CATH Classification

Domain Context

CATH Clusters

Superfamily Aromatic amino acid hydroxylase
Functional Family

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 1J8U
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.
Andersen, O.A., Flatmark, T., Hough, E.
J.Mol.Biol.