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Literature summary for 2.6.1.1 extracted from
- L-Phenylalanine synthesis catalyzed by immobilized aspartate aminotransferase (2012), Biochem. Eng. J., 63, 15-21.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | an enzymatic method for the synthesis of the amino acid Phe is developed. AAT from porcine heart is immobilized by covalent attachment and entrapment, and the resulting immobilized preparations are compared to the soluble enzyme both in terms of stability and reaction efficiency | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-aspartate + phenylpyruvate | - |
Sus scrofa | oxaloacetate + L-phenylalanine | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AAT | - |
Sus scrofa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Sus scrofa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Sus scrofa |
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Release 2023.1 (January 2023)
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