Tryptophan catabolizing enzymes – party of three
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway. The depletion of tryptophan and formation of kynurenine pathway metabolites modulate...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2014-10-01
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| Series: | Frontiers in Immunology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fimmu.2014.00485/full |
| _version_ | 1818143426651095040 |
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| author | Helen J Ball Felicita Fedelis Jusof Supun Madushani Bakmiwewa Nicholas H Hunt Hajime eYuasa |
| author_facet | Helen J Ball Felicita Fedelis Jusof Supun Madushani Bakmiwewa Nicholas H Hunt Hajime eYuasa |
| author_sort | Helen J Ball |
| collection | DOAJ |
| description | Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway. The depletion of tryptophan and formation of kynurenine pathway metabolites modulates the activity of the mammalian immune, reproductive and central nervous systems. IDO and TDO enzymes can have overlapping or distinct functions depending on their expression patterns. The expression of TDO and IDO enzymes in mammals differs not only by tissue/cellular localization but also by their induction by distinct stimuli. To add to the complexity, these genes also have undergone duplications in some organisms leading to multiple isoforms of IDO or TDO. For example, many vertebrates, including all mammals, have acquired two IDO genes via gene duplication, although the IDO1-like gene has been lost in some lower vertebrate lineages. Gene duplications can allow the homologs to diverge and acquire different properties to the original gene. There is evidence for IDO enzymes having differing enzymatic characteristics, signaling properties and biological functions. This review analyses the evolutionary convergence of IDO and TDO enzymes as tryptophan-catabolizing enzymes and the divergent evolution of IDO homologs to generate an enzyme family with diverse characteristics not possessed by TDO enzymes, with an emphasis on the immune system. |
| first_indexed | 2024-12-11T11:31:29Z |
| format | Article |
| id | doaj.art-1137f8f08d1d40d5a0a3202eb4f245eb |
| institution | Directory Open Access Journal |
| issn | 1664-3224 |
| language | English |
| last_indexed | 2024-12-11T11:31:29Z |
| publishDate | 2014-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Immunology |
| spelling | doaj.art-1137f8f08d1d40d5a0a3202eb4f245eb2022-12-22T01:08:52ZengFrontiers Media S.A.Frontiers in Immunology1664-32242014-10-01510.3389/fimmu.2014.00485111961Tryptophan catabolizing enzymes – party of threeHelen J Ball0Felicita Fedelis Jusof1Supun Madushani Bakmiwewa2Nicholas H Hunt3Hajime eYuasa4Sydney Medical School, University of SydneySydney Medical School, University of SydneySydney Medical School, University of SydneySydney Medical School, University of SydneyNational University Corporation Kochi UniversityIndoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that have independently evolved to catalyze the first step in tryptophan catabolism via the kynurenine pathway. The depletion of tryptophan and formation of kynurenine pathway metabolites modulates the activity of the mammalian immune, reproductive and central nervous systems. IDO and TDO enzymes can have overlapping or distinct functions depending on their expression patterns. The expression of TDO and IDO enzymes in mammals differs not only by tissue/cellular localization but also by their induction by distinct stimuli. To add to the complexity, these genes also have undergone duplications in some organisms leading to multiple isoforms of IDO or TDO. For example, many vertebrates, including all mammals, have acquired two IDO genes via gene duplication, although the IDO1-like gene has been lost in some lower vertebrate lineages. Gene duplications can allow the homologs to diverge and acquire different properties to the original gene. There is evidence for IDO enzymes having differing enzymatic characteristics, signaling properties and biological functions. This review analyses the evolutionary convergence of IDO and TDO enzymes as tryptophan-catabolizing enzymes and the divergent evolution of IDO homologs to generate an enzyme family with diverse characteristics not possessed by TDO enzymes, with an emphasis on the immune system.http://journal.frontiersin.org/Journal/10.3389/fimmu.2014.00485/fullGene DuplicationImmunoregulationconvergent evolutionkynurenine pathwaydivergent evolutionindoleamine 2 |
| spellingShingle | Helen J Ball Felicita Fedelis Jusof Supun Madushani Bakmiwewa Nicholas H Hunt Hajime eYuasa Tryptophan catabolizing enzymes – party of three Frontiers in Immunology Gene Duplication Immunoregulation convergent evolution kynurenine pathway divergent evolution indoleamine 2 |
| title | Tryptophan catabolizing enzymes – party of three |
| title_full | Tryptophan catabolizing enzymes – party of three |
| title_fullStr | Tryptophan catabolizing enzymes – party of three |
| title_full_unstemmed | Tryptophan catabolizing enzymes – party of three |
| title_short | Tryptophan catabolizing enzymes – party of three |
| title_sort | tryptophan catabolizing enzymes party of three |
| topic | Gene Duplication Immunoregulation convergent evolution kynurenine pathway divergent evolution indoleamine 2 |
| url | http://journal.frontiersin.org/Journal/10.3389/fimmu.2014.00485/full |
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