caa a22 4500 445821434 CHVBK 20180317145245.0 cr unu---uuuuu 170323e20110201xx s 000 0 eng 10.1007/s00239-010-9412-5 doi (NATIONALLICENCE)springer-10.1007/s00239-010-9412-5 Molecular Evolution and Characterization of Fungal Indoleamine 2,3-Dioxygenases [Elektronische Daten] [Hajime Yuasa, Helen Ball] Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes. Mammalian IDO expression is induced by cytokines and has antimicrobial and immunomodulatory effects. A major role of mammalian TDO is to supply nicotinamide adenine dinucleotide (NAD+). In fungi, the IDO homologue is thought to be expressed constitutively and supply NAD+, as TDO is absent from their genomes. Here, we reveal the distribution of IDO genes among fungal species and characterize their enzymatic activity. The yeast, Saccharomyces cerevisiae has only one IDO gene, whereas the koji-mold, Aspergillus oryzae has two genes, IDOα and IDOβ. The A. oryzae IDOα showed more similar enzymatic properties to those of S. cerevisiae IDO than IDOβ, suggesting that the A. oryzae IDOα is a functional homologue of the S. cerevisiae IDO. From the IDOβ gene, two isoforms, IDOβ and IDOβ+ could be generated by alternative splicing. The latter contained a 17 amino acids insertion which were encoded by the first intron of IDOβ gene. In comparison to IDOβ+, bacterially expressed IDOβ showed much lower K m value and more than five-times faster V max value, resulting in 85 times higher catalytic efficiency; i.e., the removal of the domain encoded by the first intron from IDOβ+ increases its enzymatic activity drastically. This might be a unique regulation mechanism of the l-Trp metabolism in the A. oryzae. The levo-1-methyl tryptophan (l-1MT) is a good inhibitor of both IDO1 and IDO2. However, the activity of fungal IDOs tested was not inhibited at all by l-1MT. Springer Science+Business Media, LLC, 2010 Comparative biochemistry nationallicence Enzymatic parameters nationallicence Fungi nationallicence Indoleamine 2,3-dioxygenase nationallicence Molecular evolution nationallicence Tryptophan metabolism nationallicence IDO1 : Indoleamine 2,3-dioxygenase 1 nationallicence IDO2 : Indoleamine 2,3-dioxygenase 2 nationallicence Kyn : Kynurenine nationallicence 1-MT : 1-Methyl-tryptophan nationallicence ORF : Open reading frame nationallicence TDO : Tryptophan 2,3-dioxygenase nationallicence TON : Turnover number nationallicence Yuasa Hajime Laboratory of Biochemistry, Department of Applied Science, Faculty of Science, National University Corporation Kochi University, 780-8520, Kochi, Japan aut Ball Helen Molecular Immunopathology Unit, Discipline of Pathology, School of Medical Sciences, and Bosch Institute, University of Sydney, 2006, Sydney, NSW, Australia aut Journal of Molecular Evolution Springer-Verlag 72/2(2011-02-01), 160-168 0022-2844 72:2<160 2011 72 239 https://doi.org/10.1007/s00239-010-9412-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00239-010-9412-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yuasa Hajime Laboratory of Biochemistry, Department of Applied Science, Faculty of Science, National University Corporation Kochi University, 780-8520, Kochi, Japan aut NATIONALLICENCE 700 1- Ball Helen Molecular Immunopathology Unit, Discipline of Pathology, School of Medical Sciences, and Bosch Institute, University of Sydney, 2006, Sydney, NSW, Australia aut NATIONALLICENCE 773 0- Journal of Molecular Evolution Springer-Verlag 72/2(2011-02-01), 160-168 0022-2844 72:2<160 2011 72 239 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer