Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase

Shengnan Zhang; Kenneth M. Roberts; Paul F. Fitzpatrick

doi:10.1021/bi501109s

Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase

Shengnan Zhang, Kenneth M. Roberts, Paul F. Fitzpatrick

Department of Biochemistry & Structural Biology

Resultado de la investigación: Article › revisión exhaustiva

25 Citas (Scopus)

Resumen

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 (K_d = 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.

Idioma original	English (US)
Páginas (desde-hasta)	6625-6627
Número de páginas	3
Publicación	Biochemistry
Volumen	53
N.º	42
DOI	https://doi.org/10.1021/bi501109s
Estado	Published - oct. 28 2014

ASJC Scopus subject areas

Biochemistry

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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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N2 - 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.

AB - 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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Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase

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