Information on EC 3.4.24.58 - russellysin

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The expected taxonomic range for this enzyme is: Viperidae

EC NUMBER
COMMENTARY
3.4.24.58
-
RECOMMENDED NAME
GeneOntology No.
russellysin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Blood-coagulation factor X activating enzyme
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-
-
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EC 3.4.21.23
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formerly
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Metalloproteinase RVV-x
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Proteinase, Vipera russelli
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-
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Russell's viper blood coagulation factor X activator
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Russell's viper venom factor X activator, RVV-X
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-
-
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Russell`s viper venom coagulation factor X-activating enzyme
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Russell’s viper venom factor X activator
Daboia russellii
-
-
RVV-V
-
-
-
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RVV-X
Daboia russellii
-
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snake venom protease
Daboia russellii
-
-
CAS REGISTRY NUMBER
COMMENTARY
79393-92-3
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Daboia russellii
-
-
-
Manually annotated by BRENDA team
Daboia russellii
factor V activator is separated from factor X activator by gel filtration
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coagulation factor IX + H2O
?
show the reaction diagram
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cleavage at the Arg-Xaa bond
-
-
?
coagulation factor X + H2O
?
show the reaction diagram
-
cleavage at the Arg-Ile bond
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-
?
Factor IX + H2O
Factor IXaalpha
show the reaction diagram
Daboia russellii
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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-
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Factor V + H2O
Factor Va
show the reaction diagram
Daboia russellii
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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
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
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Factor X + H2O
A small activation fragment + a large activation fragment
show the reaction diagram
Daboia russellii
-
not
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-
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Factor X + H2O
A small activation fragment + a large activation fragment
show the reaction diagram
Daboia russellii
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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
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factor X + H2O
factor Xa + propeptide of factor Xa
show the reaction diagram
Daboia russellii
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-
-
-
?
o-aminobenzoyl-Gly-Phe-Arg-Leu-Leu-2,4-dinitroanilinoethylamide + H2O
?
show the reaction diagram
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-
-
-
?
protein C + H2O
?
show the reaction diagram
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cleavage at the Arg-Xaa bond
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-
?
factor X + H2O
factor Xa + propeptide of factor Xa
show the reaction diagram
Daboia russellii
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docking model for factor X, overview
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-
?
additional information
?
-
Daboia russellii
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no hydrolysis of: L-Phe-L-Phe, L-Phe-Gly, N-benzyloxycarbonyl-Gly-L-Phe, N-benzyloxycarbonyl-Gly-L-Phe-NH2, Gly-L-Phe-L-Phe, N-benzyloxycarbonyl-Glu-L-Tyr, benzoyl-L-Arg-NH2, L-Leu-Gly, Gly-L-Phe, Gly-L-Phe-NH2, hippuryl-L-Phe, B-chain of bovine insulin
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-
-
additional information
?
-
Daboia russellii
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hydrolyzes arginine esters, such as benzoyl-Arg ethyl ester and tosyl-Arg methyl ester
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-
-
additional information
?
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Daboia russellii
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potently inhibits collagen-stimulated and ADP-stimulated platelet aggregation
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-
-
additional information
?
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no action on the B chain of insulin
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-
?
additional information
?
-
Daboia russellii
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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
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-
-
additional information
?
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Daboia russellii
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Daboia russellii
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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
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METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Daboia russellii
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mediates the interaction of factor V to factor Va
Ca2+
Daboia russellii
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absolute requirement for; maximal concentration: 7 mM
Ca2+
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essential for proteolytic activity
Zn2+
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essential for proteolytic activity
Ca2+
Daboia russellii
-
-
additional information
Daboia russellii
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metalloproteinase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
diisopropyl fluorophosphate
Daboia russellii
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RNA132
Daboia russellii
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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
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Snake venom factor IX/factor X-binding protein
Daboia russellii
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with a C-type lectin structure, inhibits factor X activation
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00025
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Factor X
Daboia russellii
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Daboia russellii
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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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.7
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Daboia russellii
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7.8
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Daboia russellii
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assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.7
Daboia russellii
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6.0: 25% of activity maximum, 7.7: activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Daboia russellii
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Daboia russellii
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-
Manually annotated by BRENDA team
Daboia russellii
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-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Daboia russellii
-
-
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
18000
-
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light chain
21000
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light chain
59000
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heavy chain, consists of metalloproteinase, disintegrin and cysteine-rich domains
79000
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Daboia russellii
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Vipera russelli
124000
-
Daboia russellii
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Vipera russelli, sedimentation equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
Daboia russellii
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2 * 60000, Vipera russelli, SDS-PAGE in absence and presence of 2-mercaptoethanol
dimer
Daboia russellii
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1 * 59000 (heavy chain contains a zinc-binding endopeptidase domain and a disintegrin) + 1 * 18000-21000 (heterogeneous light chain), Vipera russelli, SDS-PAGE
monomer
Daboia russellii
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1 * 27200, Vipera russelli, sedimentation equilibrium under denaturing conditions
trimer
Daboia russellii
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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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Daboia russellii
-
6% carbohydrate
glycoprotein
Daboia russellii
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13% carbohydrate; the heavy chains contains 4 asparagine-linked oligosaccharides
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Daboia russellii
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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
85
-
Daboia russellii
-
60 min, enzyme retains approximately 50% of its coagulant and esterase activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70°C to 50°C, procoagulant activity stable
Daboia russellii
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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 russellii
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Daboia russellii
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further purification of the commercial venom enzyme by CM-resin chromatography in presence of N-[(2R)-2-(hydroxamidocarbonyllethyl)-4-methylpentanoyl]-L-tryptophan methylamide
Daboia russellii
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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russellysin is able to inhibit platelet aggregation but the RGD sequence is replaced by Arg-Asp-Glu in the corresponding region