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
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RECOMMENDED NAME
GeneOntology No.
russellysin
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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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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Blood-coagulation factor X activating enzyme
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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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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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Russell`s viper venom coagulation factor X-activating enzyme
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Russell’s viper venom factor X activator
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RVV-V
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snake venom protease
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CAS REGISTRY NUMBER
COMMENTARY
79393-92-3
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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
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?
coagulation factor X + H2O
?
show the reaction diagram
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cleavage at the Arg-Ile bond
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?
Factor IX + H2O
Factor IXaalpha
show the reaction diagram
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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
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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
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not
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Factor X + H2O
A small activation fragment + a large activation fragment
show the reaction diagram
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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
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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
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docking model for factor X, overview
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?
additional information
?
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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
?
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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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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
?
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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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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
?
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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+
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mediates the interaction of factor V to factor Va
Ca2+
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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
additional information
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metalloproteinase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
diisopropyl fluorophosphate
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RNA132
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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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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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
7.8
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assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.7
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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
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Daboia siamensis
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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Vipera russelli
124000
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Vipera russelli, sedimentation equilibrium centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
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2 * 60000, Vipera russelli, SDS-PAGE in absence and presence of 2-mercaptoethanol
dimer
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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
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1 * 27200, Vipera russelli, sedimentation equilibrium under denaturing conditions
trimer
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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
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6% carbohydrate
glycoprotein
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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
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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
85
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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
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
further purification of the commercial venom enzyme by CM-resin chromatography in presence of N-[(2R)-2-(hydroxamidocarbonyllethyl)-4-methylpentanoyl]-L-tryptophan methylamide
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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