Cloning and functional expression of human kynurenine 3-monooxygenase

被引：42

作者：

AlberatiGiani, D ^{[1
]}

Cesura, AM ^{[1
]}

Broger, C ^{[1
]}

Warren, WD ^{[1
]}

Rover, S ^{[1
]}

Malherbe, P ^{[1
]}

机构：

[1] PETER MACCALLUM CANC INST,MELBOURNE,VIC 3002,AUSTRALIA

来源：

FEBS LETTERS | 1997年 / 410卷 / 2-3期

关键词：

kynurenine; 3-monooxygenase; flavin monooxygenase; sequence comparison; kynurenine pathway; Drosophila melanogaster; human liver;

D O I：

10.1016/S0014-5793(97)00627-3

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：

Kynurenine 3-monooxygenase, an NADPH-dependent flavin monooxygenase, catalyses the hydroxylation of L- kynurenine to L-3-hydroxykynurenine. By hybridization screening using a cDNA probe encoding the entire exon 2 of Drosophila melanogaster kynurenine 3-monooxygenase, we isolated a 2.0 kb cDNA clone coding for the corresponding human liver enzyme. The deduced amino acid sequence of the human protein consists of 486 amino acids with a predicted molecular mass of 55 762 Da, Transfection of the human cDNA in HEK-293 cells resulted in the functional expression of the enzyme,vith kinetic properties similar to those found for the native human protein, RNA blot analysis of human tissues revealed the presence of a major mRNA species of similar to 2.0 kb in liver, placenta and kidney. (C) 1997 Federation of European Biochemical Societies.

引用

页码：407 / 412

页数：6

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