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Literature summary for 3.5.2.B2 extracted from
- Promiscuous (+)-gamma-lactamase activity of an amidase from nitrile hydratase pathway for efficient synthesis of carbocyclic nucleosides intermediate (2018), Bioorg. Med. Chem. Lett., 28, 1071-1076 .
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | the enzyme is an ideal catalyst for the preparation of carbocyclic nucleosides of pharmaceutical interest. IT can be used in a scalable bioprocess and is an efficient, economical, and environmentally route for producing optically pure (-)-gamma-lactam | Rhodococcus erythropolis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression in Escherichia coli BL21(DE3) | Rhodococcus erythropolis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 53.9 | - |
2-azabicyclo[2.2.1]hept-5-en-3-one | pH and temperature not specified in the publication | Rhodococcus erythropolis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus erythropolis | Q7DKE4 | - |
- |
| Rhodococcus erythropolis R4 | Q7DKE4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Rhodococcus erythropolis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-azabicyclo[2.2.1]hept-5-en-3-one + H2O | i.e. Vince lactam. Promiscuous (+)-gamma-lactamase activity of a versatile amidase involved in the nitrile degradation pathway. The kcat for Vince lactam is higher than that of acetamide and acrylamide and lower than that of propionamide and benzamide, indicating that Vince lactam is a moderate preferable substrate | Rhodococcus erythropolis | (-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid | - |
? | |
| 2-azabicyclo[2.2.1]hept-5-en-3-one + H2O | i.e. Vince lactam. Promiscuous (+)-gamma-lactamase activity of a versatile amidase involved in the nitrile degradation pathway. The kcat for Vince lactam is higher than that of acetamide and acrylamide and lower than that of propionamide and benzamide, indicating that Vince lactam is a moderate preferable substrate | Rhodococcus erythropolis R4 | (-)-2-azabicyclo[2.2.1]hept-5-en-3-one + (+)-4-amino-cyclopent-2-enecarboxylic acid | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Rhodococcus erythropolis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
1 h, the enzyme can maintain 100% of its original activity when incubated for 1 h | Rhodococcus erythropolis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 78 | - |
2-azabicyclo[2.2.1]hept-5-en-3-one | pH and temperature not specified in the publication | Rhodococcus erythropolis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Rhodococcus erythropolis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.45 | - |
2-azabicyclo[2.2.1]hept-5-en-3-one | pH and temperature not specified in the publication | Rhodococcus erythropolis | |
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