Cloning and functional expression of human kynurenine 3-monooxygenase
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 c...
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| Published in | FEBS letters Vol. 410; no. 2; pp. 407 - 412 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier B.V
30.06.1997
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0014-5793 1873-3468 |
| DOI | 10.1016/S0014-5793(97)00627-3 |
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| Abstract | 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. |
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| AbstractList | 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. 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. 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 approximately 2.0 kb in liver, placenta and kidney.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 approximately 2.0 kb in liver, placenta and kidney. 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 similar to 2.0 kb in liver, placenta and kidney. 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. 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 approximately 2.0 kb in liver, placenta and kidney. |
| Author | Röver, Stephan Warren, William D Malherbe, Pari Broger, Clemens Cesura, Andrea M Alberati-Giani, Daniela |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9237672$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1046/j.1471-4159.1996.66030996.x 10.1016/0014-5793(95)00123-Q 10.1016/0306-4522(94)90227-5 10.1073/pnas.88.4.1416 10.1016/0003-2697(92)90432-7 10.1016/0022-2836(89)90158-7 10.1016/0022-2836(86)90409-2 10.1073/pnas.87.7.2506 10.1093/brain/118.3.735 10.1111/j.1432-1033.1996.0460u.x 10.1093/oxfordjournals.jbchem.a123712 10.1016/0014-5793(95)00546-L 10.1016/0006-291X(90)91666-G 10.1073/pnas.93.22.12553 10.1074/jbc.270.49.29330 10.1093/brain/116.6.1425 10.1042/bst0210083 10.1007/978-1-4613-0381-7_35 10.1006/geno.1995.9990 10.1016/S0021-9258(17)36717-0 |
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| Copyright | 1997 Federation of European Biochemical Societies FEBS Letters 410 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies |
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| Keywords | ORF hKMO Human liver dmKMO kb Kynurenine 3-monooxygenase Flavin monooxygenase Sequence comparison KMO Drosophila melanogaster bp Kynurenine pathway |
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| References | Heyes (BIB2) 1993; 21 Alberati-Giani, Ricciardi-Castagnoli, Köhler, Cesura (BIB4) 1996; 66 Carpenedo, Chiarugi, Russi, Lombardi, Carlà, Pellicciari, Mattoli, Moroni (BIB16) 1994; 61 Huynh, T.V., Young, R.A. and Davis, R.W. (1984) in: Practical Approaches in Biochemistry (Grover, D., Ed) pp. 49–77, IRL Press, Oxford. Alberati-Giani, Buchli, Malherbe, Broger, Lang, Köhler, Lahm, Cesura (BIB9) 1996; 239 Comings, Muhleman, Dietz, Sherman, Forest (BIB7) 1995; 29 Schreuder, Prick, Wierenga, Vriend, Wilson, Hol, Drenth (BIB23) 1989; 208 Perry, Harries, Schofield, Lock, King, Gibson, Goldfarb (BIB11) 1995; 360 Buchli, Alberati-Giani, Malherbe, Köhler, Broger, Cesura (BIB12) 1995; 270 Dai, Gupta (BIB8) 1990; 168 Mitoma, Ito (BIB22) 1992; 111 Okuda, Nishiyama, Saito, Katsuki (BIB5) 1996; 93 Christen, Peterhans, Stocker (BIB6) 1990; 87 Malherbe, Alberati-Giani, Köhler, Cesura (BIB13) 1995; 367 Heyes, Saito, Crowley, Major, Milstien, Markey, Vickers (BIB3) 1993; 116 Wierenga, Terpstra, Hol (BIB21) 1986; 187 Speciale, Cine, Wu, Salvati, Schwarcz, Molinari, Calabresi, Varasi (BIB17) 1996; 398 Erickson, Flanagan, Russo, Reinhard (BIB14) 1992; 205 Bligth, Cohen, Saito, Heyes (BIB15) 1995; 118 Bertocci, Miggiano, Da Prada, Dembic, Lahm, Malherbe (BIB20) 1991; 88 Warren, W.D., Palmer, S. and Howells, A.J. (1996) Genetica, in press. Stone (BIB1) 1993; 45 