Allosteric regulation of phenylalanine hydroxylase

Paul F. Fitzpatrick

Research output: Contribution to journalReview article

49 Scopus citations

Abstract

The liver enzyme phenylalanine hydroxylase is responsible for conversion of excess phenylalanine in the diet to tyrosine. Phenylalanine hydroxylase is activated by phenylalanine; this activation is inhibited by the physiological reducing substrate tetrahydrobiopterin. Phosphorylation of Ser16 lowers the concentration of phenylalanine for activation. This review discusses the present understanding of the molecular details of the allosteric regulation of the enzyme.

Original languageEnglish (US)
Pages (from-to)194-201
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume519
Issue number2
DOIs
StatePublished - Mar 15 2012

Keywords

  • Allostery
  • Phenylalanine hydroxylase
  • Phosphorylation
  • Regulation
  • Tetrahydrobiopterin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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