Molecular Cloning and Recombinant Expression of the Human Liver Phenylalanine Hydroxylase Stimulating Factor Revealed Structural and Functional Identity to the ... View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1993

AUTHORS

Beat Thöny , Frank Neuheiser , Charles R. Hauer , Claus W. Heizmann

ABSTRACT

Conversion of phenylalanine to tyrosine by the cytosolic liver enzyme phenylalanine hydroxylase (PAH) requires phenylalanine, molecular O2 and the obligatory cofactor tetrahydrobiopterin (BH4)1.The phenylalanine hydroxylation produces stoichiometrically an oxidized BH4 intermediate, the pterin-4α-carbinolamine (4α-CA). This unstable intermediate is proposed to be dehydrated to the quinonoid dihydrobiopterin (q-BH2) by the phenylalanine hydroxylase stimulating factor (PHS; also termed pterin-4α-carbinolamine dehydratase)2. The presence of the dihydropteridine reductase (DHPR) together with NADH completes the reductive recycling of the BH4 cofactor. A deficiency in PAH, PHS or DHPR leads to different forms of hyperphenylalaninemia3. More... »

PAGES

103-6

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-2960-6_20

DOI

http://dx.doi.org/10.1007/978-1-4615-2960-6_20

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044990053

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8304090


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