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Literature summary extracted from
- Enzymatic activities and functional characterization of a novel recombinant snake venom proteinase from Agkistrodon acutus (2009), Biochimie, 91, 277-287.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.B39 | Cu2+ | 83.8% residual activity at 3.2 mM | Deinagkistrodon acutus |  |
| 3.4.24.B39 | dithiothreitol | incubation with 5 mM dithiothreitol results in 34% inhibition of azocasein hydrolysis | Deinagkistrodon acutus | |
| 3.4.24.B39 | EDTA | 29.6% residual activitty at 5 mM | Deinagkistrodon acutus | |
| 3.4.24.B39 | additional information | aprotinin, and trypsin inhibitor SBTI do not affect the enzymatic activity | Deinagkistrodon acutus | |
| 3.4.24.B39 | phenylmethylsulfonyl fluoride | 1.2% residual activitty at 2 mM | Deinagkistrodon acutus | |
| 3.4.24.B39 | Zn2+ | 85.1% residual activity at 3.2 mM | Deinagkistrodon acutus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.24.B39 | 0.5382 | - |
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide | at pH 8.0 and 37°C | Deinagkistrodon acutus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.B39 | additional information | Ca2+, Mg2+, Na+, and K+ do not affect proteolytic activity | Deinagkistrodon acutus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B39 | Fibrin + H2O | Deinagkistrodon acutus | - |
? | - |
? | |
| 3.4.24.B39 | Fibrinogen + H2O | Deinagkistrodon acutus | the enzyme preferentially cleaves the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and finally the gamma chain | ? | - |
? | |
| 3.4.24.B39 | Fibronectin + H2O | Deinagkistrodon acutus | - |
? | - |
? | |
| 3.4.24.B39 | Oxidized insulin B-chain + H2O | Deinagkistrodon acutus | the enzyme preferentially cleaves oxidized insulin B-chain at the site of Val12-Glu13, Leu15-Tyr16, and Phe24-Phe25 | ? | - |
? | |
| 3.4.24.B39 | plasmin + H2O | Deinagkistrodon acutus | - |
? | - |
? | |
| 3.4.24.B39 | type IV collagen | Deinagkistrodon acutus | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.B39 | Deinagkistrodon acutus | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.24.B39 | venom | - |
Deinagkistrodon acutus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.B39 | azocasein + H2O | - |
Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | casein + H2O | - |
Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | D-Pro-Phe-Arg-4-nitroanilide + H2O | synthetic substrate P7959 | Deinagkistrodon acutus | D-Pro-Phe-Arg + 4-nitroaniline | - |
? | |
| 3.4.24.B39 | Fibrin + H2O | - |
Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | Fibrinogen + H2O | the enzyme preferentially cleaves the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and finally the gamma chain | Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | Fibronectin + H2O | - |
Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O | best synthetic substrate, T6140 | Deinagkistrodon acutus | N-(4-tosyl)-Gly-Pro-Lys + 4-nitroaniline | - |
? | |
| 3.4.24.B39 | N-benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O | synthetic substrate B2133 | Deinagkistrodon acutus | N-benzoyl-Pro-Phe-Arg + 4-nitroaniline | - |
? | |
| 3.4.24.B39 | Oxidized insulin B-chain + H2O | the enzyme preferentially cleaves oxidized insulin B-chain at the site of Val12-Glu13, Leu15-Tyr16, and Phe24-Phe25 | Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | plasmin + H2O | - |
Deinagkistrodon acutus | ? | - |
? | |
| 3.4.24.B39 | type IV collagen | - |
Deinagkistrodon acutus | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.B39 | fibrinogenase | - |
Deinagkistrodon acutus |
| 3.4.24.B39 | rFII | - |
Deinagkistrodon acutus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B39 | 30 | 50 | the enzyme shows highest activity between 30 and 50°C. Activity drops sharply under higher temperatures, with a complete loss of activity occurring above 60°C | Deinagkistrodon acutus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.24.B39 | 0.419 | - |
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide | at pH 8.0 and 37°C | Deinagkistrodon acutus | |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.B39 | 7 | 10.5 | the enzyme shows highest activity between pH 7.0 and 10.5. Activity drops sharply under more alkaline or acidic conditions with a complete loss of activity occurring at pH values 4.0 and 11.5 | Deinagkistrodon acutus |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.24.B39 | Deinagkistrodon acutus | isoelectric focusing | - |
9 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.B39 | physiological function | the enzyme dose-dependently inhibits platelet aggregation triggered by ADP (0.005 mM) in human platelet-rich plasma. The enzyme cannot activate plasminogen | Deinagkistrodon acutus |
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