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Volumn 504, Issue 1, 2012, Pages 64-74

The evolution of three types of indoleamine 2,3 dioxygenases in fungi with distinct molecular and biochemical characteristics

Author keywords

Comparative biochemistry; Enzymatic parameters; Fungi; Indoleamine 2,3 dioxygenase; Molecular evolution; Tryptophan metabolism

Indexed keywords

FUNGAL ENZYME; INDOLEAMINE 2,3 DIOXYGENASE; INDOLEAMINE 2,3 DIOXYGENASE ALPHA; INDOLEAMINE 2,3 DIOXYGENASE BETA; UNCLASSIFIED DRUG;

EID: 84862321270     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.04.082     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0014027133 scopus 로고
    • Nicotinic acid biosynthesis in prototrophs and tryptophan auxotrophs of Saccharomyces cerevisiae
    • Ahmad F., Moat A.G. Nicotinic acid biosynthesis in prototrophs and tryptophan auxotrophs of Saccharomyces cerevisiae. J. Biol. Chem. 1966, 241:775-780.
    • (1966) J. Biol. Chem. , vol.241 , pp. 775-780
    • Ahmad, F.1    Moat, A.G.2
  • 2
    • 84755160743 scopus 로고    scopus 로고
    • Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2
    • Austin C.J.D., et al. Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2. Amino Acids 2010, 39:565-1578.
    • (2010) Amino Acids , vol.39 , pp. 565-1578
    • Austin, C.J.D.1
  • 3
    • 34249295962 scopus 로고    scopus 로고
    • Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice
    • Ball H.J., et al. Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice. Gene 2007, 396:203-213.
    • (2007) Gene , vol.396 , pp. 203-213
    • Ball, H.J.1
  • 5
    • 37849002571 scopus 로고    scopus 로고
    • Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase
    • Batabyal D., Yeh S. Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase. J. Am. Chem. Soc. 2007, 129:15690-15701.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15690-15701
    • Batabyal, D.1    Yeh, S.2
  • 6
    • 20044385748 scopus 로고    scopus 로고
    • A crucial role for tryptophan catabolism at the host/Candida albicans interface
    • Bozza S., et al. A crucial role for tryptophan catabolism at the host/Candida albicans interface. J. Immunol. 2005, 174:2910-2918.
    • (2005) J. Immunol. , vol.174 , pp. 2910-2918
    • Bozza, S.1
  • 7
    • 0014736869 scopus 로고
    • Regulation of enzymes involved in the conversion of tryptophan to nicotinamide adenine dinucleotide in a colorless strain of Xanthomonas pruni
    • Brown A.T., Wagner C. Regulation of enzymes involved in the conversion of tryptophan to nicotinamide adenine dinucleotide in a colorless strain of Xanthomonas pruni. J. Bacteriol. 1970, 101:456-463.
    • (1970) J. Bacteriol. , vol.101 , pp. 456-463
    • Brown, A.T.1    Wagner, C.2
  • 8
    • 67849124704 scopus 로고    scopus 로고
    • Reassessment of the reaction mechanism in the heme dioxygenases
    • Chauhan N., et al. Reassessment of the reaction mechanism in the heme dioxygenases. J. Am. Chem. Soc. 2009, 131:4186-4187.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4186-4187
    • Chauhan, N.1
  • 9
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 10
    • 34247591012 scopus 로고    scopus 로고
    • Two distinct pathways supply anthranilate as a precursor of the Pseudomonas quinolone signal
    • Farrow J.M., Pesci E.C. Two distinct pathways supply anthranilate as a precursor of the Pseudomonas quinolone signal. J. Bacteriol. 2007, 189:3425-3433.
    • (2007) J. Bacteriol. , vol.189 , pp. 3425-3433
    • Farrow, J.M.1    Pesci, E.C.2
  • 11
    • 77953775808 scopus 로고    scopus 로고
    • Control of immune response by amino acid metabolism
    • Grohmann U., Bronte V. Control of immune response by amino acid metabolism. Immunol. Rev. 2010, 236:243-264.
