3.4.24.B35: Vipera ammodytes ammodytes metalloproteinase VaH4
This is an abbreviated version!
For detailed information about Vipera ammodytes ammodytes metalloproteinase VaH4, go to the full flat file.
Word Map on EC 3.4.24.B35
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3.4.24.B35
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acyltransferase
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diacylglycerol
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triglyceride
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acyl-coa:diacylglycerol
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coa:diacylglycerol
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steatosis
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biofuels
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medicine
- 3.4.24.B35
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acyltransferase
- diacylglycerol
- triglyceride
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acyl-coa:diacylglycerol
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coa:diacylglycerol
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steatosis
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biofuels
- medicine
Reaction
Cleavage of Glu422-/-Leu423 and Glu520-/-Phe521 bond of alpha-chain of human fibrinogen. Fibrinogen beta-chain is hydrolysed only partially at Lys22-/-Arg23 and Pro28-Leu29. In insulin B-chain the enzyme preferentially cleaves Tyr16-/-Leu17, followed by Gln4-/-His5 and His10-/-Leu11 =
Synonyms
hemorrhagin VaH4
ECTree
3.4.24.B35 Vipera ammodytes ammodytes metalloproteinase VaH4Advanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.B35 - Vipera ammodytes ammodytes metalloproteinase VaH4
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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 major products of proteolysis of factor X by the enzyme are in the mass range from 33 to 45 kDa. Their N-terminal residues correspond to cleavage at residues 17, 20 and 22 upstream of the N-terminus of the heavy chain FXa
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?
bovine prothrombin + H2O
?
the enzyme does not activate prothrombin in vitro. After 1 h of incubation a weak band at 70 kDa is observed, which is not further hydrolysed if incubation is extended to 24 h. The enzyme cleaves prothrombin at Ser157-/-Gly158, releasing fragment 1 of activation peptide and prethrombin 1
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-
?
human fibrinogen alpha-chain + H2O
?
powerful alpha-fibrinogenase, hydrolysis at Glu422-/-Leu423 and Glu520-/-Phe521
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-
?
human fibrinogen beta-chain + H2O
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hydrolysed only partially at Lys22-/-Arg23 and Pro28-Leu29
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-
?
Insulin B-chain + H2O
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the enzyme cleaves Tyr16-Leu17 preferentially, followed by Gln4-His5 and His10-Leu11
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-
?
Nidogen + H2O
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two cleavage positions: Ser322-/-Phe323 and Tyr352-/-Asn353
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-
?
additional information
?
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no hydrolysis of human fibrinogen gamma-chain. No hydrolysis of fibrin. Hemorrhagic activity of the enzyme is ascribed to its hydrolysis of components of the extracellular matrix, particularly fibronectin and nidogen, and of some blood coagulation proteins, in particular the alpha-chain of fibrinogen
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?
additional information
?
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no hydrolysis of human fibrinogen gamma-chain. No hydrolysis of fibrin. Hemorrhagic activity of the enzyme is ascribed to its hydrolysis of components of the extracellular matrix, particularly fibronectin and nidogen, and of some blood coagulation proteins, in particular the alpha-chain of fibrinogen
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?
