Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of -Arg-/- bonds. Has no action on insulin B chain
Synonyms
rvv-x, snake venom protease, russell's viper venom factor x activator, more
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of -Arg-/- bonds. Has no action on insulin B chain
cleavage of a single internal Arg-Val peptide bond which leads to the formation of factor IXaalpha, a protein with the same molecular weight as the precursor, factor IXaalpha is composed of two polypeptide chains held together by a disulfide bond(s), and these two chains have an NH2-terminal sequence of Tyr-Asn-Ser-Gly- and Val-Val-Gly-Gly-
a protein with the same molecular weight as the precursor, factor IXaalpha is composed of two polypeptide chains held together by a disulfide bond(s), and these two chains have an NH2-terminal sequence of Tyr-Asn-Ser-Gly- and Val-Val-Gly-Gly-
activation by proteolytic cleavage of an Arg-Ile bond on the heavy chain of factor X which yields a small activation fragment with a molecular weight of 11000 and a large activation fragment (containing the active site serine) with a molecular weight of 44000
small activation fragment with a molecular weight of 11000 and a large activation fragment (containing the active site serine) with a molecular weight of 44000
the enzyme triggers the blood coagulation cascade, which results in an eye-visible phase transition, i.e. precipitation, of polystyrene microspheres bound to clotted fibrin, overview
Cys389 in the hyper-variable-region, residues 373-394, mediates the protein-protein interactions of the enzyme, Cys389 forms a disulfide bond with the C-terminal Cys133 of the enzyme's light-chain A
the enzyme triggers the blood coagulation cascade, which results in an eye-visible phase transition, i.e. precipitation, of polystyrene microspheres bound to clotted fibrin, overview
an allosteric RNA aptamer, secondary structure folding, overview, causes 87% inhibition of the enzyme in the RVV-X-SPZXa assay, using a chromogenic substrate for the activated factor X, releasing the chromophore, 4-nitroanilide acetate, the snake venom protease competes with the human or murine vascular endothelial growth factor, VEGF165, for binding to RNA132 and reverses the inhibitory activity of RNA132 on RVV-X and restores its enzymatic activity, the VEGF165 of zebrafish functions partially, mapping of binding sites, overview
determination of enzyme activity in the RVV-X-SPZXa assay, using a chromogenic substrate for the activated factor X, releasing the chromophore, 4-nitroanilide acetate
RVV-X is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains, it shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme by the sitting drop vapor diffusion method, mixing of 0.001 ml of protein solution with 0.001 ml of reservoir solution, containing 0.1M calcium acetate, 0.1M sodium cacodylate, 10% PEG 8000, pH 6.5, supplemented with one fifth volume of 10% PEG 3350, and equilibration against 1 ml of reservoir solution at 20°C, one week, cryoprotection with 15% 2-methyl-2,4-pentanediol in reservoir solution, X-ray diffraction structure determination and analysis at 2.9 A resolution, modeling
further purification of the commercial venom enzyme by CM-resin chromatography in presence of N-[(2R)-2-(hydroxamidocarbonyllethyl)-4-methylpentanoyl]-L-tryptophan methylamide
thrombin is a common hemostatic drug used in surgical practice. Investigation of a method with the optimum conditions for rapid preparation of thrombin from cryoprecipitate-depleted plasma using RVV-X
Coagulation factor X activating enzyme from Russells viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains