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
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
Dynamic regulation of phenylalanine hydroxylase
Pteridines, 2014 Phenylalanine hydroxylase (PAH) is the key enzyme in phenylalanine metabolism, catalyzing its oxidative breakdown to tyrosine. Its function in the committed step of amino acid metabolism requires strict regulation. Thus, several regulatory mechanisms are
Fuchs Julian E. +2 more
doaj +3 more sources
Conformational selection turns on phenylalanine hydroxylase. [PDF]
J Biol Chem, 2018 Phenylalanine hydroxylase catalyzes a critical step in the phenylalanine catabolic pathway, and impairment of the human enzyme is linked to phenylketonuria. Phenylalanine is also a positive allosteric regulator of the enzyme, and the allosteric binding site has been determined by crystallography.
Konovalov KA, Wang W, Huang X.
europepmc +6 more sources
Investigation of five common mutations on Phenylalanine Hydroxylase Gene of Phenylketonuria Patients from Two Provinces in North of Iran [PDF]
International Journal of Preventive Medicine, 2017 Background: There are more than 500 different mutations on phenylalanine hydroxylase (PAH) gene that is responsible for phenylketonuria (PKU) diseases and the spectrum of these mutations is varied in different populations. The main clinical manifestation
Daniel Zamanfar +5 more
doaj +2 more sources
Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase. [PDF]
J Biol Chem, 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 ...
Zhang S, Fitzpatrick PF.
europepmc +4 more sources
In Vivo Studies of Phenylalanine Hydroxylase by Phenylalanine Breath Test: Diagnosis of Tetrahydrobiopterin-Responsive Phenylalanine Hydroxylase Deficiency [PDF]
Pediatric Research, 2004 Tetrahydrobiopterin (BH4)-responsive phenylalanine hydroxylase (PAH) deficiency is characterized by reduction of blood phenylalanine level after a BH4-loading test. Most cases of BH4-responsive PAH deficiency include mild phenylketonuria (PKU) or mild hyperphenylalaninemia (HPA), but not all patients with mild PKU respond to BH4.
Yoshiyuki Okano +9 more
openalex +3 more sources
The Isoenzymes of Phenylalanine Hydroxylase in Humans [PDF]
Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 1977 Charles E. Parker +3 more
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