EC Number   |
Application |
Reference |
|---|
    4.3.1.25 | analysis |
rapid quantization of Phe and Tyr in plasma and serum from subjects with phenylketonuria |
34341 |
| 4.3.1.25 | food industry |
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients |
-, 748347 |
| 4.3.1.25 | medicine |
enzyme substitution therapy for the treatment of phenylketonuria |
749285 |
| 4.3.1.25 | nutrition |
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients |
-, 748347 |
| 4.3.1.25 | pharmacology |
enzyme substitution therapy for the treatment of phenylketonuria |
749285 |
| 4.3.1.25 | pharmacology |
the enzyme is a useful biocatalyst for removal of L-phenylalanine from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for phenylketonuria patients. The enzyme is also capable to catalyze the deamination of L-tyrosine to p-coumaric acid but at a substantially low reaction rate. Therefore, the final content of L-Tyr in samples treated with L-phenylalanine ammonia-lyase should be analyzed in each case and taken in consideration to avoid its deficiency in phenylketonuria patients |
-, 748347 |
| 4.3.1.25 | synthesis |
immobilization of Escherichia coli cells stably expressing the enzyme on calcium alginate beads for use in batch coversion of L-tyrosine to p-hydroxycinnamic acid. Immobilization and controlling of pH value to 9.8 results in stabilization. In 1 l batch reactions, 50 g/l tyrosine can be converted to 39 g/l p-hydroxycinnamic acid |
678905 |
| 4.3.1.25 | synthesis |
reconstructed phenylpropanoid pathway in engineered Escherichia coli or Saccharomyces cerevisiae leads to the biosynthesis of a wide range of phenylpropanoid-derived compounds, including pinocembrin, naringenin, styrene, 2',4',6'-trihydroxydihydrochalcone, trans-resveratrol, trans-cinnamic acid, p-coumarate, p-hydroxystyrene |
749285 |
| 4.3.1.25 | synthesis |
synthesis of p-hydroxycinnamic acid methyl ester, which shows antibacterial activity |
747845 |
| 4.3.1.25 | synthesis |
use of enzyme for synthesis of optically pure L-phenylalanine from trans-cinnamate |
-, 680331 |
