Structural insights into the regulation of aromatic amino acid hydroxylation

Paul F. Fitzpatrick

Research output: Contribution to journalReview articlepeer-review

18 Scopus citations


The aromatic amino acid hydroxylases phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase are homotetramers, with each subunit containing a homologous catalytic domain and a divergent regulatory domain. The solution structure of the regulatory domain of tyrosine hydroxylase establishes that it contains a core ACT domain similar to that in phenylalanine hydroxylase. The isolated regulatory domain of tyrosine hydroxylase forms a stable dimer, while that of phenylalanine hydroxylase undergoes a monomer-dimer equilibrium, with phenylalanine stabilizing the dimer. These solution properties are consistent with the regulatory mechanisms of the two enzymes, in that phenylalanine hydroxylase is activated by phenylalanine binding to an allosteric site, while tyrosine hydroxylase is regulated by binding of catecholamines in the active site.

Original languageEnglish (US)
Pages (from-to)1-6
Number of pages6
JournalCurrent Opinion in Structural Biology
StatePublished - Dec 1 2015

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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