Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation
about
Tyrosine hydroxylase and regulation of dopamine synthesisActivation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactorEvidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylaseRegulation of phenylalanine hydroxylase: conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometryMechanism of aromatic amino acid hydroxylationInsights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylationMechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic AnalysisAn additional substrate binding site in a bacterial phenylalanine hydroxylaseSpectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activationAn inquiry into protein structure and genetic disease: introducing undergraduates to bioinformatics in a large introductory courseFormation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases.A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis.Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulationFunctional domains of human tryptophan hydroxylase 2 (hTPH2).Phenylketonuria: an inborn error of phenylalanine metabolism.Non-heme iron enzymes: contrasts to heme catalysisProton-coupled electron transfer of ruthenium(III)-pterin complexes: a mechanistic insightCatalytic residues and a predicted structure of tetrahydrobiopterin-dependent alkylglycerol mono-oxygenase.Role 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.Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation.Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine hydroxylaseSingle turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases.Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps.Mutagenesis of a specificity-determining residue in tyrosine hydroxylase establishes that the enzyme is a robust phenylalanine hydroxylase but a fragile tyrosine hydroxylasePredicted 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.Functional studies of tyrosine hydroxylase missense variants reveal distinct patterns of molecular defects in Dopa-responsive dystonia.A flexible loop in tyrosine hydroxylase controls coupling of amino acid hydroxylation to tetrahydropterin oxidation.Identification of phenylalanine 3-hydroxylase for meta-tyrosine biosynthesis.Modeled ligand-protein complexes elucidate the origin of substrate specificity and provide insight into catalytic mechanisms of phenylalanine hydroxylase and tyrosine hydroxylase.Probing cofactor specificity in phenylalanine hydroxylase by molecular dynamics simulations.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.Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations.Endogenous tetrahydroisoquinolines associated with Parkinson's disease mimic the feedback inhibition of tyrosine hydroxylase by catecholamines.Melanoma cases demonstrate increased carrier frequency of phenylketonuria/hyperphenylalanemia mutations.
P2860
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P2860
Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Crystal structure of the terna ...... lysis and substrate activation
@ast
Crystal structure of the terna ...... lysis and substrate activation
@en
Crystal structure of the terna ...... lysis and substrate activation
@nl
type
label
Crystal structure of the terna ...... lysis and substrate activation
@ast
Crystal structure of the terna ...... lysis and substrate activation
@en
Crystal structure of the terna ...... lysis and substrate activation
@nl
prefLabel
Crystal structure of the terna ...... lysis and substrate activation
@ast
Crystal structure of the terna ...... lysis and substrate activation
@en
Crystal structure of the terna ...... lysis and substrate activation
@nl
P1476
Crystal structure of the terna ...... lysis and substrate activation
@en
P2093
Edward Hough
Torgeir Flatmark
P304
P356
10.1016/S0022-2836(02)00560-0
P407
P577
2002-07-26T00:00:00Z