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Literature summary 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
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.21.74 | analysis | the enzyme may be useful for developing potential diagnostic agents for detecting coagulation disorders | Macrovipera lebetina lebetina |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.95 | cloning from venom gland cDNA library, DNA and amino acid sequence determination and analysis | Macrovipera lebetina |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.74 | diisopropylfluorophosphate | - |
Macrovipera lebetina |  |
| 3.4.21.74 | additional information | no inhibition by EDTA | Macrovipera lebetina | |
| 3.4.21.74 | PMSF | - |
Macrovipera lebetina | |
| 3.4.21.74 | PMSF | - |
Macrovipera lebetina lebetina | |
| 3.4.21.74 | Soybean trypsin inhibitor | partial inhibition | Macrovipera lebetina | |
| 3.4.21.95 | diisopropylfluorophosphate | - |
Macrovipera lebetina | |
| 3.4.21.95 | PMSF | - |
Macrovipera lebetina | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.74 | extracellular | - |
Macrovipera lebetina | - |
- |
| 3.4.21.74 | extracellular | - |
Macrovipera lebetina cernovi | - |
- |
| 3.4.21.74 | extracellular | - |
Macrovipera lebetina lebetina | - |
- |
| 3.4.21.74 | extracellular | - |
Macrovipera lebetina obtusa | - |
- |
| 3.4.21.74 | extracellular | - |
Macrovipera lebetina transmediterranea | - |
- |
| 3.4.21.95 | extracellular | - |
Macrovipera lebetina | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.74 | fibrinogen + H2O | Macrovipera lebetina | cleavage in the alpha-chain | fibrin + fibrinopeptide A | - |
? | |
| 3.4.21.74 | fibrinogen + H2O | Macrovipera lebetina | cleavage in the alpha-chain, low activity | fibrin + fibrinopeptide A | - |
? | |
| 3.4.21.74 | fibrinogen + H2O | Macrovipera lebetina | cleavage in the beta-chain | fibrin + fibrinopeptide B | - |
? | |
| 3.4.21.95 | factor V + H2O | Macrovipera lebetina | activation | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.74 | Macrovipera lebetina | E0Y419 | turanica | - |
| 3.4.21.74 | Macrovipera lebetina | Q8JH85 | turanica | - |
| 3.4.21.74 | Macrovipera lebetina cernovi | - |
- |
- |
| 3.4.21.74 | Macrovipera lebetina lebetina | - |
- |
- |
| 3.4.21.74 | Macrovipera lebetina obtusa | - |
- |
- |
| 3.4.21.74 | Macrovipera lebetina transmediterranea | - |
- |
- |
| 3.4.21.95 | Macrovipera lebetina | Q9PT41 | turanica | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.74 | venom | Latoxan, toxin profile, overview | Macrovipera lebetina lebetina | - |
| 3.4.21.74 | 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 | - |
| 3.4.21.74 | venom | toxin profile, overview | Macrovipera lebetina | - |
| 3.4.21.74 | venom | toxin profile, overview | Macrovipera lebetina cernovi | - |
| 3.4.21.74 | 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 | - |
| 3.4.21.95 | venom | toxin profile, overview | Macrovipera lebetina | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.74 | fibrinogen + H2O | cleavage in the alpha-chain | Macrovipera lebetina | fibrin + fibrinopeptide A | - |
? | |
| 3.4.21.74 | fibrinogen + H2O | cleavage in the alpha-chain, low activity | Macrovipera lebetina | fibrin + fibrinopeptide A | - |
? | |
| 3.4.21.74 | fibrinogen + H2O | cleavage in the beta-chain | Macrovipera lebetina | fibrin + fibrinopeptide B | - |
? | |
| 3.4.21.74 | additional information | the enzyme shows no esterolytic activity | Macrovipera lebetina | ? | - |
? | |
| 3.4.21.74 | 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 | ? | - |
? | |
| 3.4.21.74 | Nalpha-benzyloxycarbonyl-L-arginine-4-nitroanilide + H2O | - |
Macrovipera lebetina lebetina | Nalpha-benzyloxycarbonyl-L-arginine + 4-nitroaniline | - |
? | |
| 3.4.21.95 | Benzoylarginine ethyl ester + H2O | - |
Macrovipera lebetina | ? | - |
? | |
| 3.4.21.95 | factor V + H2O | activation | Macrovipera lebetina | ? | - |
? | |
| 3.4.21.95 | additional information | enzyme VLFVA hydrolyses several synthetic arginine ester substrates, such as benzoylarginine ethyl ester (BAEE), tosylarginine methyl ester (TAME) and amide substrates such as Pro-Phe-Arg-MCA | Macrovipera lebetina | ? | - |
? | |
| 3.4.21.95 | Pro-Phe-Arg-7-amido-4-methyl coumarin + H2O | - |
Macrovipera lebetina | Pro-Phe-Arg + 7-amino-4-methyl coumarin | - |
? | |
| 3.4.21.95 | tosylarginine methyl ester + H2O | - |
Macrovipera lebetina | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.74 | ? | x * 60000, SDS-PAGE | Macrovipera lebetina lebetina |
| 3.4.21.74 | ? | x * 42200, SDS-PAGE | Macrovipera lebetina |
| 3.4.21.74 | ? | x * 31100, SDS-PAGE | Macrovipera lebetina |
| 3.4.21.95 | ? | x * 28400, SDS-PAGE | Macrovipera lebetina |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.74 | alpha-Fibrinogenase | - |
Macrovipera lebetina |
| 3.4.21.74 | beta-fibrinogenase | - |
Macrovipera lebetina |
| 3.4.21.74 | coagulant serine protease | - |
Macrovipera lebetina lebetina |
| 3.4.21.74 | VLAF | - |
Macrovipera lebetina |
| 3.4.21.74 | VLBF | - |
Macrovipera lebetina |
| 3.4.21.74 | VLCII | - |
Macrovipera lebetina lebetina |
| 3.4.21.95 | Factor V activator | - |
Macrovipera lebetina |
| 3.4.21.95 | VLFVA | - |
Macrovipera lebetina |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.21.74 | Macrovipera lebetina | below | - |
3 |
| 3.4.21.74 | Macrovipera lebetina | above | - |
9.3 |
| 3.4.21.95 | Macrovipera lebetina | above | - |
9.3 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.21.74 | metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina |
| 3.4.21.74 | metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina cernovi |
| 3.4.21.74 | metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina lebetina |
| 3.4.21.74 | metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina obtusa |
| 3.4.21.74 | metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina transmediterranea |
| 3.4.21.74 | 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 |
| 3.4.21.74 | 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 |
| 3.4.21.74 | physiological function | VLCII displays proaggregating effect on human platelet in a concentration-dependent manner with absence of lag time | Macrovipera lebetina lebetina |
| 3.4.21.95 | evolution | the amino acid sequence of VLFVA shows significant homology with snake venom and mammalian serine proteinases. The other sequences (VLP2, VLP3 and VLP4) are homologous to VLFVA, but have two principal discrepancies in the translated protein sequence in comparison with snake venom serine protease structures: in the active site triad Ser195 is replaced by Asn195 and His57 by Arg57. Sequences of VLP3 and VLP4 represent combinations of VLFVA and VLP2 clones | Macrovipera lebetina |
| 3.4.21.95 | metabolism | proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview | Macrovipera lebetina |
| 3.4.21.95 | physiological function | the enzyme VLFVA has the ability to activate factor V | Macrovipera lebetina |
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Release 2023.1 (January 2023)
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