Deduced primary structure of rat tryptophan-2,3-dioxygenase

Katsumi Maezono, Kosuke Tashiro, Toshikazu Nakamura

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

The complete amino acid sequence of the tryptophan 2, 3-dioxygenase (TO) of rat liver was determined from the nucleotide sequence of a full length TO cDNA isolated from a rat liver cDNA library and determined its primary structure. TO was encoded in a mRNA of about 1.7 kb containing an open reading frame of 1218 bp. According to the deduced amino acid sequence, the monomeric polypeptide of TO consisted of 406 amino acid residues with a calculated molecular weight of 47,796 daltons. It has twelve histidine residues around its hydrophobic region, which has homology with some heme proteins and oxygenase, suggesting that this hydrophobic region might to be the core of TO for the activity.

Original languageEnglish
Pages (from-to)176-181
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume170
Issue number1
DOIs
Publication statusPublished - Jul 16 1990

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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