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Literature summary for 1.14.16.1 extracted from
- Phenylalanine monooxygenase and the sulfur oxygenation of S-carboxymethyl-L-cysteine in mice (2016), Xenobiotica, 46, 379-384 .
No PubMed abstract available
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine + tetrahydrobiopterin + O2 | Mus musculus | - |
L-tyrosine + 4a-hydroxytetrahydrobiopterin | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine + tetrahydrobiopterin + O2 | - |
Mus musculus | L-tyrosine + 4a-hydroxytetrahydrobiopterin | - |
? | |
| additional information | phenylalanine monooxygenase is the only enzyme responsible for the sulfur oxygenation of S-carboxymethyl-L-cysteine | Mus musculus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAH | - |
Mus musculus |
| phenylalanine hydroxylase | - |
Mus musculus |
| phenylalanine monooxygenase | - |
Mus musculus |
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