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Literature summary extracted from
- VaH3, one of the principal hemorrhagins in Vipera ammodytes ammodytes venom, is a homodimeric P-IIIc metalloproteinase (2013), Biochimie, 95, 1158-1170.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.24.B33 | medicine | snake venom metalloproteinases are important targets in antivenom therapy | Vipera ammodytes ammodytes |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.24.B33 | DNA and amino acid sequence determination and analysis | Vipera ammodytes ammodytes |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.24.B33 | 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 |
| 3.4.24.B33 | stability depends on the presence of Zn2+ and Ca2+ ions | Vipera ammodytes ammodytes |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.B33 | anti-ammodytagin antibodies | complete inhibition, the antibodies strongly crossreact with VaH3 and completely neutralize its hemorrhagic activity in rat | Vipera ammodytes ammodytes | |
| 3.4.24.B33 | EDTA | alpha-fibrinogenolytic activity is completely inhibited | Vipera ammodytes ammodytes |  |
| 3.4.24.B33 | additional information | no inhibition by PMSF | Vipera ammodytes ammodytes |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.24.B33 | extracellular | - |
Vipera ammodytes ammodytes | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.B33 | Ca2+ | required for enzyme stability and activity | Vipera ammodytes ammodytes | |
| 3.4.24.B33 | Zn2+ | dependent on, required for enzyme stability | Vipera ammodytes ammodytes | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B33 | 53700 | - |
2 * 58000, SDS-PAGE, 2 * 53700, mass spectrometric analysis after chemical reduction and S-carbamoylmethylation | Vipera ammodytes ammodytes |
| 3.4.24.B33 | 58000 | - |
2 * 58000, SDS-PAGE, 2 * 53700, mass spectrometric analysis after chemical reduction and S-carbamoylmethylation | Vipera ammodytes ammodytes |
| 3.4.24.B33 | 104000 | - |
MALDI/TOF mass spectrometric analysis | Vipera ammodytes ammodytes |
| 3.4.24.B33 | 130000 | - |
native PAGE | Vipera ammodytes ammodytes |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B33 | Collagen IV + H2O | Vipera ammodytes ammodytes | - |
? | - |
? | |
| 3.4.24.B33 | factor X + H2O | Vipera ammodytes ammodytes | - |
? | - |
? | |
| 3.4.24.B33 | fibrinogen alpha-chain + H2O | Vipera ammodytes ammodytes | - |
? | - |
? | |
| 3.4.24.B33 | Fibronectin + H2O | Vipera ammodytes ammodytes | - |
? | - |
? | |
| 3.4.24.B33 | additional information | Vipera ammodytes ammodytes | hydrolyzes plasma proteins involved in blood coagulation. VaH3 only very weakly inhibits collagen-, ADP- and ristocetin-induced platelet aggregation | ? | - |
? | |
| 3.4.24.B33 | Nidogen + H2O | Vipera ammodytes ammodytes | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.B33 | Vipera ammodytes ammodytes | R4NNL0 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.24.B33 | glycoprotein | low N-glycosylation level, deglycosylation reduces the molecular weight by 4.6 kDa | Vipera ammodytes ammodytes |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.24.B33 | 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
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.24.B33 | 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 |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.24.B33 | venom | - |
Vipera ammodytes ammodytes | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B33 | 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 | ? | - |
? | |
| 3.4.24.B33 | bovine fibronectin + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | 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 | ? | - |
? | |
| 3.4.24.B33 | Collagen IV + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | factor X + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | fibrinogen alpha-chain + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | Fibronectin + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | 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 | ? | - |
? | |
| 3.4.24.B33 | human type collagen IV + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | 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 | ? | - |
? | |
| 3.4.24.B33 | additional information | hydrolyzes plasma proteins involved in blood coagulation. VaH3 only very weakly inhibits collagen-, ADP- and ristocetin-induced platelet aggregation | Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | additional information | VaH3 does not degrade fibrin clots in vitro | Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | murine laminin + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | murine nidogen + H2O | from Matrigel Growth Factor Reduced, preferentially cleaved at positions Ser322-/-Phe323 and and Tyr352-/-Asn353 | Vipera ammodytes ammodytes | ? | - |
? | |
| 3.4.24.B33 | Nidogen + H2O | - |
Vipera ammodytes ammodytes | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.24.B33 | homodimer | 2 * 58000, SDS-PAGE, 2 * 53700, mass spectrometric analysis after chemical reduction and S-carbamoylmethylation | Vipera ammodytes ammodytes |
| 3.4.24.B33 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.B33 | VaH3 | - |
Vipera ammodytes ammodytes |
| 3.4.24.B33 | Vipera ammodytes hemorrhagin 3 | - |
Vipera ammodytes ammodytes |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B33 | 37 | - |
assay at | Vipera ammodytes ammodytes |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B33 | 8.4 | - |
assay at | Vipera ammodytes ammodytes |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.24.B33 | Vipera ammodytes ammodytes | isoelectric focusing | - |
6.2 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.B33 | evolution | the enzyme VaH3 belongs to the P-IIIc class of snake venom metalloproteinases | Vipera ammodytes ammodytes |
| 3.4.24.B33 | additional information | enzyme three-dimensional structure model and structure-function relationship analysis, overview | Vipera ammodytes ammodytes |
| 3.4.24.B33 | 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 |
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