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Literature summary extracted from

  • Kurtovic, T.; Brgles, M.; Leonardi, A.; Balija, M.L.; Krizaj, I.; Allmaier, G.; Marchetti-Deschmann, M.; Halassy, B
    Ammodytagin, a heterodimeric metalloproteinase from Vipera ammodytes ammodytes venom with strong hemorrhagic activity (2011), Toxicon, 58, 570-582.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B38 dithiothreitol 1 mM, reduces activity to 2.8% Vipera ammodytes ammodytes
3.4.24.B38 EDTA 5 mM, inhibits azocaseinolytic activity Vipera ammodytes ammodytes
3.4.24.B38 L-cysteine 5 mM, reduces activity to 52% Vipera ammodytes ammodytes
3.4.24.B38 additional information antiserum raised against ammodytagin is able to completely neutralise the hemorrhagic activity of the whole venom Vipera ammodytes ammodytes
3.4.24.B38 Zn2+ 5 mM, inhibits azocaseinolytic activity Vipera ammodytes ammodytes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B38 Ca2+ 5 mM, slightly enhances activity for 19.2% Vipera ammodytes ammodytes
3.4.24.B38 Mg2+ 5 mM, slightly enhances activity for 16.9% Vipera ammodytes ammodytes
3.4.24.B38 Zn2+ Zn2+-dependent enzyme Vipera ammodytes ammodytes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B38 50000
-
 1 * 50000 + 1 * 60000, SDS-PAGE under reducing conditions Vipera ammodytes ammodytes
3.4.24.B38 60000
-
 1 * 50000 + 1 * 60000, SDS-PAGE under reducing conditions Vipera ammodytes ammodytes
3.4.24.B38 108000
-
 MALDI mass spectrometry Vipera ammodytes ammodytes

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B38 Vipera ammodytes ammodytes P0DJE2
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B38 glycoprotein total carbohydrate content is approximately 7.1% Vipera ammodytes ammodytes

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B38
-
 Vipera ammodytes ammodytes

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.B38 venom
-
 Vipera ammodytes ammodytes
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B38 azocasein + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 bovine factor X + H2O cleavage occurs at position Gln49-/-Cys50 in the light chain and at position Asp173-/-Leu174 in the heavy chain Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 bovine oxidized insulin B-chain + H2O the enzyme hydrolyzes at positions Gln4–His5, His10–Leu11 and Tyr16–Leu17. No other peptide bond hydrolysis is detected after 30 min of incubation Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 bovine prothrombin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 Fibronectin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 human fibrinogen alpha-chain + H2O hydrolysis at multiple positions, including Ser220-/-Gln221, Lys413-/-Leu414, Glu422-/-Leu423 and Glu520-/-Phe521. Hydrolysis at lower rate (after 6 h) is detected at sites Asn109-/-Arg110, Arg23-/-Met240 and Arg491-/-His492 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 human fibrinogen beta-chain + H2O the fibrinogen beta-chain is cleaved much slower than the alpha-chain Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 additional information the enzyme acts as a strong hemorrhagin in both rats and mice. Laminin is not cleaved even after 24 h treatment with ammodytagin. No cleavage of the human fibrinogen gamma-chain Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B38 Nidogen + H2O in Matrigel Growth Factor Reduced, nidogen is cleaved at positions Val422-/-Phe423 and Tyr352-/-Asn353 Vipera ammodytes ammodytes ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B38 heterodimer 1 * 50000 + 1 * 60000, SDS-PAGE under reducing conditions Vipera ammodytes ammodytes