ArticleBiochemistry2014
Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Synthetic closed-loop gene circuit for phenylalanine regulation.Nucleic acids research · 2025Article
- Blood phenylalanine reduction reverses gene expression changes observed in a mouse model of phenylketonuria.Scientific reports · 2021Article
- Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability.Scientific reports · 2019Article
- The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability.The Journal of biological chemistry · 2019Article
- The quaternary structure of human tyrosine hydroxylase: effects of dystonia-associated missense variants on oligomeric state and enzyme activity.Journal of neurochemistry · 2019Article
- Simulations of the regulatory ACT domain of human phenylalanine hydroxylase (PAH) unveil its mechanism of phenylalanine binding.The Journal of biological chemistry · 2018Article
- Phosphorylation of Phenylalanine Hydroxylase Increases the Rate Constant for Formation of the Activated Conformation of the Enzyme.Biochemistry · 2018Article
- Substituting TyrFEBS open bio · 2017Article
- X-ray Scattering Studies of Protein Structural Dynamics.Chemical reviews · 2017Review
- PKU mutation p.G46S prevents the stereospecific binding of l-phenylalanine to the dimer of human phenylalanine hydroxylase regulatory domain.FEBS open bio · 2017Article
- Stabilization of tryptophan hydroxylase 2 by l-phenylalanine-induced dimerization.FEBS open bio · 2016Article
- The structural origin of metabolic quantitative diversity.Scientific reports · 2016Article
- The regulatory domain of human tryptophan hydroxylase 1 forms a stable dimer.Biochemical and biophysical research communications · 2016Article
- From structural biology to designing therapy for inborn errors of metabolism.Journal of inherited metabolic disease · 2016Review
- Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.Journal of the American Chemical Society · 2016Article
- Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Scientific reports · 2016Article
- Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase.The Journal of biological chemistry · 2016Article
- First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural insights into the regulation of aromatic amino acid hydroxylation.Current opinion in structural biology · 2015Review
- The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers.Biochemistry · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Analytical ultracentrifugation has been used to analyze the oligomeric structure of the isolated regulatory domain of phenylalanine hydroxylase. The protein exhibits a monomer-dimer equilibrium with a dissociation constant of ~46 μM; this value is unaffected by the removal of the 24 N-terminal residues or by phosphorylation of Ser16. In contrast, phenylalanine binding (Kd = 8 μM) stabilizes the dimer. These results suggest that dimerization of the regulatory domain of phenylalanine hydroxylase is linked to allosteric activation of the enzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.