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

Katsumi Maezono; Kosuke Tashiro; Toshikazu Nakamura

doi:10.1016/0006-291X(90)91256-R

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

Katsumi Maezono, Kosuke Tashiro, Toshikazu Nakamura

Systems Biology

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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 language	English
Pages (from-to)	176-181
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	170
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(90)91256-R
Publication status	Published - Jul 16 1990

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Maezono, Katsumi

AU - Tashiro, Kosuke

AU - Nakamura, Toshikazu

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Y1 - 1990/7/16

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AB - 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.

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

Abstract

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