3.4.24.B33: Vipera ammodytes ammodytes metalloproteinase VaH3
This is an abbreviated version!
For detailed information about Vipera ammodytes ammodytes metalloproteinase VaH3, go to the full flat file.
Reaction
Cleavage of the Lys413-/-Leu414 bond of alpha-chain of human fibrinogen. Cleavage of Ala14-/-Leu15 and additional information slowly Tyr16-/-Leu17 in insulin B chain. Hemorrhagic metalloproteinase =
Synonyms
VaH3, Vipera ammodytes hemorrhagin 3
ECTree
3.4.24.B33 Vipera ammodytes ammodytes metalloproteinase VaH3Advanced search results
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Substrates Products on EC 3.4.24.B33 - Vipera ammodytes ammodytes metalloproteinase VaH3
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bovine factor X + H2O
?
the enzyme is able to activate factor X only to a very small extent. However it strongly degrades factor X. The major proteolytic products accumulates between 34 and 37 kDa and their N-terminals correspond to cleavage at residues 17, 20 and 22 upstream of the N-terminal of the factor Xa heavy chain
-
-
?
bovine prothrombin + H2O
?
the enzyme degrades prothrombin in vitro, however in a nonactivating way. VaH3 cleaves the molecule at sites involved in the physiological process of its activation. This results in the formation of prethrombin-1 and prethrombin-2, along with fragments 1 and 2. However, VaH3 does not cleave the Arg320-/-Ile321 peptide bond that is essential for the formation of active alpha-thrombin
-
-
?
human fibrinogen alpha-chain + H2O
?
the alpha-chain of human fibrinogen is cleaved between Lys413 and Leu414, no hydrolysis of the beta- or gamma-chains is observed
-
-
?
Insulin B-chain + H2O
?
VaH3 rapidly cleaves the peptide bond Ala14-/-Leu15, the bond Tyr16-/-Leu17 is hydrolyzed at a much slower rate
-
-
?
murine nidogen + H2O
?
from Matrigel Growth Factor Reduced, preferentially cleaved at positions Ser322-/-Phe323 and and Tyr352-/-Asn353
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-
?
additional information
?
-
hydrolyzes plasma proteins involved in blood coagulation. VaH3 only very weakly inhibits collagen-, ADP- and ristocetin-induced platelet aggregation
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-
?
additional information
?
-
VaH3 does not degrade fibrin clots in vitro
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-
?
