Modulation of Human Phenylalanine Hydroxylase by 3-Hydroxyquinolin-2(1H)-One Derivatives [PDF]
Biomolecules, 2021 Phenylketonuria (PKU) is a genetic disease caused by deficient activity of human phenylalanine hydroxylase (hPAH) that, when untreated, can lead to severe psychomotor impairment.
Raquel R. Lopes +12 more
doaj +2 more sources
The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase [PDF]
Nature Communications, 2021 Phenylketonuria (PKU) is caused by autosomal recessive variants in phenylalanine hydroxylase (PAH) and can lead to neurotoxicity. Here the authors describe a mouse model of PKU based on a mutation in phenylalanine hydroxylase (R261Q) which replicates ...
Oscar Aubi +11 more
doaj +2 more sources
Phenylalanine hydroxylase mRNA rescues the phenylketonuria phenotype in mice [PDF]
Frontiers in Bioengineering and Biotechnology, 2022 Phenylketonuria (PKU) is an inborn error of metabolism caused by a deficiency in functional phenylalanine hydroxylase (PAH), resulting in accumulation of phenylalanine (Phe) in patients’ blood and organs.
Maximiliano L. Cacicedo +11 more
doaj +2 more sources
Concurrent Phenylalanine Hydroxylase–Related Disorder and Celiac: A Rare Co-occurrence With Implications for Clinical Management [PDF]
Annals of Internal Medicine: Clinical CasesComorbid nutritional disorders can present with clinical management challenges. Phenylalanine hydroxylase (PAH) deficiency and celiac disease are both associated with dietary protein intolerance, yet they are different disorders.
Jade Jensen +6 more
doaj +2 more sources
Optical Coherence Tomography to Assess Neurodegeneration in Phenylalanine Hydroxylase Deficiency [PDF]
Frontiers in Neurology, 2021 In phenylalanine hydroxylase (PAH) deficiency, an easily feasible method to access the progression of neurodegeneration is warranted to contribute to current discussions on treatment indications and targets.
Amelie S. Lotz-Havla +9 more
doaj +2 more sources
Allosteric regulation of phenylalanine hydroxylase [PDF]
Archives of Biochemistry and Biophysics, 2012 The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin.
Paul Fitzpatrick
exaly +3 more sources
Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase [PDF]
Journal of Biological Chemistry, 2016 Liver phenylalanine hydroxylase (PheH) is an allosteric enzyme that requires activation by phenylalanine for full activity. The location of the allosteric site for phenylalanine has not been established. NMR spectroscopy of the isolated regulatory domain (RDPheH(25-117) is the regulatory domain of PheH lacking residues 1-24) of the rat enzyme in the ...
Shengnan, Zhang, Paul F, Fitzpatrick
openaire +3 more sources
Phenylalanine–tyrosine–catecholamine axis disorders: pathways, molecular diagnosis, therapeutics, and emerging translational monitoring technologies [PDF]
Frontiers in Molecular BiosciencesDisorders of the phenylalanine–tyrosine–catecholamine axis are a clinically relevant group of neurometabolic conditions in which pathogenic variants in key enzymes impair dopamine and norepinephrine biosynthesis.
Martina Isabella Armas Samaniego +12 more
doaj +2 more sources
Detection of IVS4+1G>A mutation in phenylalanine hydroxylase gene in North of Iran using PCR-sequencing [PDF]
Journal of Shahrekord University of Medical Sciences, 2023 Background and aims: Phenylketonuria (PKU) is an autosomal recessive disorder of phenylalanine (Phe) metabolism. Mutations in the phenylalanine hydroxylase (PAH) gene are the main reason for the incidence of PKU.
Maryam Amini Chelak +1 more
doaj +1 more source
Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2019 Martin Alcorlo Pages +2 more
exaly +2 more sources