DEDUCED PRIMARY STRUCTURE OF RAT TRYPTOPHAN-2,3-DIOXYGENASE

被引：28

作者：

MAEZONO, K ^{[1
]}

TASHIRO, K ^{[1
]}

NAKAMURA, T ^{[1
]}

机构：

[1] KYUSHU UNIV,FAC SCI,DEPT BIOL,FUKUOKA 812,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 170卷 / 01期

关键词：

D O I：

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

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1990.

引用

页码：176 / 181

页数：6

共 24 条

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