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Information on EC 3.4.21.95 - Snake venom factor V activator and Organism(s) Daboia siamensis and UniProt Accession P18964

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EC Tree
     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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This record set is specific for:
Daboia siamensis
UNIPROT: P18964 not found.
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Word Map
The taxonomic range for the selected organisms is: Daboia siamensis
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Russell's viper venom factor V activator
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blood coagulation factor V-activating proteinase
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Factor V activator
Factor V-activating enzyme
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-
-
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Factor V-activating proteinase alpha
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-
-
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Factor V-activating proteinase gamma
-
-
-
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RVV-V
RVV-Vgamma
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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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
123757-15-3
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123757-16-4
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123757-17-5
-
471269-12-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
factor V + H2O
?
show the reaction diagram
factor V + H2O
?
show the reaction diagram
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specifically activates factor V by cleaving a single peptide bond between Arg1545 and Ser1546
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
factor V + H2O
?
show the reaction diagram
specifically cleaves the site III (Arg1545-Ser1546) of the factor V
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-Phe-Pro-Arg-chloromethylketone
-
-
pefabloc
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4-(2-aminoethyl)-benzenesulfonyl fluoride
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
VSPA_DABSI
236
0
26182
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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pre-pro peptide indicates that RVV-V is expressed and secreted to the venom glands as a zymogen
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Resource S column chromatography and Sephacryl S-100 gel filtration
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team