    • (2010) Immunol. Rev. , vol.236 , pp. 243-264
    • Grohmann, U.1    Bronte, V.2
  • 12
    • 2542497814 scopus 로고    scopus 로고
    • Analysis of a nonribosomal peptide synthetase gene from Alternaria brassicae and flanking genomic sequences
    • Guillemette T., Sellam A., Simoneau P. Analysis of a nonribosomal peptide synthetase gene from Alternaria brassicae and flanking genomic sequences. Curr. Genet. 2004, 45:214-224.
    • (2004) Curr. Genet. , vol.45 , pp. 214-224
    • Guillemette, T.1    Sellam, A.2    Simoneau, P.3
  • 14
    • 0036375569 scopus 로고    scopus 로고
    • Intracellular pH homeostasis in the filamentous fungus Aspergillus niger
    • Hesse S.J., Ruijter G.J., Dijkema C., Visser J. Intracellular pH homeostasis in the filamentous fungus Aspergillus niger. Eur. J. Biochem. 2002, 269:3485-3494.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3485-3494
    • Hesse, S.J.1    Ruijter, G.J.2    Dijkema, C.3    Visser, J.4
  • 15
    • 33846689594 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase in dendritic cells by stereoisomers of 1-methyl-tryptophan correlates with antitumor responses
    • Hou D.Y., et al. Inhibition of indoleamine 2,3-dioxygenase in dendritic cells by stereoisomers of 1-methyl-tryptophan correlates with antitumor responses. Cancer Res. 2007, 67:792-801.
    • (2007) Cancer Res. , vol.67 , pp. 792-801
    • Hou, D.Y.1
  • 16
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Taylor W.R., Thornton J.M. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 1992, 8:275-282.
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 17
    • 65349192177 scopus 로고    scopus 로고
    • Tryptophan 2,3-dioxygenase is a key modulator of physiological neurogenesis and anxiety-related behavior in mice
    • Kanai M., et al. Tryptophan 2,3-dioxygenase is a key modulator of physiological neurogenesis and anxiety-related behavior in mice. Mol. Brain 2009, 2:8.
    • (2009) Mol. Brain , vol.2 , pp. 8
    • Kanai, M.1
  • 18
    • 33745748315 scopus 로고    scopus 로고
    • Pigment pattern formation in the quail mutant of the silkworm, Bombyx mori: parallel increase of pteridine biosynthesis and pigmentation of melanin and ommochromes
    • Kato T., Sawada H., Yamamoto T., Mase K., Nakagoshi M. Pigment pattern formation in the quail mutant of the silkworm, Bombyx mori: parallel increase of pteridine biosynthesis and pigmentation of melanin and ommochromes. Pigment Cell Res. 2006, 19:337-345.
    • (2006) Pigment Cell Res. , vol.19 , pp. 337-345
    • Kato, T.1    Sawada, H.2    Yamamoto, T.3    Mase, K.4    Nakagoshi, M.5
  • 19
    • 34447301305 scopus 로고    scopus 로고
    • Why do some yeast species require niacin for growth? Different modes of NAD synthesis
    • Li Y.F., Bao W.G. Why do some yeast species require niacin for growth? Different modes of NAD synthesis. FEMS Yeast Res. 2007, 7:657-664.
    • (2007) FEMS Yeast Res. , vol.7 , pp. 657-664
    • Li, Y.F.1    Bao, W.G.2
  • 20
    • 58449097916 scopus 로고    scopus 로고
    • NAD biosynthesis evolution in bacteria: lateral gene transfer of kynurenine pathway in Xanthomonadales and Flavobacteriales
    • Lima W.C., Varani A.M., Menck C.F. NAD biosynthesis evolution in bacteria: lateral gene transfer of kynurenine pathway in Xanthomonadales and Flavobacteriales. Mol. Biol. Evol. 2009, 26:399-406.
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 399-406
    • Lima, W.C.1    Varani, A.M.2    Menck, C.F.3
  • 21
    • 67649432744 scopus 로고    scopus 로고
    • Inhibitors of indoleamine-2,3-dioxygenase for cancer therapy: can we see the wood for the trees?
