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
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
21555948 Phenylalanine hydroxylase deficiency

Scriver, CR, Trakadis, YJ, Mitchell, JJ

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
Authored
Jassal, B  (2014-12-08)
Reviewed
D'Eustachio, P  (2015-01-28)
Created
Jassal, B  (2014-11-20)
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