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

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

Mitchell, JJ, Trakadis, YJ, Scriver, CR

Genet. Med. 2011
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
Participants
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Participant Of
hasEvent
Catalyst Activity
Catalyst Activity
Title
phenylalanine 4-monooxygenase activity of PAH S40L:Fe2+ tetramer [cytosol]
Physical Entity
PAH S40L:Fe2+ tetramer [cytosol]
Activity
phenylalanine 4-monooxygenase activity (0004505)
Normal reaction
PAH:Fe2+ tetramer hydroxylates L-Phe to L-Tyr (Homo sapiens)
Disease
Name Identifier Synonyms
phenylketonuria 9281 PKU, maternal phenylketonuria, Følling's disease, phenylalaninemia
Authored
Jassal, B  (2014-12-08)
Reviewed
D'Eustachio, P  (2015-01-28)
Created
Jassal, B  (2014-11-20)
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