Information on EC 3.4.21.95 - Snake venom factor V activator

Word Map on EC 3.4.21.95
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.95
-
RECOMMENDED NAME
GeneOntology No.
Snake venom factor V activator
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
123757-15-3
-
123757-16-4
-
123757-17-5
-
471269-12-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Daboia lebetina
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-SRDPDNIAAWYLRS + H2O
?
show the reaction diagram
-
synthetic N-acetylated 14-amino acid peptide (FV-14)
-
-
?
Benzoyl-L-Arg ethyl ester + H2O
Benzoyl-L-Arg + ethanol
show the reaction diagram
-
-
-
-
-
Benzoylarginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
?
Clotting factor V + H2O
?
show the reaction diagram
-
-
-
-
-
Clotting factor V + H2O
Clotting factor Va
show the reaction diagram
clotting factor V + H2O
clotting factor Va + ?
show the reaction diagram
factor V + H2O
?
show the reaction diagram
human blood coagulation factor V + H2O
activated human blood coagulation factor V
show the reaction diagram
L-Phe-pipecolyl-L-Arg 4-nitroanilide + H2O
L-Phe-pipecolyl-L-Arg + 4-nitrolaniline
show the reaction diagram
-
-
-
-
-
Pro-Phe-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
?
Tosyl-L-Arg methyl ester + H2O
Tosyl-L-Arg + methanol
show the reaction diagram
-
-
-
-
-
tosylarginine methyl ester + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
-
hydrolyzes several synthetic arginine ester substrates
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Clotting factor V + H2O
?
show the reaction diagram
-
-
-
-
-
factor V + H2O
?
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-Phe-Pro-Arg-chloromethylketone
-
-
diisopropylfluorophosphate
heparin
pefabloc
-
4-(2-aminoethyl)-benzenesulfonyl fluoride
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heparin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.2
-
benzoylarginine ethyl ester as substrate
4.9
-
Pro-Phe-Arg-4-methylcoumarin 7-amide as substrate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
-
analytical isoelectric focusing studies reveals a protein band near the cathode, pI higer than 9.3
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26172
-
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
26182
-
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
27200
-
x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
28000
-
x * 27200 sedimentation equilibrium centrifugation, denaturing conditions, x * 28000, SDS-PAGE, non-reducing conditions, X * 29000, SDS-PAGE, reducing conditions
28400
-
gel filtration, MALDI-TOF mass spectrometry
30000
-
1 * 30000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 30000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
pre-pro peptide indicates that RVV-V is expressed and secreted to the venom glands as a zymogen
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-70 - 50
-
-
70
-
thermostable, heating for 20 min does not alter the arginine esterase activity of the enzyme
85
-
60 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM Tris-HCl, pH 7.5, 0.02% NaN3, protein concentration 0.5-1.5 mg/ml
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Resource S column chromatography and Sephacryl S-100 gel filtration
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine