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

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
9642259	Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. Fusetti, F, Erlandsen, H, Flatmark, T, Stevens, RC	J Biol Chem	1998
8889590	Phenylalanine hydroxylase deficiency in a population in Germany: mutational profile and nine novel mutations Mallmann, R, Güttler, F, Henriksen, KF, Guldberg, P	Hum Mutat	1996
	The Metabolic and Molecular Bases of Inherited Disease, 8th ed Beaudet, AL, Scriver, CR, Sly, WS, Valle, D		2001