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Literature summary extracted from
- Genome sequencing, purification, and biochemical characterization of a strongly fibrinolytic enzyme from Bacillus amyloliquefaciens Jxnuwx-1 isolated from Chinese traditional douchi (2020), J. Gen. Appl. Microbiol., 66, 153-162.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.B66 | DNA and amino acid sequence determination and analysis, genetic ontology | Bacillus amyloliquefaciens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.B66 | EDTA | almost complete inhibition | Bacillus amyloliquefaciens |  |
| 3.4.21.B66 | Fe2+ | 18.96% inhibition at 5 mM | Bacillus amyloliquefaciens | |
| 3.4.21.B66 | Fe3+ | 35.63% inhibition at 5 mM | Bacillus amyloliquefaciens | |
| 3.4.21.B66 | PMSF | 19.27% inhibition at 5 mM | Bacillus amyloliquefaciens | |
| 3.4.21.B66 | Soybean trypsin inhibitor | 73.19% inhibition at 5 mM | Bacillus amyloliquefaciens |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.B66 | Ca2+ | 31.61% activation at 5 mM | Bacillus amyloliquefaciens | |
| 3.4.21.B66 | Co2+ | 46.16% activation at 5 mM | Bacillus amyloliquefaciens | |
| 3.4.21.B66 | Cu2+ | 31.61% activation at 5 mM | Bacillus amyloliquefaciens | |
| 3.4.21.B66 | Mg2+ | 31.61% activation at 5 mM | Bacillus amyloliquefaciens | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.B66 | Fibrin + H2O | Bacillus amyloliquefaciens | - |
? | - |
? | |
| 3.4.21.B66 | Fibrin + H2O | Bacillus amyloliquefaciens Jxnuwx-1 | - |
? | - |
? | |
| 3.4.21.B66 | Fibrinogen + H2O | Bacillus amyloliquefaciens | - |
? | - |
? | |
| 3.4.21.B66 | Fibrinogen + H2O | Bacillus amyloliquefaciens Jxnuwx-1 | - |
? | - |
? | |
| 3.4.21.B66 | additional information | Bacillus amyloliquefaciens | the enzyme degrades both fibrinogen and fibrin, displaying its highest degrading activity towards the Aalpha-chains followed by Bbeta chains and Cgamma chains. The enzyme is also activated by plasminogen, indicating its ability to degrade fibrinogen and fibrin in two ways: (a) by activating plasminogen conversion into plasmin (plasminogen activator activity), or (b) by direct hydrolysis. It degrades thrombin. Mode of hydrolysis of fibrinogen and fibrin by the enzyme, overview | ? | - |
- |
|
| 3.4.21.B66 | additional information | Bacillus amyloliquefaciens Jxnuwx-1 | the enzyme degrades both fibrinogen and fibrin, displaying its highest degrading activity towards the Aalpha-chains followed by Bbeta chains and Cgamma chains. The enzyme is also activated by plasminogen, indicating its ability to degrade fibrinogen and fibrin in two ways: (a) by activating plasminogen conversion into plasmin (plasminogen activator activity), or (b) by direct hydrolysis. It degrades thrombin. Mode of hydrolysis of fibrinogen and fibrin by the enzyme, overview | ? | - |
- |
|
| 3.4.21.B66 | plasminogen + H2O | Bacillus amyloliquefaciens | - |
? | - |
? | |
| 3.4.21.B66 | plasminogen + H2O | Bacillus amyloliquefaciens Jxnuwx-1 | - |
? | - |
? | |
| 3.4.21.B66 | thrombin + H2O | Bacillus amyloliquefaciens | - |
? | - |
? | |
| 3.4.21.B66 | thrombin + H2O | Bacillus amyloliquefaciens Jxnuwx-1 | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.B66 | Bacillus amyloliquefaciens | A0AAQ2MQD8 | Bacillus velezensis, isolated from chinese traditional douchi, traditional fermented black soya bean | - |
| 3.4.21.B66 | Bacillus amyloliquefaciens Jxnuwx-1 | A0AAQ2MQD8 | Bacillus velezensis, isolated from chinese traditional douchi, traditional fermented black soya bean | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 1.5 | - |
purified enzyme, substrate N-benzoyl-Phe-Val-Arg-4-nitroanilide, pH 7.8, 37°C | Bacillus amyloliquefaciens |
| 3.4.21.B66 | 4.74 | - |
purified enzyme, substrate N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide, pH 7.8, 37°C | Bacillus amyloliquefaciens |
| 3.4.21.B66 | 33.13 | - |
purified enzyme, substrate N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, pH 7.8, 37°C | Bacillus amyloliquefaciens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.B66 | Fibrin + H2O | - |
Bacillus amyloliquefaciens | ? | - |
? | |
| 3.4.21.B66 | Fibrin + H2O | analysis of the cleavage patterns in fibrin | Bacillus amyloliquefaciens | ? | - |
? | |
| 3.4.21.B66 | Fibrin + H2O | - |