Malherbe, Köhler, Da Prada, Lang, Kiefer, Schwarcz, Lahm, Cesura (BIB10) 1994; 269 1989; 208 1993; 45 1990; 87 1994; 269 1986; 187 1991; 88 1992; 111 1993; 21 1996; 93 1992; 205 1995; 118 1995; 367 1995; 29 1990; 168 1993; 116 1994; 61 1995; 360 1996; 398 1996; 239 1995; 270 1996; 66 e_1_2_5_15_1 e_1_2_5_14_1 e_1_2_5_17_1 e_1_2_5_9_1 e_1_2_5_16_1 e_1_2_5_8_1 e_1_2_5_11_1 e_1_2_5_23_1 e_1_2_5_7_1 e_1_2_5_10_1 e_1_2_5_24_1 e_1_2_5_6_1 e_1_2_5_13_1 e_1_2_5_21_1 e_1_2_5_5_1 e_1_2_5_12_1 e_1_2_5_22_1 e_1_2_5_4_1 e_1_2_5_3_1 Stone T.W. (e_1_2_5_2_1) 1993; 45 e_1_2_5_19_1 e_1_2_5_18_1 e_1_2_5_20_1 |
| References_xml | – volume: 88 start-page: 1416 year: 1991 end-page: 1420 ident: BIB20 publication-title: Proc. Natl. Acad. Sci. USA – volume: 239 start-page: 460 year: 1996 end-page: 468 ident: BIB9 publication-title: Eur. J. Biochem. – volume: 269 start-page: 13792 year: 1994 end-page: 13797 ident: BIB10 publication-title: Biol. Chem. – volume: 21 start-page: 83 year: 1993 end-page: 89 ident: BIB2 publication-title: Biochem. Soc. Trans. – volume: 116 start-page: 1425 year: 1993 end-page: 1450 ident: BIB3 publication-title: Brain – volume: 66 start-page: 996 year: 1996 end-page: 1004 ident: BIB4 publication-title: J. Neurochem. – volume: 360 start-page: 277 year: 1995 end-page: 280 ident: BIB11 publication-title: FEBS Lett. – volume: 367 start-page: 141 year: 1995 end-page: 144 ident: BIB13 publication-title: FEBS Lett. – volume: 111 start-page: 20 year: 1992 end-page: 24 ident: BIB22 publication-title: J. Biochem. (Tokyo) – volume: 118 start-page: 735 year: 1995 end-page: 752 ident: BIB15 publication-title: Brain – volume: 29 start-page: 390 year: 1995 end-page: 396 ident: BIB7 publication-title: Genomics – volume: 205 start-page: 257 year: 1992 end-page: 262 ident: BIB14 publication-title: Anal. Biochem. – volume: 93 start-page: 12553 year: 1996 end-page: 12558 ident: BIB5 publication-title: Proc. Natl. Acad. Sci. USA – reference: Warren, W.D., Palmer, S. and Howells, A.J. (1996) Genetica, in press. – volume: 208 start-page: 679 year: 1989 end-page: 696 ident: BIB23 publication-title: J. Mol. Biol. – volume: 270 start-page: 29330 year: 1995 end-page: 29335 ident: BIB12 publication-title: J. Biol. Chem. – volume: 398 start-page: 221 year: 1996 end-page: 227 ident: BIB17 publication-title: Adv. Exp. Med. Biol. – volume: 87 start-page: 2506 year: 1990 end-page: 2510 ident: BIB6 publication-title: Proc. Natl. Acad. Sci. USA – volume: 168 start-page: 1 year: 1990 end-page: 8 ident: BIB8 publication-title: Biochem. Biophys. Res. Commun. – reference: Huynh, T.V., Young, R.A. and Davis, R.W. (1984) in: Practical Approaches in Biochemistry (Grover, D., Ed) pp. 49–77, IRL Press, Oxford. – volume: 61 start-page: 237 year: 1994 end-page: 244 ident: BIB16 publication-title: Neuroscience – volume: 45 start-page: 309 year: 1993 end-page: 379 ident: BIB1 publication-title: Pharmacol. Rev. – volume: 187 start-page: 101 year: 1986 end-page: 107 ident: BIB21 publication-title: J. Mol. Biol. – volume: 269 start-page: 13792 year: 1994 end-page: 13797 publication-title: Biol. Chem. – volume: 360 start-page: 277 year: 1995 end-page: 280 publication-title: FEBS Lett. – volume: 29 start-page: 390 year: 1995 end-page: 396 publication-title: Genomics – volume: 367 start-page: 141 year: 1995 end-page: 144 publication-title: FEBS Lett. – volume: 208 start-page: 679 year: 1989 end-page: 696 publication-title: J. Mol. Biol. – volume: 21 start-page: 83 year: 1993 end-page: 89 publication-title: Biochem. Soc. Trans. – volume: 111 start-page: 20 year: 1992 end-page: 24 publication-title: J. Biochem. (Tokyo) – volume: 88 start-page: 1416 year: 1991 end-page: 1420 publication-title: Proc. Natl. Acad. Sci. USA – volume: 66 start-page: 996 year: 1996 end-page: 1004 publication-title: J. Neurochem. – volume: 