title: Deduced primary structure of rat tryptophan-2,3-dioxygenase.
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.
authors.affiliation: Department of Biology, Faculty of Science, Kyushu University, Fukuoka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Maezono
authors.forename: K
authors.initials: K
authors.lastname: Tashiro
authors.forename: T
authors.initials: T
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004274:DNA, Recombinant / Q000032:analysis; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D051381:Rats; D014366:Tryptophan Oxygenase / Q000032:analysis* / Q000235:genetics
chemical_list: D004274:DNA, Recombinant; D014366:Tryptophan Oxygenase