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

Stable Identifier
R-HSA-5649483
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Defective PAH does not hydroxylate L-Phe to L-Tyr
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Input
Participates
as an event of
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)
Cite Us!