Spectroscopic and kinetic properties of unphosphorylated rat hepatic phenylalanine hydroxylase expressed in Escherichia coli. Comparison of resting and activated states.

Spectroscopic and kinetic properties of unphosphorylated rat hepatic phenylalanine hydroxylase expressed in Escherichia coli. Comparison of resting and activated states.

Item
http://www.wikidata.org/entity/Q54598160
Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactorStructure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuriaEssential role of the N-terminal autoregulatory sequence in the regulation of phenylalanine hydroxylase.Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme.Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active siteThe role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis.The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers.Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.Allosteric regulation of phenylalanine hydroxylase.Tetrahydrobiopterin, its mode of action on phenylalanine hydroxylase, and importance of genotypes for pharmacological therapy of phenylketonuria.Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation.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.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

Spectroscopic and kinetic properties of unphosphorylated rat hepatic phenylalanine hydroxylase expressed in Escherichia coli. Comparison of resting and activated states.

Item
http://www.wikidata.org/entity/Q54598160
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Spectroscopic and kinetic prop ...... resting and activated states.
@en
Spectroscopic and kinetic prop ...... resting and activated states.
@nl
type
label
Spectroscopic and kinetic prop ...... resting and activated states.
@en
Spectroscopic and kinetic prop ...... resting and activated states.
@nl
prefLabel
Spectroscopic and kinetic prop ...... resting and activated states.
@en
Spectroscopic and kinetic prop ...... resting and activated states.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P356
P1433
P1476
Spectroscopic and kinetic prop ...... resting and activated states.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698