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
-
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
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General Information on EC 3.4.21.95 - Snake venom factor V activator
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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
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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
