3.4.24.58: russellysin
This is an abbreviated version!
For detailed information about russellysin, go to the full flat file.
Word Map on EC 3.4.24.58
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3.4.24.58
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prothrombin
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envenom
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x-activating
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hemophilia
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daboia
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prothrombinase
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lebetina
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snakebite
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echis
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medicine
- 3.4.24.58
- prothrombin
-
envenom
-
x-activating
-
hemophilia
-
daboia
- prothrombinase
- lebetina
-
snakebite
-
echis
- medicine
Reaction
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
Blood-coagulation factor X activating enzyme, EC 3.4.21.23, Metalloproteinase RVV-x, Proteinase, Vipera russelli, Russell's viper blood coagulation factor X activator, Russell's Viper venom factor X activator, Russell's viper venom factor X activator, RVV-X, Russell`s viper venom coagulation factor X-activating enzyme, Russell’s viper venom factor X activator, RVV-X, snake venom protease
ECTree
3.4.24.58 russellysinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.58 - russellysin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coagulation factor IX + H2O
?
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cleavage at the Arg-Xaa bond
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-
?
coagulation factor X + H2O
?
-
cleavage at the Arg-Ile bond
-
-
?
Factor IX + H2O
Factor IXaalpha
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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-
?
Factor X + H2O
A small activation fragment + a large activation fragment
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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
?
o-aminobenzoyl-Gly-Phe-Arg-Leu-Leu-2,4-dinitroanilinoethylamide + H2O
?
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-
-
-
?
factor X + H2O
factor Xa + propeptide of factor Xa
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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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potently inhibits collagen-stimulated and ADP-stimulated platelet aggregation
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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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?
additional information
?
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no action on the B chain of insulin
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-
?
