×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

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 P04176
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)

P04176
PH4H_RAT
Rattus norvegicus
Phenylalanine-4-hydroxylase

PDB Structure

PDB 5EGQ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
Meisburger, S.P., Taylor, A.B., Khan, C.A., Zhang, S., Fitzpatrick, P.F., Ando, N.
J.Am.Chem.Soc.
CATH-Gene3D is a Global Biodata Core Resource Learn more...