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Cloning and functional expression of human kynurenine 3‐monooxygenase
Author(s) -
Alberati-Giani Daniela,
Cesura Andrea M,
Broger Clemens,
Warren William D,
Röver Stephan,
Malherbe Pari
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00627-3
Subject(s) - complementary dna , microbiology and biotechnology , kynurenine , biochemistry , biology , amino acid , monooxygenase , molecular cloning , enzyme , gene , tryptophan , cytochrome p450
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 with 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 ∼2.0 kb in liver, placenta and kidney.