Information on EC 3.4.24.B34 - Vipera ammodytes ammodytes metalloproteinase VaF1

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The expected taxonomic range for this enzyme is: Vipera ammodytes ammodytes

EC NUMBER
COMMENTARY hide
3.4.24.B34
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Vipera ammodytes ammodytes metalloproteinase VaF1
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of the Lys413-/-Leu414 bond of alpha-chain of human fibrinogen. Cleavage of Ala14-/-Leu15 and Tyr16-/-Leu17 in insulin B chain. Non-hemorrhagic proteinase
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bovine factor X + H2O
?
show the reaction diagram
slow degradation. The heavy chain offactor X is more susceptible to hydrolysis by the enzyme than the light chain whose hydrolysis is observed only after prolonged incubation
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-
?
bovine fibronectin + H2O
?
show the reaction diagram
-
-
-
?
bovine plasminogen + H2O
?
show the reaction diagram
slow degradation. Very limited proteolysis, giving rise to multiple products with molecular masses between 40 and 60 kDa
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-
?
bovine prothrombin + H2O
?
show the reaction diagram
slow degradation. Two major cleavage products, of 60 and 28 kDa, accumulate after extended incubation. N-terminal sequencing shows them to be prethrombin-1 and fragment 1, indicating the cleavage of prothrombin at the Ser157-/-Gly158 bond
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-
?
factor X + H2O
?
show the reaction diagram
partial hydrolysis
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-
?
Human fibrinogen + H2O
?
show the reaction diagram
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-
-
?
human fibrinogen alpha-chain + H2O
?
show the reaction diagram
cleavage of the Lys413-/-Leu414 bond of alpha-chain of fibrinogen. Fibrinogen beta- and gamma-chains remain intact even after 3 h incubation
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-
?
human type collagen IV + H2O
?
show the reaction diagram
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-
-
?
insulin B chain + H2O
?
show the reaction diagram
cleavage of two peptide bonds is detected, Ala14-/-Leu15 and Tyr16-/-Leu17
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-
?
Nidogen + H2O
?
show the reaction diagram
hydrolysis at the Ser322-/-Phe323 bond
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-
?
plasminogen + H2O
?
show the reaction diagram
partial hydrolysis
-
-
?
prothrombin + H2O
?
show the reaction diagram
partial hydrolysis
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-
?
additional information
?
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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
factor X + H2O
?
show the reaction diagram
A0A0B4U9L8
partial hydrolysis
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-
?
Human fibrinogen + H2O
?
show the reaction diagram
A0A0B4U9L8
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
A0A0B4U9L8
partial hydrolysis
-
-
?
prothrombin + H2O
?
show the reaction diagram
A0A0B4U9L8
partial hydrolysis
-
-
?
additional information
?
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A0A0B4U9L8
hydrolysis of fibrinogen, factor X, prothrombin and plasminogen, plasma proteins involved in blood coagulation
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
pre-incubation of the enzyme with EDTA blocks the fibrinogenolytic activity
additional information
pefabloc, an inhibitor of serine proteases, has no effect on the enzyme proteolytic activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
isoelectric focussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49735
1 * 49735, mass spectrometry, SDS-PAGE and native PAGE
49740
mass spectrometry, SDS-PAGE and native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 49735, mass spectrometry, SDS-PAGE and native PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the enzyme contains two consensus N-glycosylation sites, the extent of its glycosylation is 5.2% of the total molecular mass. Deglycosylation by peptide N-glycosidase F. Deglycosylation reduces the molecular weight by 3.0 kDa
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by several steps including cation exchange chromatography, dialysis and anion exchange chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
in standard experimental conditions, enzyme VaF1 is not recognised by antiserum against the whole venom, so it can contribute to postserotherapy complications, such as ineffective blood coagulation, in the envenomed patient