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Literature summary extracted from

  • Leonardi, A.; Gubensek, F.; Krizaj, I.
    Purification and characterisation of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes (2002), Toxicon, 40, 55-62.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B36 EDTA eliminates the proteolytic as well as the hemorrhagic activity Vipera ammodytes ammodytes
3.4.24.B36 additional information iodoacetamide, phenylmethylsulfonyl fluoride and pepstatin A, inhibitors of cysteine, serine and aspartic proteinases respectively, have no effect Vipera ammodytes ammodytes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B36 70000
-
 1 * 70000, SDS-PAGE Vipera ammodytes ammodytes

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B36 Vipera ammodytes ammodytes P0DJ44
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B36 glycoprotein
-
 Vipera ammodytes ammodytes

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B36
-
 Vipera ammodytes ammodytes

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B36 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 no activity with beta-chain or gamma-chain of human fibrinogen Vipera ammodytes ammodytes
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.B36 venom
-
 Vipera ammodytes ammodytes
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B36 azocasein + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B36 human fibrinogen alpha-chain + H2O exclusively hydrolyzes the alpha-chain of fibrinogen Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B36 insulin B chain + H2O the enzyme hydrolyzes most rapidly the peptide bond between Ala14 and Lys156 followed by Tyr16-Leu17 and His10-Leu11 at much slower rates Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B36 additional information VaH1 is a metalloproteinase whose strong hemorrhagic activity is very likely the result of its proteolytic activity Vipera ammodytes ammodytes ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B36 monomer 1 * 70000, SDS-PAGE Vipera ammodytes ammodytes

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B36 VaH1
-
 Vipera ammodytes ammodytes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B36 7.5
-
-
 Vipera ammodytes ammodytes

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.24.B36 Vipera ammodytes ammodytes isoelectric focusing
-
 5.5