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Literature summary for 3.4.24.B36 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
Search for more literature for 3.4.24.B36

Inhibitors

Inhibitors Comment Organism Structure
EDTA eliminates the proteolytic as well as the hemorrhagic activity Vipera ammodytes ammodytes
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 1 * 70000, SDS-PAGE Vipera ammodytes ammodytes

Organism

Organism UniProt Comment Textmining
Vipera ammodytes ammodytes P0DJ44
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Vipera ammodytes ammodytes

Purification (Commentary)

Purification (Comment) Organism
-
 Vipera ammodytes ammodytes

Reaction

Reaction Comment Organism Reaction ID
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

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 ?
-
 ?
human fibrinogen alpha-chain + H2O exclusively hydrolyzes the alpha-chain of fibrinogen Vipera ammodytes ammodytes ?
-
 ?
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 ?
-
 ?
additional information VaH1 is a metalloproteinase whose strong hemorrhagic activity is very likely the result of its proteolytic activity Vipera ammodytes ammodytes ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 70000, SDS-PAGE Vipera ammodytes ammodytes

Synonyms

Synonyms Comment Organism
VaH1
-
 Vipera ammodytes ammodytes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Vipera ammodytes ammodytes

pI Value

Organism Comment pI Value Maximum pI Value
Vipera ammodytes ammodytes isoelectric focusing
-
 5.5