Article
Structural interpretation of mutations in phenylalanine hydroxylase protein aids in identifying genotype-phenotype correlations in phenylketonuria.
European journal of human genetics : EJHG - 1 Sept 2000
Jennings I G, Cotton R G, Kobe B
Abstract excerpt
Phenylalanine hydroxylase (PAH) is the enzyme that converts phenylalanine to tyrosine as a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis. Over 300 mutations have been identified in the gene encoding PAH that result in a deficient enzyme activity and lead to the disorders hyperphenylalaninaemia and phenylketonuria. The determination of the crystal structure of PAH now...
Topics
- Alternative Splicing
- Amino Acid Sequence
- Animals
- Binding Sites
- Crystallography, X-Ray
- Dimerization
- Frameshift Mutation
- Genotype
- Humans
- Mice
- Molecular Sequence Data
- Mutagenesis, Insertional
- Mutation
- Phenotype
- Phenylalanine Hydroxylase
- Phenylketonurias
- Protein Structure, Tertiary
- Rats