Regulation of phenylalanine hydroxylase: Conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry

Jun Li, Paul F. Fitzpatrick

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The enzyme phenylalanine hydroxylase catalyzes the hydroxylation of excess phenylalanine in the liver to tyrosine. The enzyme is regulated allosterically by phenylalanine and by phosphorylation of Ser16. Hydrogen/deuterium exchange monitored by mass spectrometry has been used to gain insight into any structural change upon phosphorylation. Peptides in both the catalytic and regulatory domains show increased deuterium incorporation into the phosphorylated protein. Deuterium is incorporated into fewer peptides than when the enzyme is activated by phenylalanine, and the incorporation is slower. This establishes that the conformational change upon phosphorylation of phenylalanine hydroxylase is different from and less extensive than that upon phenylalanine activation.

Original languageEnglish (US)
Pages (from-to)115-119
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume535
Issue number2
DOIs
StatePublished - May 9 2013

Keywords

  • Allostery
  • Hydrogen-deuterium exchange
  • Phenylalanine hydroxylase
  • Phosphorylation
  • Regulation
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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