3.4.21.95: Snake venom factor V activator

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For detailed information about Snake venom factor V activator, go to the full flat file.

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 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.95 Snake venom factor V activator

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Results	in table
2	Activating Compound
3	AA Sequence
2	Application
4	CAS Registry Number
1	Cloned(Commentary)
2	Crystallization (Commentary)
7	General Information
1	General Stability
14	Inhibitors
3	Localization
1	Metals/Ions
11	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
17	Organism
4	PDB ID
1	pH Optimum
2	pI Value
4	Posttranslational Modification
6	Purification (Commentary)
1	Reaction
3	Reaction Type
16	Reference
9	Source Tissue
3	Specific Activity [micromol/min/mg]
3	Storage Stability
35	Substrates and Products (Substrate)
7	Subunits
29	Synonyms
1	Temperature Optimum [°C]
4	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.4.21.95 - Snake venom factor V activator

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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

Daboia russelii

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717606

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

Daboia siamensis

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706966