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

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

Stable Identifier

R-HSA-71118

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

phenylalanine + tetrahydrobiopterin + O2 => tyrosine + 4a-hydroxytetrahydrobiopterin + H2O

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

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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, Güttler, 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