Associated Papers
The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.
Khan CA et al.
The Journal of Biological Chemistry, 2019
Recombinant heteromeric phenylalanine monooxygenase and the oxygenation of carbon and sulfur substrates.
Boonyapiwat B et al.
The Journal of Pharmacy and Pharmacology, 2011
The activity of wild type and mutant phenylalanine hydroxylase with respect to the C-oxidation of phenylalanine and the S-oxidation of S-carboxymethyl-L-cysteine.
Steventon GB et al.
Molecular Genetics and Metabolism, 2009
The activity of wild-type and mutant phenylalanine hydroxylase and its regulation by phenylalanine and tetrahydrobiopterin at physiological and pathological concentrations: an isothermal titration calorimetry study.
Pey AL et al.
Molecular Genetics and Metabolism, 2005
Kinetic and stability analysis of PKU mutations identified in BH4-responsive patients.
Pérez B et al.
Molecular Genetics and Metabolism, 2005
Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations.
Pey AL et al.
Human Mutation, 2004
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