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Literature summary for 4.3.1.24 extracted from
- Hybrid magnetic cross-linked enzyme aggregates of phenylalanine ammonia lyase from Rhodotorula glutinis (2014), PLoS ONE, 9, 835-844.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | compared to the free enzyme, the PAL-CLEA exhibit increased stability of the enzyme against various deactivating conditions such as pH, temperature, denaturants, and organic solvents and show higher storage stability than its soluble counterpart. Additionally, PAL-CLEAs can be recycled at least for 12 consecutive batch reactions without dramatic activity loss, increases the commercial potential of PAL for synthesis of L-phenylalanine | Rhodotorula glutinis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodotorula glutinis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine | - |
Rhodotorula glutinis | (E)-cinnamate + NH3 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAL-CLEA | cross-linked enzyme aggregates of phenylalanine ammonia lyase | Rhodotorula glutinis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Rhodotorula glutinis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.8 | - |
assay at | Rhodotorula glutinis |
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