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Literature summary for 3.4.21.74 extracted from
- Biochemistry and pharmacology of proteins and peptides purified from the venoms of the snakes Macrovipera lebetina subspecies (2019), Toxicon, 158, 16-32 .
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | the enzyme may be useful for developing potential diagnostic agents for detecting coagulation disorders | Macrovipera lebetina lebetina |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diisopropylfluorophosphate | - |
Macrovipera lebetina |  |
| additional information | no inhibition by EDTA | Macrovipera lebetina | |
| PMSF | - |
Macrovipera lebetina | |
| PMSF | - |
Macrovipera lebetina lebetina | |
| Soybean trypsin inhibitor | partial inhibition | Macrovipera lebetina |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Macrovipera lebetina | - |
- |
| extracellular | - |
Macrovipera lebetina cernovi | - |
- |
| extracellular | - |
Macrovipera lebetina lebetina | - |
- |
| extracellular | - |
Macrovipera lebetina obtusa | - |
- |
| extracellular | - |
Macrovipera lebetina transmediterranea | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fibrinogen + H2O | Macrovipera lebetina | cleavage in the alpha-chain | fibrin + fibrinopeptide A | - |
? | |
| fibrinogen + H2O | Macrovipera lebetina | cleavage in the alpha-chain, low activity | fibrin + fibrinopeptide A | - |
? | |
| fibrinogen + H2O | Macrovipera lebetina | cleavage in the beta-chain | fibrin + fibrinopeptide B | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Macrovipera lebetina | E0Y419 | turanica | - |
| Macrovipera lebetina | Q8JH85 | turanica | - |
| Macrovipera lebetina cernovi | - |
- |
- |
| Macrovipera lebetina lebetina | - |
- |
- |
| Macrovipera lebetina obtusa | - |
- |
- |
| Macrovipera lebetina transmediterranea | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| venom | Latoxan, toxin profile, overview | Macrovipera lebetina lebetina | - |
| venom | the proteome of the Macrovipera lebetina transmediterranea venom is estimated to belong to a limited protein families: natriuretic peptides, short disintegrin, dimeric disintegrin, disintegrin/cystein rich protein, C-type lectin-like protein, vascular endothelial growth factor (VEGF), Zn2+ metalloproteinases, serine proteinases, phospholipase A2. L-amino acid oxidase, hyaluronidase, phosphodiesterase, 5'-nucleotidase, nerve growth factor have not been identified by this proteomic analysis, toxin profile, overview | Macrovipera lebetina transmediterranea | - |
| venom | toxin profile, overview | Macrovipera lebetina | - |
| venom | toxin profile, overview | Macrovipera lebetina cernovi | - |
| venom | venom from the Armenian mountain viper Macrovipera lebetina obtusa contains proteins of only 9 families: Zn2+-dependent metalloproteinases, serine proteinases, PLA2, L-amino acid oxidase, C-type lectin-like protein, cysteine-rich secretory protein (CRISP), monomeric and dimeric disintegrins, DC-fragment and bradykinin-potentiating/C-natriuretic peptides (BPP/C-NP), toxin profile, overview | Macrovipera lebetina obtusa | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fibrinogen + H2O | cleavage in the alpha-chain | Macrovipera lebetina | fibrin + fibrinopeptide A | - |
? | |
| fibrinogen + H2O | cleavage in the alpha-chain, low activity | Macrovipera lebetina | fibrin + fibrinopeptide A | - |
? | |
| fibrinogen + H2O | cleavage in the beta-chain | Macrovipera lebetina | fibrin + fibrinopeptide B | - |
? | |
| additional information | the enzyme shows no esterolytic activity | Macrovipera lebetina | ? | - |
? | |
| additional information | the thrombin-like enzyme VLCII hydrolyzes the chromogenic substrate Nalpha-benzyloxycarbonyl-L-arginine-4-nitroanilide hydrochloride, but not benzoylarginine ethyl ester (BAEE). The enzyme shows high coagulant activity against human plasma and cleaved both Aalpha- and Bbeta-chain of bovine fibrinogen | Macrovipera lebetina lebetina | ? | - |
? | |
| Nalpha-benzyloxycarbonyl-L-arginine-4-nitroanilide + H2O | - |
Macrovipera lebetina lebetina | Nalpha-benzyloxycarbonyl-L-arginine + 4-nitroaniline | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 60000, SDS-PAGE | Macrovipera lebetina lebetina |
| ? | x * 42200, SDS-PAGE | Macrovipera lebetina |
| ? | x * 31100, SDS-PAGE | Macrovipera lebetina |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-Fibrinogenase | - |
Macrovipera lebetina |
| beta-fibrinogenase | - |
Macrovipera lebetina |
| coagulant serine protease | - |
Macrovipera lebetina lebetina |
| VLAF | - |
Macrovipera lebetina |
| VLBF | - |
Macrovipera lebetina |
| VLCII | - |
Macrovipera lebetina lebetina |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Macrovipera lebetina | below | - |
3 |
| Macrovipera lebetina | above | - |
9.3 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina |
| metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina cernovi |
| metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina lebetina |
| metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina obtusa |
| metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina transmediterranea |
| physiological function | the enzyme degrades the fibrinogen alpha-chain. VLAF is active on casein but not on esters and amides of arginine. It splits the oxidized insulin B-chain at Tyr16-Leu17, Phe24-Phe25 and Phe25-Tyr26, and glucagon at Tyr10-Ser11, Leu14-Asp15 and Leu26-Met27. Alpha-fibrinogenase has N-terminal similarity with snake venom arginine esterases but does not hydrolyze the esters of arginine, lysine and tyrosine. The enzyme has strong proteolytic activity and degrades the alpha-chain of fibrinogen altering its clottability by thrombin | Macrovipera lebetina |
| physiological function | VLBF cleaves in fibrinogen the Bbeta-chain first and later also the Aalpha-chain. VLBF is a glycoprotein containing 23% of neutral sugars, and has extremely high thermostability. The enzyme is active on esters and amides of arginine, but not lysine esters. Beta-fibrinogenase is a typical arginine esterase, which hydrolyzes esters and amides of arginine and attacks mainly the beta-chain of fibrinogen | Macrovipera lebetina |
| physiological function | VLCII displays proaggregating effect on human platelet in a concentration-dependent manner with absence of lag time | Macrovipera lebetina lebetina |
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Release 2023.1 (January 2023)
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