3.4.21.95: Snake venom factor V activator
This is an abbreviated version!
For detailed information about Snake venom factor V activator, go to the full flat file.
Word Map on EC 3.4.21.95
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3.4.21.95
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thrombin
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prothrombin
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lebetina
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vipera
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thrombin-like
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procoagulant
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russelli
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prothrombinase
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daboia
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agkistrodon
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batroxobin
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thrombin-catalyzed
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levantine
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medicine
- 3.4.21.95
- thrombin
- prothrombin
- lebetina
-
vipera
-
thrombin-like
-
procoagulant
- russelli
- prothrombinase
- daboia
-
agkistrodon
- batroxobin
-
thrombin-catalyzed
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levantine
- medicine
Reaction
Fully activates human clotting factor V by a single cleavage at the Trp-Tyr-Leu-Arg1545!Ser-Asn-Asn-Gly bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2 =
Synonyms
blood coagulation factor V-activating proteinase, coagulant serine proteinase, Factor V activator, Factor V-activating enzyme, Factor V-activating proteinase alpha, Factor V-activating proteinase gamma, FV activating enzymes, Human blood coagulation Factor V activating enzymes, LVV-V, Russell's viper venom factor V (FV) activator, Russell's viper venom factor V activator, RVV-V, RVV-Vgamma, Snake venom factor V activator alpha, Snake venom factor V activator gamma, VLCII, VLFVA, VSPF5
ECTree
3.4.21.95 Snake venom factor V activatorAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.95 - Snake venom factor V activator
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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
Ac-SRDPDNIAAWYLRS + H2O
?
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synthetic N-acetylated 14-amino acid peptide (FV-14)
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?
Factor V + H2O
Factor Va
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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
?
L-Phe-pipecolyl-L-Arg 4-nitroanilide + H2O
L-Phe-pipecolyl-L-Arg + 4-nitrolaniline
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?
Nalpha-CBZ L-arginine-4-nitroanilide + H2O
Nalpha-CBZ L-arginine + 4-nitroaniline
thrombin-like activity
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?
Pro-Phe-Arg-7-amido-4-methyl coumarin + H2O
Pro-Phe-Arg + 7-amino-4-methyl coumarin
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?
Clotting factor V + H2O
Clotting factor Va
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clotting factor V of human and bovine origin, no other protein substrate, not rabbit clotting factor V
cleavage of a single peptide bond, Va is composed of a heavy chain of MW 230000 and a light chain of MW 80000
?
clotting factor V + H2O
clotting factor Va + ?
Daboia lebetina
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exosite-mediated interactions are responsible for the enzymes' specificity for the Arg1545 site. The enzyme activates clotting factor V by a fast cleavage after Arg1545, generating a clotting factor Va heavy chain of 290000 Da
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?
clotting factor V + H2O
clotting factor Va + ?
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exosite-mediated interactions are responsible for the enzyme´s specificity for the Arg1545 site. The enzyme activates clotting factor V by a fast cleavage after Arg1545, generating a clotting factor Va heavy chain of 290000 Da
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?
factor V + H2O
?
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specifically activates factor V by cleaving a single peptide bond between Arg1545 and Ser1546
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?
factor V + H2O
?
specifically cleaves the site III (Arg1545-Ser1546) of the factor V
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?
factor V + H2O
?
specifically cleaves the site III (Arg1545-Ser1546) of the factor V. Binding kinetic study of RVV-V with two designed peptides corresponding to the regions from site I (Gln699ÐAsn713) and site II (1008LysÐPro1022), respectively, that include 15 amino acids
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?
factor V + H2O
?
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hydrolyzes human factor V peptide fragments, containing 7-9 amino acids, YLRSNNG, WYLRSNNG and AWYLRSNNG, cleaves Arg-Ser in these peptides
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?
factor V + H2O
?
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aside from factor V, no other protein substrate yet been identified
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?
human blood coagulation factor V + H2O
activated human blood coagulation factor V
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snake venom proteases activates FV by a single cleavage at Arg1545, various mutated variants of blood coagulation factor V are used, snake venom protease require the C-terminal region of the B-domain for efficient activation of FV, this acidic region is importance for the recognition of the Arg1545 cleavage site by the venom FV activators
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?
human blood coagulation factor V + H2O
activated human blood coagulation factor V
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snake venom proteases activates FV by a single cleavage at Arg1545, various mutated variants of blood coagulation factor V are used, snake venom protease require the C-terminal region of the B-domain for efficient activation of FV, this acidic region is importance for the recognition of the Arg1545 cleavage site by the venom FV activators
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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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hydrolyzes several synthetic arginine ester substrates
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?
additional information
?
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purified VLCII is able to clot human plasma
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?
additional information
?
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purified VLCII is able to clot human plasma
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?
additional information
?
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enzyme VLFVA hydrolyses several synthetic arginine ester substrates, such as benzoylarginine ethyl ester (BAEE), tosylarginine methyl ester (TAME) and amide substrates such as Pro-Phe-Arg-MCA
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?
additional information
?
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VLCII is a thrombin-like serine protease able to hydrolyze Nalpha-CBZ L-arginine-4-nitroanilide hydrochloride. The enzyme shows high coagulant activity against human plasma and cleaves both Aalpha chain and Bbeta chain of bovine fibrinogen. The enzyme also exhibits esterase activity on BAEE substrate. The coagulant activity of venom or VLCII is evaluated using human-citrated platelet-poor plasma and human platelet-rich plasma
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?
additional information
?
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VLCII is a thrombin-like serine protease able to hydrolyze Nalpha-CBZ L-arginine-4-nitroanilide hydrochloride. The enzyme shows high coagulant activity against human plasma and cleaves both Aalpha chain and Bbeta chain of bovine fibrinogen. The enzyme also exhibits esterase activity on BAEE substrate. The coagulant activity of venom or VLCII is evaluated using human-citrated platelet-poor plasma and human platelet-rich plasma
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?
