Factor V Activating Enzyme
Factor V Activating Enzyme structure
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Common Name | Factor V Activating Enzyme | ||
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| CAS Number | 65522-14-7 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junction.
Blood 117(26) , 7164-73, (2011) Thrombin-catalyzed activation of coagulation factor V (FV) is an essential positive feedback reaction within the blood clotting system. Efficient processing at the N- (Arg(709)-Ser(710)) and C-terminal activation cleavage sites (Arg(1545)-Ser(1546)) requires ... |
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Phosphatidylserine-induced factor Xa dimerization and binding to factor Va are competing processes in solution.
Biochemistry 52(1) , 143-51, (2013) A soluble, short chain phosphatidylserine, 1,2-dicaproyl-sn-glycero-3-phospho-l-serine (C6PS), binds to discrete sites on FXa, FVa, and prothrombin to alter their conformations, to promote FXa dimerization (K(d) ~ 14 nM), and to enhance both the catalytic act... |
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Modulation of prothrombinase assembly and activity by phosphatidylethanolamine.
J. Biol. Chem. 286(41) , 35535-42, (2011) Constituents of platelet membranes regulate the activity of the prothrombinase complex. We demonstrate that membranes containing phosphatidylcholine and phosphatidylethanolamine (PE) bind factor Va with high affinity (K(d) = ∼10 nm) in the absence of phosphat... |
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Structural basis of coagulation factor V recognition for cleavage by RVV-V.
FEBS Lett. 585(19) , 3020-5, (2011) Russell's viper venom factor V (FV) activator (RVV-V) is a thrombin-like proteinase that specifically cleaves the Arg1545-Ser1546 bond of FV. Here we present the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) dete... |
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Crystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venom.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65(Pt 12) , 1306-8, (2009) Russell's viper venom blood coagulation factor V activator (RVV-V) is a thrombin-like serine proteinase that specifically activates factor V by cleaving a single peptide bond between Arg1545 and Ser1546. Activated factor V combines with activated factor X pro... |
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Cross-reactivity of rabbit anti-bovine prothrombin/thrombin IgGs with bovine factor V/Va-related antigens.
Clin. Appl. Thromb. Hemost. 16(5) , 522-8, (2010) The purpose of this study was to determine whether rabbit anti-bovine prothrombin/thrombin immunoglobulin Gs (IgGs) would cross-react with bovine factor V/Va-related antigens. Bovine prothrombin, crude thrombin, as well as 2 purified versions of thrombin, tha... |
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Cleavage at both Arg306 and Arg506 is required and sufficient for timely and efficient inactivation of factor Va by activated protein C.
Blood Coagul. Fibrinolysis 22(4) , 317-24, (2011) Activated protein C (APC) inactivates membrane-bound factor Va following cleavages of the heavy chain at Arg, Arg, and Arg. The objective of this study is to examine which cleavage is most important for inactivation. The recombinant factor V molecules were co... |
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The C-terminus of tissue factor pathway inhibitor α is required for its interaction with factors V and Va.
J. Thromb. Haemost. 10(9) , 1944-6, (2012)
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Bioengineered factor Xa as a potential new strategy for hemophilia therapy.
Expert Rev. Hematol. 5(2) , 121-3, (2012)
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The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences.
J. Biol. Chem. 263(33) , 17471-81, (1988) The complete amino acid sequences of two isoproteins of the factor V-activating enzyme (RVV-V) isolated from Vipera russelli (Russell's viper) venom were determined by sequencing S-pyridylethylated derivatives of the proteins and their peptide fragments gener... |