Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria
about
Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylaseDynamic dissociating homo-oligomers and the control of protein functionRegulation of phenylalanine hydroxylase: conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometryProtein design: toward functional metalloenzymesAn additional substrate binding site in a bacterial phenylalanine hydroxylaseThe Solution Structure of the Regulatory Domain of Tyrosine HydroxylaseMissense mutations in the N-terminal domain of human phenylalanine hydroxylase interfere with binding of regulatory phenylalanineFolding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.Protein stability and in vivo concentration of missense mutations in phenylalanine hydroxylase.The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation. Effect of L-Phe and comparison with the rat enzyme.Deamidations in recombinant human phenylalanine hydroxylase. Identification of labile asparagine residues and functional characterization of Asn --> Asp mutant forms.Essential role of the N-terminal autoregulatory sequence in the regulation of phenylalanine hydroxylase.A comparison of kinetic and regulatory properties of the tetrameric and dimeric forms of wild-type and Thr427-->Pro mutant human phenylalanine hydroxylase: contribution of the flexible hinge region Asp425-Gln429 to the tetramerization and cooperativPhenylketonuria: old disease, new approach to treatment.Purification, crystallization and crystallographic analysis of Dictyostelium discoideum phenylalanine hydroxylase in complex with dihydrobiopterin and FeIII.A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis.Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulationStructures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine.Phenylalanine hydroxylase misfolding and pharmacological chaperones.First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramerLoss of function in phenylketonuria is caused by impaired molecular motions and conformational instabilityRole of the phenylalanine-hydroxylating system in aromatic substance degradation and lipid metabolism in the oleaginous fungus Mortierella alpinaDomain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations.Allosteric regulation of phenylalanine hydroxylase.Phenylalanine hydroxylase: function, structure, and regulation.Tetrahydrobiopterin, its mode of action on phenylalanine hydroxylase, and importance of genotypes for pharmacological therapy of phenylketonuria.Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme.C-terminal domains implicated in the functional surface expression of potassium channels.Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Phenylketonuria: genotype-phenotype correlations based on expression analysis of structural and functional mutations in PAH.Computational study of missense mutations in phenylalanine hydroxylase.Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases.Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation.Identification of phenylalanine 3-hydroxylase for meta-tyrosine biosynthesis.The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase.Assessing the relative importance of the biophysical properties of amino acid substitutions associated with human genetic disease.Phosphorylation and mutations of Ser(16) in human phenylalanine hydroxylase. Kinetic and structural effects.Modeled ligand-protein complexes elucidate the origin of substrate specificity and provide insight into catalytic mechanisms of phenylalanine hydroxylase and tyrosine hydroxylase.Probing the role of crystallographically defined/predicted hinge-bending regions in the substrate-induced global conformational transition and catalytic activation of human phenylalanine hydroxylase by single-site mutagenesis.
P2860
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P2860
Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Structure of tetrameric human ...... plications for phenylketonuria
@ast
Structure of tetrameric human ...... plications for phenylketonuria
@en
Structure of tetrameric human ...... plications for phenylketonuria
@nl
type
label
Structure of tetrameric human ...... plications for phenylketonuria
@ast
Structure of tetrameric human ...... plications for phenylketonuria
@en
Structure of tetrameric human ...... plications for phenylketonuria
@nl
prefLabel
Structure of tetrameric human ...... plications for phenylketonuria
@ast
Structure of tetrameric human ...... plications for phenylketonuria
@en
Structure of tetrameric human ...... plications for phenylketonuria
@nl
P2093
P2860
P3181
P356
P1476
Structure of tetrameric human ...... plications for phenylketonuria
@en
P2093
H Erlandsen
R C Stevens
T Flatmark
P2860
P304
P3181
P356
10.1074/JBC.273.27.16962
P407
P577
1998-07-03T00:00:00Z