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Information on EC 3.4.21.95 - Snake venom factor V activator
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EC Tree
3.4.21.95 Snake venom factor V activatorSpecify your search results
Word Map
- 3.4.21.95
- thrombin
- prothrombin
- lebetina
-
vipera
-
thrombin-like
-
procoagulant
- russelli
- prothrombinase
- daboia
-
agkistrodon
- batroxobin
-
thrombin-catalyzed
-
levantine
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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
rvv-v, factor v activator, vlfva, lvv-v, factor v-activating enzyme, russell's viper venom factor v activator, rvv-vgamma, fv activating enzymes, coagulant serine proteinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Factor V activator
Factor V-activating enzyme
-
-
-
-
Factor V-activating proteinase alpha
-
-
-
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Factor V-activating proteinase gamma
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-
-
-
FV activating enzymes
Human blood coagulation Factor V activating enzymes
RVV-V
RVV-Vgamma
-
the deduced amino acid sequence of the mature RVV-V is 99% identical with the RVV-Vgamma since there is one amino acid substitution (H192K)
Snake venom factor V activator alpha
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-
-
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Snake venom factor V activator gamma
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-
-
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VLFVA
Factor V activator
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-
-
-
RVV-V
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
123757-15-3
-
123757-16-4
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123757-17-5
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471269-12-2
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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
?
-
synthetic N-acetylated 14-amino acid peptide (FV-14)
-
-
?
Factor V + H2O
Factor Va
-
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
-
-
-
-
?
Nalpha-CBZ L-arginine-4-nitroanilide + H2O
Nalpha-CBZ L-arginine + 4-nitroaniline
thrombin-like activity
-
-
?
Pro-Phe-Arg-7-amido-4-methyl coumarin + H2O
Pro-Phe-Arg + 7-amino-4-methyl coumarin
-
-
-
?
Clotting factor V + H2O
Clotting factor Va
-
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
-
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
-
-
?
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
-
-
?
factor V + H2O
?
-
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
-
-
?
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
-
-
?
factor V + H2O
?
-
hydrolyzes human factor V peptide fragments, containing 7-9 amino acids, YLRSNNG, WYLRSNNG and AWYLRSNNG, cleaves Arg-Ser in these peptides
-
?
factor V + H2O
?
-
aside from factor V, no other protein substrate yet been identified
-
?
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
-
-
?
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
?
-
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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-
?
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NATURAL SUBSTRATE
NATURAL 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
factor V + H2O
?
specifically cleaves the site III (Arg1545-Ser1546) of the factor V
-
-
?
factor V + H2O
?
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aside from factor V, no other protein substrate yet been identified
-
?
additional information
?
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purified VLCII is able to clot human plasma
-
-
?
additional information
?
-
-
purified VLCII is able to clot human plasma
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Acetylsalicylic acid
aspirin, reduces markedly platelet aggregating effect induced by VLCII, less effective compared to clopidogrel
ADP
reduces slightly platelet aggregating effect induced by VLCII
clopidogrel
P2Y12 adenosine diphosphate (ADP) receptor inhibitor, reduces markedly platelet aggregating effect induced by VLCII
additional information
no inhibition of the proteolytic activity of VLCII by EDTA and 1,10-phenanthroline, poor inhibition by EGTA. VLCII activity on platelet aggregation is tested after treatment with acetylsalicylic acid (aspirin) irreversible inhibitor of cyclooxygenase-1 (COX-1) and clopidogrel (plavix) antagonist of P2Y12 receptor
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additional information
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no inhibition of the proteolytic activity of VLCII by EDTA and 1,10-phenanthroline, poor inhibition by EGTA. VLCII activity on platelet aggregation is tested after treatment with acetylsalicylic acid (aspirin) irreversible inhibitor of cyclooxygenase-1 (COX-1) and clopidogrel (plavix) antagonist of P2Y12 receptor
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
Factor V activator from Daboia russelli russelli venom destabilize ?-amyloid aggregate, the hallmark of Alzheimer's disease.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.3
9.3
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analytical isoelectric focusing studies reveals a protein band near the cathode, pI higer than 9.3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
factor V activator is separated from factor X activator by gel filtration
