Any feedback?
Literature summary for 1.14.16.1 extracted from
- Searching distant homologs of the regulatory ACT domain in phenylalanine hydroxylase (2008), Amino Acids, 36, 235-249.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine + tetrahydrobiopterin + O2 | Homo sapiens | impact of the enzyme structure on its regulation, overview | L-tyrosine + 4a-hydroxytetrahydrobiopterin | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-phenylalanine + tetrahydrobiopterin + O2 | - |
Homo sapiens | L-tyrosine + 4a-hydroxytetrahydrobiopterin | - |
? | |
| L-phenylalanine + tetrahydrobiopterin + O2 | impact of the enzyme structure on its regulation, overview | Homo sapiens | L-tyrosine + 4a-hydroxytetrahydrobiopterin | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the N-terminal regulatory domain is an ACT domain, a small molecule-binding domain characterized by high sequence divergence and evolutionary mobility. The ACT domain displays a ferredoxin-like fold, structure comparison with ACT and ACT-like proteins and analysis, a GAL-IESRP motif is located at the interface between the interacting regulatory and catalytic domains, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAH | - |
Homo sapiens |
| phenylalanine hydroxylase | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| tetrahydrobiopterin | - |
Homo sapiens | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
