PAH:Fe2+ tetramer hydroxylates L-Phe to L-Tyr

Stable Identifier
R-HSA-71118
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
phenylalanine + tetrahydrobiopterin + O2 => tyrosine + 4a-hydroxytetrahydrobiopterin + H2O
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Inactivating mutations of cytosolic phenylalanine hydroxylase (PAH) block the normal reaction of phenylalanine, molecular oxygen and tetrahydrobiopterin to form tyrosine, water, and 4 alpha-hydroxytetrahydrobiopterin. Excess phenylalanine accumulates as a result, driving the formation of abnormally high levels of phenylpyruvate, and phenyllactate (Guldberg et al. 1996; Mitchell et al. 2011) in reactions not annotated here.

Literature References
PubMed ID Title Journal Year
8889590 Phenylalanine hydroxylase deficiency in a population in Germany: mutational profile and nine novel mutations

Guldberg, P, Mallmann, R, Henriksen, KF, G├╝ttler, F

Hum Mutat 1996
9642259 Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria.

Fusetti, F, Erlandsen, H, Flatmark, T, Stevens, RC

J Biol Chem 1998
  The Metabolic and Molecular Bases of Inherited Disease, 8th ed

Scriver, CR, Beaudet, AL, Valle, D, Sly, WS

  2001
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
phenylalanine 4-monooxygenase activity of PAH:Fe2+ tetramer [cytosol]
Physical Entity
Activity
Orthologous Events
Authored