    • Löb S., Königsrainer A., Rammensee H.G., Opelz G., Terness P. Inhibitors of indoleamine-2,3-dioxygenase for cancer therapy: can we see the wood for the trees?. Nat. Rev. Cancer 2009, 9:445-452.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 445-452
    • Löb, S.1    Königsrainer, A.2    Rammensee, H.G.3    Opelz, G.4    Terness, P.5
  • 22
    • 54849418903 scopus 로고    scopus 로고
    • IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism
    • Löb S., et al. IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism. Cancer Immunol. Immunother. 2009, 58:153-157.
    • (2009) Cancer Immunol. Immunother. , vol.58 , pp. 153-157
    • Löb, S.1
  • 23
    • 52449108671 scopus 로고    scopus 로고
    • Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis
    • Marinoni I., et al. Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis. FEBS J. 2008, 275:5090-5107.
    • (2008) FEBS J. , vol.275 , pp. 5090-5107
    • Marinoni, I.1
  • 24
    • 34547643025 scopus 로고    scopus 로고
    • Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan
    • Metz R., Duhadaway J.B., Kamasani U., Laury-Kleintop L., Muller A.J., Prendergast G.C. Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res. 2007, 67:7082-7087.
    • (2007) Cancer Res. , vol.67 , pp. 7082-7087
    • Metz, R.1    Duhadaway, J.B.2    Kamasani, U.3    Laury-Kleintop, L.4    Muller, A.J.5    Prendergast, G.C.6
  • 25
    • 0037165629 scopus 로고    scopus 로고
    • + metabolism in Saccharomyces cerevisiae
    • + metabolism in Saccharomyces cerevisiae. FEBS Lett. 2002, 517:97-102.
    • (2002) FEBS Lett. , vol.517 , pp. 97-102
    • Panozzo, C.1
  • 26
    • 27444436075 scopus 로고    scopus 로고
    • 303Ala variant: implications for catalysis
    • 303Ala variant: implications for catalysis. Biochemistry 2005, 44:14318-14328.
    • (2005) Biochemistry , vol.44 , pp. 14318-14328
    • Papadopoulou, N.D.1
  • 27
    • 77952321456 scopus 로고    scopus 로고
    • Cryptic color change in a crab spider (Misumena vatia): identification and quantification of precursors and ommochrome pigments by HPLC
    • Riou M., Christidès J.P. Cryptic color change in a crab spider (Misumena vatia): identification and quantification of precursors and ommochrome pigments by HPLC. J. Chem. Ecol. 2010, 36:412-423.
    • (2010) J. Chem. Ecol. , vol.36 , pp. 412-423
    • Riou, M.1    Christidès, J.P.2
  • 29
    • 0041386108 scopus 로고    scopus 로고
    • MRBAYES 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F., Huelsenbeck J.P. MRBAYES 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 2003, 19:1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 30
    • 67749119915 scopus 로고    scopus 로고
    • The Ascomycota tree of life: a phylum-wide phylogeny clarifies the origin and evolution of fundamental reproductive and ecological traits
    • Schoch C.L., et al. The Ascomycota tree of life: a phylum-wide phylogeny clarifies the origin and evolution of fundamental reproductive and ecological traits. Syst. Biol. 2009, 58:224-239.
    • (2009) Syst. Biol. , vol.58 , pp. 224-239
    • Schoch, C.L.1
  • 31
    • 0022458358 scopus 로고
    • Molecular characterization of the Drosophila vermilion locus and its suppressible alleles
    • Searles L.L., Voelker R.A. Molecular characterization of the Drosophila vermilion locus and its suppressible alleles. Proc. Natl. Acad. Sci. U. S. A. 1986, 83:404-408.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 404-408
    • Searles, L.L.1    Voelker, R.A.2
  • 33
    • 27544499713 scopus 로고    scopus 로고
    • Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated l-tryptophan metabolism
