Structural interpretation of mutations in phenylalanine hydroxylase protein aids in identifying genotype–phenotype correlations in phenylketonuria
✍ Scribed by Jennings, Ian G; Cotton, Richard GH; Kobe, Bostjan
- Book ID
- 110025011
- Publisher
- Nature Publishing Group
- Year
- 2000
- Tongue
- English
- Weight
- 930 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1018-4813
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When analyzed in the context of the phenylalanine hydroxylase (PAH) three-dimensional structure, only a minority of the PKU mutations described world-wide affect catalytic residues. Consistent with these observations, recent data point to defective folding and subsequent aggregation/degradation as a
Mutations in the human phenylalanine hydroxylase gene (PAH) altering the expressed cDNA nucleotide sequence (GenBank U49897) can impair activity of the corresponding enzyme product (hepatic phenylalanine hydroxylase, PAH) and cause hyperphenylalaninemia (HPA), a metabolic phenotype for which the maj