Role of tryptophan hydroxylase Phe313 in determining substrate specificity

S. Colette Daubner, Graham R. Moran, Paul F. Fitzpatrick

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


The active site residue phenylalanine 313 is conserved in the sequences of all known tryptophan hydroxylases. The tryptophan hydroxylase F313W mutant protein no longer shows a preference for tryptophan over phenylalanine as a substrate, consistent with a role of this residue in substrate specificity. A tryptophan residue occupies the homologous position in tyrosine hydroxylase. The tyrosine hydroxylase W372F mutant enzyme does not show an increased preference for tryptophan over tyrosine or phenylalanine, so that this residue cannot be considered the dominant factor in substrate specificity in this family of enzymes.

Original languageEnglish (US)
Article number96719
Pages (from-to)639-641
Number of pages3
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 2002


  • Active site
  • Kinetics
  • Mutagenesis
  • Substrate specificity
  • Tryptophan hydroxylase
  • Tyrosine hydroxylase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Role of tryptophan hydroxylase Phe313 in determining substrate specificity'. Together they form a unique fingerprint.

Cite this