffusion method, using 0.8% (w/v) tryptone, 0.04 M Na HEPES pH 7.0 and 9.6% (w/v) PEG 3350 Daboia siamensis

Inhibitors

Inhibitors Comment Organism Structure
D-Phe-Pro-Arg-chloromethylketone
-
Daboia siamensis
pefabloc 4-(2-aminoethyl)-benzenesulfonyl fluoride Daboia siamensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
SDS-PAGE Daboia siamensis

Organism

Organism UniProt Comment Textmining
Daboia siamensis
-
Russell's viper
-

Purification (Commentary)

Purification (Comment) Organism
Resource S column chromatography and Sephacryl S-100 gel filtration Daboia siamensis

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Daboia siamensis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor V + H2O specifically activates factor V by cleaving a single peptide bond between Arg1545 and Ser1546 Daboia siamensis ?
-
?

Synonyms

Synonyms Comment Organism
blood coagulation factor V-activating proteinase
-
Daboia siamensis
RVV-V
-
Daboia siamensis