descriptionPublicationkeyboard_double_arrow_right Article , Other literature type 13 Oct 2014 English Publisher:American Chemical Society (ACS)Journal:Biochemistry, volume 53, pages 6,625-6,627 (issn: 0006-2960, eissn: 1520-4995,

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

doi: 10.1021/bi501109s

pmid: 25299136

pmc: PMC4251497

Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase

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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.

Related Organizations

The University of Texas Health Science Center at San Antonio
United States

Keywords

Phenylalanine, Serine, Phenylalanine Hydroxylase, Phosphorylation, Dimerization, Protein Binding, Protein Structure, Tertiary

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