Defective PAH does not hydroxylate L-Phe to L-Tyr

Stable Identifier
R-HSA-5649483
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Defective PAH does not hydroxylate 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
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
21555948 Phenylalanine hydroxylase deficiency

Mitchell, JJ, Trakadis, YJ, Scriver, CR

Genet. Med. 2011
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Catalyst Activity

phenylalanine 4-monooxygenase activity of PAH S40L:Fe2+ tetramer [cytosol]

Physical Entity
PAH S40L:Fe2+ tetramer [cytosol] (Homo sapiens)
Activity
phenylalanine 4-monooxygenase activity (GO:0004505)
Normal reaction
PAH:Fe2+ tetramer hydroxylates L-Phe to L-Tyr (Homo sapiens)
Functional status

Loss of function of PAH S40L:Fe2+ tetramer [cytosol]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
phenylketonuria DOID:9281 PKU, maternal phenylketonuria, Følling's disease, phenylalaninemia
Cross References
Mondo
Authored
Jassal, B  (2014-12-08)
Reviewed
D'Eustachio, P  (2015-01-28)
Created
Jassal, B  (2014-11-20)
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