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Literature summary for 3.4.24.B38 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
Search for more literature for 3.4.24.B38

Inhibitors

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Vipera ammodytes ammodytes P0DJE2
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein total carbohydrate content is approximately 7.1% Vipera ammodytes ammodytes

Purification (Commentary)

Purification (Comment) Organism
-
 Vipera ammodytes ammodytes

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Vipera ammodytes ammodytes
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azocasein + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
bovine prothrombin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
Fibronectin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
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 ?
-
 ?
human fibrinogen beta-chain + H2O the fibrinogen beta-chain is cleaved much slower than the alpha-chain Vipera ammodytes ammodytes ?
-
 ?
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 ?
-
 ?
Nidogen + H2O in Matrigel Growth Factor Reduced, nidogen is cleaved at positions Val422-/-Phe423 and Tyr352-/-Asn353 Vipera ammodytes ammodytes ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 50000 + 1 * 60000, SDS-PAGE under reducing conditions Vipera ammodytes ammodytes