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

(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 => (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine, phenylalanine + tetrahydrobiopterin + O2 => tyrosine + 4a-hydroxytetrahydrobiopterin + H2O

ReviewStatus

5/5

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

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Cytosolic phenylalanine hydroxylase (PAH) catalyzes the reaction of phenylalanine, molecular oxygen and tetrahydrobiopterin (BH4) to form tyrosine, water, and 4 alpha-hydroxytetrahydrobiopterin (4aOH-BH4) (Fusetti et al. 1998; Andersen et al. 2002). Defects in PAH lead to phenylalanine accumulation and the formation of abnormally high levels of phenylpyruvate, and phenyllactate (Guldberg et al. 1996) 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 Guldberg, P, Mallmann, R, Henriksen, KF, Güttler, F	Hum Mutat	1996
12126628	Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation Andersen, OA, Flatmark, T, Hough, E	J Mol Biol	2002