The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanism.
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Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactorInsights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylationStructure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stabilityEssential 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 cooperativFormation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases.Phenylalanine hydroxylase misfolding and pharmacological chaperones.Phenylalanine 4-monooxygenase and the role of endobiotic metabolism enzymes in xenobiotic biotransformation.Structural characterization of the N-terminal autoregulatory sequence of phenylalanine hydroxylase.Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine 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.A flexible loop in tyrosine hydroxylase controls coupling of amino acid hydroxylation to tetrahydropterin oxidation.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.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 cofactor specificity in phenylalanine hydroxylase by molecular dynamics simulations.Mechanisms underlying responsiveness to tetrahydrobiopterin in mild phenylketonuria mutations.
P2860
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P2860
The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanism.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The structural basis of the re ...... s for the catalytic mechanism.
@ast
The structural basis of the re ...... s for the catalytic mechanism.
@en
type
label
The structural basis of the re ...... s for the catalytic mechanism.
@ast
The structural basis of the re ...... s for the catalytic mechanism.
@en
prefLabel
The structural basis of the re ...... s for the catalytic mechanism.
@ast
The structural basis of the re ...... s for the catalytic mechanism.
@en
P2093
P356
P1476
The structural basis of the re ...... s for the catalytic mechanism.
@en
P2093
Frøystein NA
Martínez A
P304
P356
10.1006/JMBI.1999.3288
P407
P577
1999-12-01T00:00:00Z