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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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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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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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
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
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