CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.800 | Phenylalanine Hydroxylase | |
1.10.800.10 | Aromatic amino acid hydroxylase |
Domain Context
CATH Clusters
Superfamily | Aromatic amino acid hydroxylase |
Functional Family | Phenylalanine-4-hydroxylase |
Enzyme Information
1.14.16.1 |
Phenylalanine 4-monooxygenase.
based on mapping to UniProt P00439
L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin.
-!- The reaction involves an arene oxide which rearranges to give the phenolic hydroxy group. -!- This results in the hydrogen at C-4 migrating to C-3 and in part being retained, a process known as the NIH-shift. -!- The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7- dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96. -!- The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin. -!- Formerly EC 1.14.3.1 and EC 1.99.1.2.
|
UniProtKB Entries (1)
P00439 |
PH4H_HUMAN
Homo sapiens
Phenylalanine-4-hydroxylase
|
PDB Structure
PDB | 6N1K |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium.
J.Biol.Chem.
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