Phenylalanine hydroxylase mRNA rescues the phenylketonuria phenotype in mice. [PDF]
Front Bioeng Biotechnol, 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.
Cacicedo ML +11 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
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
Phenylalanine hydroxylase contributes to serotonin synthesis in mice
The FASEB Journal, 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.
Alexander Mordhorst +10 more
semanticscholar +1 more source
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
Unique aspects of sequence variant interpretation for inborn errors of metabolism (IEM): The ClinGen IEM Working Group and the Phenylalanine Hydroxylase Gene. [PDF]
Hum Mutat, 2018 The ClinGen Inborn Errors of Metabolism Working Group was tasked with creating a comprehensive, standardized knowledge base of genes and variants for metabolic diseases.
Zastrow DB +23 more
europepmc +2 more sources
Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain. [PDF]
Sci Rep, 2016 The multi-domain enzyme phenylalanine hydroxylase (PAH) catalyzes the hydroxylation of dietary I-phenylalanine (Phe) to I-tyrosine. Inherited mutations that result in PAH enzyme deficiency are the genetic cause of the autosomal recessive disorder ...
Patel D +4 more
europepmc +2 more sources
Phenylalanine hydroxylase variants interact with the co‐chaperone DNAJC12
Human Mutation, 2019 DNAJC12, a type III member of the HSP40/DNAJ family, has been identified as the specific co‐chaperone of phenylalanine hydroxylase (PAH) and the other aromatic amino acid hydroxylases.
Kunwar Jung-Kc +9 more
semanticscholar +1 more source