Information on EC 3.4.24.B36 - Vipera ammodytes ammodytes metalloproteinase VaH1

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

EC NUMBER
COMMENTARY hide
3.4.24.B36
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Vipera ammodytes ammodytes metalloproteinase VaH1
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolyzes the alpha-chain of human fibrinogen. The enzyme hydrolyzes most rapidly the peptide bond between Ala14 and Lys156 followed by Tyr16-/-Leu17 and His10-/-Leu11 at much slower rates. Strong hemorrhagic activity
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
azocasein + H2O
?
show the reaction diagram
-
-
-
?
human fibrinogen alpha-chain + H2O
?
show the reaction diagram
exclusively hydrolyzes the alpha-chain of fibrinogen
-
-
?
insulin B chain + H2O
?
show the reaction diagram
the enzyme hydrolyzes most rapidly the peptide bond between Ala14 and Lys156 followed by Tyr16-Leu17 and His10-Leu11 at much slower rates
-
-
?
additional information
?
-
VaH1 is a metalloproteinase whose strong hemorrhagic activity is very likely the result of its proteolytic activity
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
eliminates the proteolytic as well as the hemorrhagic activity
additional information
iodoacetamide, phenylmethylsulfonyl fluoride and pepstatin A, inhibitors of cysteine, serine and aspartic proteinases respectively, have no effect
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
1 * 70000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 70000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE