Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulation.
PLoS ONE, 2012 Recent clinical studies revealed increased phenylalanine levels and phenylalanine to tyrosine ratios in patients suffering from infection, inflammation and general immune activity.
Julian E Fuchs +6 more
doaj +2 more sources
Structural features of the regulatory ACT domain of phenylalanine hydroxylase. [PDF]
PLoS ONE, 2013 Phenylalanine hydroxylase (PAH) catalyzes the conversion of L-Phe to L-Tyr. Defects in PAH activity, caused by mutations in the human gene, result in the autosomal recessively inherited disease hyperphenylalaninemia. PAH activity is regulated by multiple
Carla Carluccio +4 more
doaj +2 more sources
Phenylalanine hydroxylase contributes to serotonin synthesis in mice. [PDF]
FASEB J, 2021 Serotonin is an important signaling molecule in the periphery and in the brain. The hydroxylation of tryptophan is the first and rate‐limiting step of its synthesis.
Mordhorst A +10 more
europepmc +2 more sources
Phenylalanine iminoboronates as new phenylalanine hydroxylase modulators
RSC Adv., 2014 Herein we report the discovery of new modulators of human phenylalanine hydroxylase (hPAH) inspired by the structure of its substrate and regulatorl-phenylalanine.
Rita C. Guedes +7 more
openaire +3 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.
P. Fitzpatrick
openaire +4 more sources
Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin. [PDF]
Proc Natl Acad Sci U S A, 2019 Significance The present crystal structure of phenylalanine hydroxylase (PAH) provides the 3D structure of the full-length human PAH, both unbound and complexed with the tetrahydrobiopterin (BH4) cofactor. The BH4-bound state is physiologically relevant,
Flydal MI +7 more
europepmc +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
Mutations of the phenylalanine hydroxylase gene in patients with phenylketonuria in Shanxi, China
Genetics and Molecular Biology, 2012 The variation in mutations in exons 3, 6, 7, 11 and 12 of the phenylalanine hydroxylase (PAH) gene was investigated in 59 children with phenylketonuria (PKU) and 100 normal children.
Yong-An Zhou +8 more
doaj +2 more sources
Mutation analysis of Phenylalanine hydroxylase gene in Iranian patients with Phenylketonuria. [PDF]
Med J Islam Repub Iran, 2018 Background: Phenylketonuria as the most common genetic metabolic disorder is the result of disruption of the phenylalanine hydroxylase gene.
Rastegar Moghadam M +4 more
europepmc +2 more sources
Simulations of the regulatory ACT domain of human phenylalanine hydroxylase (PAH) unveil its mechanism of phenylalanine binding. [PDF]
J Biol Chem, 2018 Phenylalanine hydroxylase (PAH) regulates phenylalanine (Phe) levels in mammals to prevent neurotoxicity resulting from high Phe concentrations as observed in genetic disorders leading to hyperphenylalaninemia and phenylketonuria. PAH senses elevated Phe
Ge Y +6 more
europepmc +2 more sources