Bacillus amyloliquefaciens Jxnuwx-1 | ? | - |
? | |
| 3.4.21.B66 | Fibrinogen + H2O | - |
Bacillus amyloliquefaciens | ? | - |
? | |
| 3.4.21.B66 | Fibrinogen + H2O | - |
Bacillus amyloliquefaciens Jxnuwx-1 | ? | - |
? | |
| 3.4.21.B66 | additional information | the enzyme degrades both fibrinogen and fibrin, displaying its highest degrading activity towards the Aalpha-chains followed by Bbeta chains and Cgamma chains. The enzyme is also activated by plasminogen, indicating its ability to degrade fibrinogen and fibrin in two ways: (a) by activating plasminogen conversion into plasmin (plasminogen activator activity), or (b) by direct hydrolysis. It degrades thrombin. Mode of hydrolysis of fibrinogen and fibrin by the enzyme, overview | Bacillus amyloliquefaciens | ? | - |
- |
|
| 3.4.21.B66 | additional information | the enzyme is most likely a serine metalloprotease and belongs to the S8 family peptidases, comparison to other fibrinolytic enzymes some of which are also serine metalloproteases, overview. It also shows amidolytic activity. No activity with N-succinyl-Ala-Ala-Ala-4-nitroanilide | Bacillus amyloliquefaciens | ? | - |
- |
|
| 3.4.21.B66 | additional information | the enzyme degrades both fibrinogen and fibrin, displaying its highest degrading activity towards the Aalpha-chains followed by Bbeta chains and Cgamma chains. The enzyme is also activated by plasminogen, indicating its ability to degrade fibrinogen and fibrin in two ways: (a) by activating plasminogen conversion into plasmin (plasminogen activator activity), or (b) by direct hydrolysis. It degrades thrombin. Mode of hydrolysis of fibrinogen and fibrin by the enzyme, overview | Bacillus amyloliquefaciens Jxnuwx-1 | ? | - |
- |
|
| 3.4.21.B66 | N-(p-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O | - |
Bacillus amyloliquefaciens | N-(p-tosyl)-Gly-Pro-Lys + 4-nitroaniline | - |
? | |
| 3.4.21.B66 | N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O | - |
Bacillus amyloliquefaciens | N-benzoyl-Phe-Val-Arg + 4-nitroaniline | - |
? | |
| 3.4.21.B66 | N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | - |
Bacillus amyloliquefaciens | N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
| 3.4.21.B66 | plasminogen + H2O | - |
Bacillus amyloliquefaciens | ? | - |
? | |
| 3.4.21.B66 | plasminogen + H2O | - |
Bacillus amyloliquefaciens Jxnuwx-1 | ? | - |
? | |
| 3.4.21.B66 | thrombin + H2O | - |
Bacillus amyloliquefaciens | ? | - |
? | |
| 3.4.21.B66 | thrombin + H2O | - |
Bacillus amyloliquefaciens Jxnuwx-1 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.B66 | ? | x * 29000, SDS-PAGE | Bacillus amyloliquefaciens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.B66 | fibrinogenolytic enzyme | - |
Bacillus amyloliquefaciens |
| 3.4.21.B66 | fibrinolytic enzyme | - |
Bacillus amyloliquefaciens |
| 3.4.21.B66 | S8 family peptidase | UniProt | Bacillus amyloliquefaciens |
| 3.4.21.B66 | subtilisin-like serine metalloprotease | - |
Bacillus amyloliquefaciens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 41 | - |
- |
Bacillus amyloliquefaciens |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 23 | 55 | activity range | Bacillus amyloliquefaciens |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 23 | 43 | purified enzyme, over 80% activity remaining after 30 min incubation. Relative activity and thermostability of the purified enzyme sharply decreased above 43°C. Inactivation at 53°C | Bacillus amyloliquefaciens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 7.6 | - |
- |
Bacillus amyloliquefaciens |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 7.2 | 8 | activity range, 70% of maximal activity at pH 7.2 and pH 8.0 | Bacillus amyloliquefaciens |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.B66 | 7 | 11 | stable at, 40% activity remaining at pH 6.0, inactivation at pH 5.0 and pH 12.0 | Bacillus amyloliquefaciens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.21.B66 | evolution | the enzyme belongs to the S8 family peptidases. It is most likely a serine metalloprotease and belongs to the S8 family peptidases, comparison to other fibrinolytic enzymes some of which are also serine metalloproteases, overview | Bacillus amyloliquefaciens |
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