    • Takikawa O. Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated l-tryptophan metabolism. Biochem. Biophys. Res. Commun. 2005, 338:12-29.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 12-29
    • Takikawa, O.1
  • 34
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 35
    • 0017814311 scopus 로고
    • Stereochemistry and mechanism of reactions catalyzed by tryptophanase Escherichia coli
    • Vederas J.C., Schleicher E., Tsai M.D., Floss H.G. Stereochemistry and mechanism of reactions catalyzed by tryptophanase Escherichia coli. J. Biol. Chem. 1978, 253:5350-5354.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5350-5354
    • Vederas, J.C.1    Schleicher, E.2    Tsai, M.D.3    Floss, H.G.4
  • 36
    • 69949152972 scopus 로고    scopus 로고
    • A fungal phylogeny based on 82 complete genomes using the composition vector method
    • Wang H., Xu Z., Gao L., Hao B. A fungal phylogeny based on 82 complete genomes using the composition vector method. BMC Evol. Biol. 2009, 9:195.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 195
    • Wang, H.1    Xu, Z.2    Gao, L.3    Hao, B.4
  • 37
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., Goldman N. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 2001, 18:691-699.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 38
    • 3042820410 scopus 로고    scopus 로고
    • A simple, rapid, high-fidelity and cost-effective PCR-based two-step DNA synthesis method for long gene sequences
    • Xiong A.S., et al. A simple, rapid, high-fidelity and cost-effective PCR-based two-step DNA synthesis method for long gene sequences. Nucleic Acids Res. 2004, 32:e98.
    • (2004) Nucleic Acids Res. , vol.32
    • Xiong, A.S.1
  • 39
    • 0014217450 scopus 로고
    • Tryptophan pyrrolase of rabbit intestine. d- and l-tryptophan-cleaving enzyme or enzymes
    • Yamamoto S., Hayaishi O. Tryptophan pyrrolase of rabbit intestine. d- and l-tryptophan-cleaving enzyme or enzymes. J. Biol. Chem. 1967, 242:2560-2566.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2560-2566
    • Yamamoto, S.1    Hayaishi, O.2
  • 40
    • 79953328952 scopus 로고    scopus 로고
    • Molecular evolution and characterization of fungal indoleamine 2, 3-dioxygenases
    • Yuasa H.J., Ball H.J. Molecular evolution and characterization of fungal indoleamine 2, 3-dioxygenases. J. Mol. Evol. 2011, 72:160-168.
    • (2011) J. Mol. Evol. , vol.72 , pp. 160-168
    • Yuasa, H.J.1    Ball, H.J.2
  • 42
    • 64849100126 scopus 로고    scopus 로고
    • Characterization and evolution of vertebrate indoleamine 2, 3-dioxygenases: IDOs from monotremes and marsupials
    • Yuasa H.J., et al. Characterization and evolution of vertebrate indoleamine 2, 3-dioxygenases: IDOs from monotremes and marsupials. Comp. Biochem. Physiol. B 2009, 153:137-144.
    • (2009) Comp. Biochem. Physiol. B , vol.153 , pp. 137-144
    • Yuasa, H.J.1
  • 43
    • 77954143054 scopus 로고    scopus 로고
    • 1-L-methyltryptophan is a more effective inhibitor of vertebrate IDO2 enzymes than 1-D-methyltryptophan
    • Yuasa H.J., Ball H.J., Austin C.J.D., Hunt N.H. 1-L-methyltryptophan is a more effective inhibitor of vertebrate IDO2 enzymes than 1-D-methyltryptophan. Comp. Biochem. Physiol. B 2010, 157:10-15.
    • (2010) Comp. Biochem. Physiol. B , vol.157 , pp. 10-15
    • Yuasa, H.J.1    Ball, H.J.2    Austin, C.J.D.3    Hunt, N.H.4
  • 44
    • 80051475442 scopus 로고    scopus 로고
    • Molecular evolution of bacterial indoleamine 2,3-dioxygenase
    • Yuasa H.J., Ushigoe A., Ball H.J. Molecular evolution of bacterial indoleamine 2,3-dioxygenase. Gene 2011, 485:22-31.
    • (2011) Gene , vol.485 , pp. 22-31
    • Yuasa, H.J.1    Ushigoe, A.2    Ball, H.J.3


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