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

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

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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.

Original languageEnglish (US)
Pages (from-to)6625-6627
Number of pages3
JournalBiochemistry
Volume53
Issue number42
DOIs
Publication statusPublished - Oct 28 2014

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ASJC Scopus subject areas

  • Biochemistry

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