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Literature summary for 3.4.24.B33 extracted from

  • Sajevic, T.; Leonardi, A.; Kovacic, L.; Lang-Balija, M.; Kurtovic, T.; Pungercar, J.; Halassy, B.; Trampus-Bakija, A.; Krizaj, I.
    VaH3, one of the principal hemorrhagins in Vipera ammodytes ammodytes venom, is a homodimeric P-IIIc metalloproteinase (2013), Biochimie, 95, 1158-1170.
    View publication on PubMed
Search for more literature for 3.4.24.B33

Application

Application Comment Organism
medicine snake venom metalloproteinases are important targets in antivenom therapy Vipera ammodytes ammodytes

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis Vipera ammodytes ammodytes

General Stability

General Stability Organism
enzyme VaH3 is a labile protein that rapidly loses its proteolytic and hemorrhagic activities, presence of imidazole and absence of Ca2+ ions in the buffers reduces VaH3 stability, also 50 mM NaCl or KCl reduce the enzyme stability Vipera ammodytes ammodytes
stability depends on the presence of Zn2+ and Ca2+ ions Vipera ammodytes ammodytes

Inhibitors

Inhibitors Comment Organism Structure
anti-ammodytagin antibodies complete inhibition, the antibodies strongly crossreact with VaH3 and completely neutralize its hemorrhagic activity in rat Vipera ammodytes ammodytes
EDTA alpha-fibrinogenolytic activity is completely inhibited Vipera ammodytes ammodytes
additional information no inhibition by PMSF Vipera ammodytes ammodytes

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Vipera ammodytes ammodytes
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for enzyme stability and activity Vipera ammodytes ammodytes
Zn2+ dependent on, required for enzyme stability Vipera ammodytes ammodytes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53700
-
 2 * 58000, SDS-PAGE, 2 * 53700, mass spectrometric analysis after chemical reduction and S-carbamoylmethylation Vipera ammodytes ammodytes
58000
-
 2 * 58000, SDS-PAGE, 2 * 53700, mass spectrometric analysis after chemical reduction and S-carbamoylmethylation Vipera ammodytes ammodytes
104000
-
 MALDI/TOF mass spectrometric analysis Vipera ammodytes ammodytes
130000
-
 native PAGE Vipera ammodytes ammodytes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Collagen IV + H2O Vipera ammodytes ammodytes
-
 ?
-
 ?
factor X + H2O Vipera ammodytes ammodytes
-
 ?
-
 ?
fibrinogen alpha-chain + H2O Vipera ammodytes ammodytes
-
 ?
-
 ?
Fibronectin + H2O Vipera ammodytes ammodytes
-
 ?
-
 ?
additional information Vipera ammodytes ammodytes hydrolyzes plasma proteins involved in blood coagulation. VaH3 only very weakly inhibits collagen-, ADP- and ristocetin-induced platelet aggregation ?
-
 ?
Nidogen + H2O Vipera ammodytes ammodytes
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Vipera ammodytes ammodytes R4NNL0
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein low N-glycosylation level, deglycosylation reduces the molecular weight by 4.6 kDa Vipera ammodytes ammodytes

Purification (Commentary)

Purification (Comment) Organism
native enzyme from venom by gel filtration, concanavalin A affinity and anion-exchange chromatography, followed by hydroxyapatite and cation exchange chromatography, homogenization by isoelectric focusing Vipera ammodytes ammodytes

Reaction

Reaction Comment Organism Reaction ID
Cleavage of the Lys413-/-Leu414 bond of alpha-chain of human fibrinogen. Cleavage of Ala14-/-Leu15 and more slowly Tyr16-/-Leu17 in insulin B chain. Hemorrhagic metalloproteinase no cleavage of fibrin, fibrinogen Bbeta-chain or fibrinogen gamma-chain 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.
bovine factor X + H2O the enzyme is able to activate factor X only to a very small extent. However it strongly degrades factor X. The major proteolytic products accumulates between 34 and 37 kDa and their N-terminals correspond to cleavage at residues 17, 20 and 22 upstream of the N-terminal of the factor Xa heavy chain Vipera ammodytes ammodytes ?
-
 ?
bovine fibronectin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
bovine prothrombin + H2O the enzyme degrades prothrombin in vitro, however in a nonactivating way. VaH3 cleaves the molecule at sites involved in the physiological process of its activation. This results in the formation of prethrombin-1 and prethrombin-2, along with fragments 1 and 2. However, VaH3 does not cleave the Arg320-/-Ile321 peptide bond that is essential for the formation of active alpha-thrombin Vipera ammodytes ammodytes ?
-
 ?
Collagen IV + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
factor X + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
fibrinogen alpha-chain + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
Fibronectin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
human fibrinogen alpha-chain + H2O the alpha-chain of human fibrinogen is cleaved between Lys413 and Leu414, no hydrolysis of the beta- or gamma-chains is observed Vipera ammodytes ammodytes ?
-
 ?
human type collagen IV + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
Insulin B-chain + H2O VaH3 rapidly cleaves the peptide bond Ala14-/-Leu15, the bond Tyr16-/-Leu17 is hydrolyzed at a much slower rate Vipera ammodytes ammodytes ?
-
 ?
additional information hydrolyzes plasma proteins involved in blood coagulation. VaH3 only very weakly inhibits collagen-, ADP- and ristocetin-induced platelet aggregation Vipera ammodytes ammodytes ?
-
 ?
additional information VaH3 does not degrade fibrin clots in vitro Vipera ammodytes ammodytes ?
-
 ?
murine laminin + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?
murine nidogen + H2O from Matrigel Growth Factor Reduced, preferentially cleaved at positions Ser322-/-Phe323 and and Tyr352-/-Asn353 Vipera ammodytes ammodytes ?
-
 ?
Nidogen + H2O
-
 Vipera ammodytes ammodytes ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 58000, SDS-PAGE, 2 * 53700, mass spectrometric analysis after chemical reduction and S-carbamoylmethylation Vipera ammodytes ammodytes
More two identical, covalently linked subunits, each of the identical glycoprotein subunits comprise a metalloproteinase, a disintegrin-like domain and a cysteine-rich domain. Enzyme three-dimensional structure modeling and structure-function relationship analysis, peptide mapping after digestion of the enzyme by endoproteinase Lys-C, overview Vipera ammodytes ammodytes

Synonyms

Synonyms Comment Organism
VaH3
-
 Vipera ammodytes ammodytes
Vipera ammodytes hemorrhagin 3
-
 Vipera ammodytes ammodytes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Vipera ammodytes ammodytes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
 assay at Vipera ammodytes ammodytes

pI Value

Organism Comment pI Value Maximum pI Value
Vipera ammodytes ammodytes isoelectric focusing
-
 6.2

General Information

General Information Comment Organism
evolution the enzyme VaH3 belongs to the P-IIIc class of snake venom metalloproteinases Vipera ammodytes ammodytes
additional information enzyme three-dimensional structure model and structure-function relationship analysis, overview Vipera ammodytes ammodytes
physiological function Zn2+-dependent metalloproteinases play a major part in the pathological effects of viperid snake bites, the most pronounced being local and systemic hemorrhage, local tissue damage and coagulopathy. Enzyme VaH3 is one of the principal hemorrhagins in Vipera ammodytes ammodytes venom The enzyme is an effective alpha-fibrinogenase that cleaves prothrombin and factor X without activating them. VaH3 only very weakly inhibits collagen-, ADP- and ristocetin-induced platelet aggregation Vipera ammodytes ammodytes