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the amino acid sequence of VLFVA shows significant homology with snake venom and mammalian serine proteinases. The other sequences (VLP2, VLP3 and VLP4) are homologous to VLFVA, but have two principal discrepancies in the translated protein sequence in comparison with snake venom serine protease structures: in the active site triad Ser195 is replaced by Asn195 and His57 by Arg57. Sequences of VLP3 and VLP4 represent combinations of VLFVA and VLP2 clones
malfunction
clopidogrel P2Y12 adenosine diphosphate (ADP) receptor inhibitor reduces markedly the aggregating effect induced by VLCII indicating the involvement of ADP signaling pathway
metabolism
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview
physiological function
physiological function
-
small peptides derived from factor V activator destabilize the beta-amyloid aggregate. Factor V activator-mediated proteolysis is not involved. Peptide CTNIF and a mixture of six peptides are most potent in converting the aggregates to the monomeric state and thus, preventing cytotoxicity in SH-SY5Y human neuroblastoma cells
physiological function
binding kinetic study of RVV-V with two designed peptides corresponding to the regions from site I (Gln699-Asn713) and site II (1008Lys-Pro1022), respectively, of substrate blood coagulation factor V. Peptide II shows a lower binding affinity with KD of 2.775 mM while the Peptide I shows none. The peptide binding results in global conformational changes in the native fold of RVV-V, whereas the similar studies for thrombin fail to make major changes in the native fold
physiological function
in addition to its proteolytic activity, enzyme VLCII presents coagulant activity on human plasma. The isolated VLCII displays proaggregating effect on human platelets in a concentration-dependent manner with an absence of lag time. Purified VLCII is able to clot human plasma
physiological function
the enzyme VLFVA has the ability to activate factor V
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VSPA_DABSI
236
0
26182
Swiss-Prot
other Location (Reliability: 1)
VSPF5_MACLB
259
0
28595
Swiss-Prot
Secretory Pathway (Reliability: 2)
VSPG_DABSI
260
0
28823
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26172
-
x * 26182, enzyme RVV-Valpha, x * 26172, enzyme RVV-Vgamma, six disulfide bridges, of which Cys74-Cys234 is unique to snake venom serine proteases, amino acid sequence
26182
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x * 26182, enzyme RVV-Valpha, x * 26172, enzyme RVV-Vgamma, six disulfide bridges, of which Cys74-Cys234 is unique to snake venom serine proteases, amino acid sequence
27200
28000
-
x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
29000
27200
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x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
27200
-
1 * 27200, Vipera russelli, sedimentation equilibrium under denaturing conditions
29000
-
x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 26182, enzyme RVV-Valpha, x * 26172, enzyme RVV-Vgamma, six disulfide bridges, of which Cys74-Cys234 is unique to snake venom serine proteases, amino acid sequence
?
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x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
monomer
-
1 * 27200, Vipera russelli, sedimentation equilibrium under denaturing conditions
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
pre-pro peptide indicates that RVV-V is expressed and secreted to the venom glands as a zymogen
glycoprotein
-
single oligosaccharide chain at Asn229, 1 mol fucose, 1 mol mannose, 1 mol N-acetylneuramic acid, 2 mol galactose, 3 mol N-acetylglucosamine per mol of enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8 A resolution is shown. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P7)-Arg1545 (P1), of the cleaved substrate. Comparison with substrate-free structures reveals conformational changes of the RVV-V loops upon substrate binding, suggesting that the multiple interactions are mediated by an induced-fit mechanism
-
in complex with Pefabloc or D-Phe-Pro-Arg-chloromethylketone, sitting drop vapor diffusion method, using 0.8% (w/v) tryptone, 0.04 M Na HEPES pH 7.0 and 9.6% (w/v) PEG 3350
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
-
thermostable, heating for 20 min does not alter the arginine esterase activity of the enzyme
85
85
-
60 min, enzyme retains approximately 50% of its coagulant and esterase activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-HCl, pH 7.5, 0.02% NaN3, protein concentration 0.5-1.5 mg/ml
-
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
LITERATURE
native enzyme from venom 150.7fold by gel filtration and anion exchange chromatography, enzyme preparation is followed by lyophilization and reversed-phase HPLC on C8 column, to apparent homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from venom gland cDNA library, DNA and amino acid sequence determination and analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
potential use of snake venom proteases as diagnostic and thrombolytic agents
medicine
-
small peptides derived from factor V activator destabilize the beta-amyloid aggregate. Peptide CTNIF and a mixture of six peptides are most potent in converting the aggregates to the monomeric state and thus, preventing cytotoxicity in SH-SY5Y human neuroblastoma cells. Some of the peptides are stable in blood for 24 h
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kisiel, W.; Canfield, W.M.