87 start-page: 2506 year: 1990 end-page: 2510 publication-title: Proc. Natl. Acad. Sci. USA – volume: 239 start-page: 460 year: 1996 end-page: 468 publication-title: Eur. J. Biochem. – volume: 61 start-page: 237 year: 1994 end-page: 244 publication-title: Neuroscience – volume: 187 start-page: 101 year: 1986 end-page: 107 publication-title: J. Mol. Biol. – volume: 93 start-page: 12553 year: 1996 end-page: 12558 publication-title: Proc. Natl. Acad. Sci. USA – volume: 116 start-page: 1425 year: 1993 end-page: 1450 publication-title: Brain – volume: 45 start-page: 309 year: 1993 end-page: 379 publication-title: Pharmacol. Rev. – volume: 205 start-page: 257 year: 1992 end-page: 262 publication-title: Anal. Biochem. – volume: 168 start-page: 1 year: 1990 end-page: 8 publication-title: Biochem. Biophys. Res. Commun. – volume: 270 start-page: 29330 year: 1995 end-page: 29335 publication-title: J. Biol. Chem. – volume: 118 start-page: 735 year: 1995 end-page: 752 publication-title: Brain – volume: 398 start-page: 221 year: 1996 end-page: 227 publication-title: Adv. Exp. Med. Biol. – ident: e_1_2_5_5_1 doi: 10.1046/j.1471-4159.1996.66030996.x – ident: e_1_2_5_12_1 doi: 10.1016/0014-5793(95)00123-Q – ident: e_1_2_5_20_1 – ident: e_1_2_5_17_1 doi: 10.1016/0306-4522(94)90227-5 – ident: e_1_2_5_21_1 doi: 10.1073/pnas.88.4.1416 – ident: e_1_2_5_15_1 doi: 10.1016/0003-2697(92)90432-7 – ident: e_1_2_5_24_1 doi: 10.1016/0022-2836(89)90158-7 – volume: 45 start-page: 309 year: 1993 ident: e_1_2_5_2_1 publication-title: Pharmacol. Rev. – ident: e_1_2_5_22_1 doi: 10.1016/0022-2836(86)90409-2 – ident: e_1_2_5_7_1 doi: 10.1073/pnas.87.7.2506 – ident: e_1_2_5_16_1 doi: 10.1093/brain/118.3.735 – ident: e_1_2_5_10_1 doi: 10.1111/j.1432-1033.1996.0460u.x – ident: e_1_2_5_23_1 doi: 10.1093/oxfordjournals.jbchem.a123712 – ident: e_1_2_5_14_1 doi: 10.1016/0014-5793(95)00546-L – ident: e_1_2_5_9_1 doi: 10.1016/0006-291X(90)91666-G – ident: e_1_2_5_6_1 doi: 10.1073/pnas.93.22.12553 – ident: e_1_2_5_13_1 doi: 10.1074/jbc.270.49.29330 – ident: e_1_2_5_4_1 doi: 10.1093/brain/116.6.1425 – ident: e_1_2_5_3_1 doi: 10.1042/bst0210083 – ident: e_1_2_5_19_1 – ident: e_1_2_5_18_1 doi: 10.1007/978-1-4613-0381-7_35 – ident: e_1_2_5_8_1 doi: 10.1006/geno.1995.9990 – ident: e_1_2_5_11_1 doi: 10.1016/S0021-9258(17)36717-0 |
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| Snippet | Kynurenine 3-monooxygenase, an NADPH-dependent flavin monooxygenase, catalyses the hydroxylation of
l-kynurenine to
l-3-hydroxykynurenine. By hybridization... Kynurenine 3‐monooxygenase, an NADPH‐dependent flavin monooxygenase, catalyses the hydroxylation of l‐kynurenine to l‐3‐hydroxykynurenine. By hybridization... Kynurenine 3‐monooxygenase, an NADPH‐dependent flavin monooxygenase, catalyses the hydroxylation of l ‐kynurenine to l ‐3‐hydroxykynurenine. By hybridization... Kynurenine 3-monooxygenase, an NADPH-dependent flavin monooxygenase, catalyses the hydroxylation of L-kynurenine to L-3-hydroxykynurenine. By hybridization... |
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| SubjectTerms | Amino Acid Sequence Animals base pair(s) Base Sequence Blotting, Northern Cloning, Molecular dmKMO DNA, Complementary Drosophila melanogaster Drosophila melanogaster - enzymology Drosophila melanogaster kynurenine 3-monooxygenase Flavin monooxygenase Gene Expression hKMO human kynurenine 3-monooxygenase Human liver Humans kilobases KMO Kynurenine 3-Monooxygenase Kynurenine pathway Liver - enzymology Mixed Function Oxygenases - genetics Molecular Sequence Data open reading frame ORF Recombinant Fusion Proteins - genetics Sequence Analysis Sequence comparison Sequence Homology, Amino Acid |
| Title | Cloning and functional expression of human kynurenine 3-monooxygenase |
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