Snake venom proteases that activate blood-coagulation factor V
Methods Enzymol.
80
275-285
1981
Daboia russelii
brenda
Tokunaga, F.; Nagasawa, K.; Tamura, S.; Miyata, T.; Iwanaga, S.; Kisiel, W.
The factor V-activating enzyme (RVV-V) from Russell's viper venom
J. Biol. Chem.
263
17471-17481
1988
Daboia russelii
brenda
Siigur, E.; Samel, M.; Tonismaegi, K.; Subbi, J.; Reintamm, T.; Siigur, J.
Isolation, properties and N-terminal amino acid sequence of a factor V activator from Vipera lebetina (levantine viper) snake venom
Biochim. Biophys. Acta
1429
239-248
1998
Macrovipera lebetina
brenda
Siigur, J.; Aaspollu, A.; Tonismaegi, K.; Trummal, K.; Samel, M.; Vija, H.; Subbi, J.; Siigur, E.
Proteases from Vipera lebetina Venom Affecting Coagulation and Fibrinolysis
Haemostasis
31
123-132
2001
Macrovipera lebetina
brenda
Segers, K.; Rosing, J.; Nicolaes, G.A.
Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina
Proteins
64
968-984
2006
Daboia russelii, Daboia lebetina
brenda
Segers, K.; Dahlbaeck, B.; Bock, P.E.; Tans, G.; Rosing, J.; Nicolaes, G.A.
The role of thrombin exosites I and II in the activation of human coagulation factor V
J. Biol. Chem.
282
33915-33924
2007
Daboia russelii, Macrovipera lebetina
brenda
Nakayama, D.; Ben Ammar, Y.; Takeda, S.
Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russells viper venom
Acta Crystallogr. Sect. F
65
1306-1308
2009
Daboia siamensis
brenda
Nakayama, D.; Ben Ammar, Y.; Miyata, T.; Takeda, S.
Structural basis of coagulation factor V recognition for cleavage by RVV-V
FEBS Lett.
585
3020-3025
2011
Daboia russelii
brenda
Sukkapan, P.; Jia, Y.; Nuchprayoon, I.; Perez, J.C.
Phylogenetic analysis of serine proteases from Russells viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom
Toxicon
58
168-178
2011
Daboia siamensis
brenda
Bhattacharjee, P.; Bhattacharyya, D.
Factor V activator from Daboia russelli russelli venom destabilizes beta-amyloid aggregate, the hallmark of Alzheimer disease
J. Biol. Chem.
288
30559-30570
2013
Daboia russelii
brenda
Amel, K.; Fatima, L.
Purification and characterization of a new serine protease (VLCII) isolated from Vipera lebetina venom its role in hemostasis
J. Biochem. Mol. Toxicol.
29
388-397
2015
Macrovipera lebetina (Q9PT41), Macrovipera lebetina
brenda
Yadav, P.K.; Antonyraj, C.B.; Basheer Ahamed, S.I.; Srinivas, S.
Understanding Russells viper venom factor V activators substrate specificity by surface plasmon resonance and in-silico studies
PLoS ONE
12
e0181216
2017
Daboia siamensis (P18964), Daboia siamensis (P18965)
brenda
Siigur, J.; Aaspollu, A.; Siigur, E.
Biochemistry and pharmacology of proteins and peptides purified from the venoms of the snakes Macrovipera lebetina subspecies
Toxicon
158
16-32
2019
Macrovipera lebetina (Q9PT41)
brenda
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