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Literature summary extracted from
- Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes (2015), J. Exp. Zool. B, 324, 128-140 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.11 | gene 33737, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Monosiga brevicollis |
| 1.13.11.11 | gene BRAFLDRAFT_210874, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Branchiostoma floridae |
| 1.13.11.11 | gene C28H8.11, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Caenorhabditis elegans |
| 1.13.11.11 | gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Rattus norvegicus |
| 1.13.11.11 | gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Homo sapiens |
| 1.13.11.11 | gene TDOa, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Strongylocentrotus purpuratus |
| 1.13.11.11 | gene v1g157887, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Nematostella vectensis |
| 1.13.11.11 | gene vCG5163, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae | Drosophila melanogaster |
| 1.13.11.52 | DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. Complementation of the enzyme-deficient Saccharomyces cerevisiae | Haliotis diversicolor |
| 1.13.11.52 | DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Strongylocentrotus purpuratus |
| 1.13.11.52 | gene 31854, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. Slight complementation of the enzyme-deficient Saccharomyces cerevisiae | Monosiga brevicollis |
| 1.13.11.52 | gene BRAFLDRAFT_126354, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. Slight complementation of the enzyme-deficient Saccharomyces cerevisiae | Branchiostoma floridae |
| 1.13.11.52 | gene IDO1, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Mus musculus |
| 1.13.11.52 | gene IDO1, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Homo sapiens |
| 1.13.11.52 | gene IDO1, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Danio rerio |
| 1.13.11.52 | gene Ido2, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Mus musculus |
| 1.13.11.52 | gene iso1, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Xenopus laevis |
| 1.13.11.52 | gene v1g244579, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain KRX. No complementation of the enzyme-deficient Saccharomyces cerevisiae | Nematostella vectensis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Strongylocentrotus purpuratus | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Rattus norvegicus | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Homo sapiens | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Drosophila melanogaster | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Nematostella vectensis | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Monosiga brevicollis | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Branchiostoma floridae | |
| 1.13.11.11 | additional information | - |
additional information | Michaelis-Menten kinetics | Caenorhabditis elegans | |
| 1.13.11.11 | 0.0825 | - |
L-tryptophan | pH 8.0, 37°C | Homo sapiens |  |
| 1.13.11.11 | 0.221 | - |
L-tryptophan | pH 7.0, 37°C | Rattus norvegicus | |
| 1.13.11.11 | 0.277 | - |
L-tryptophan | pH 8.0, 37°C | Monosiga brevicollis | |
| 1.13.11.52 | 0.0191 | - |
L-tryptophan | pH 6.5, 37°C | Mus musculus | |
| 1.13.11.52 | 0.074 | - |
L-tryptophan | pH 6.5, 37°C | Homo sapiens | |
| 1.13.11.52 | 3.2 | - |
L-tryptophan | pH 7.5, 37°C | Nematostella vectensis | |
| 1.13.11.52 | 7.4 | - |
L-tryptophan | pH 7.5, 37°C | Xenopus laevis | |
| 1.13.11.52 | 29.9 | - |
L-tryptophan | pH 7.0, 37°C | Haliotis diversicolor | |
| 1.13.11.52 | 33.9 | - |
L-tryptophan | pH 7.5, 37°C | Danio rerio | |
| 1.13.11.52 | 42.7 | - |
L-tryptophan | pH 7.0, 37°C | Monosiga brevicollis | |
| 1.13.11.52 | 45.9 | - |
L-tryptophan | pH 7.5, 37°C | Mus musculus | |
| 1.13.11.52 | 55.4 | - |
L-tryptophan | pH 7.5, 37°C | Branchiostoma floridae | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.11 | L-tryptophan + O2 | Strongylocentrotus purpuratus | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Rattus norvegicus | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Homo sapiens | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Drosophila melanogaster | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Nematostella vectensis | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Monosiga brevicollis | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Branchiostoma floridae | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Caenorhabditis elegans | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Strongylocentrotus purpuratus | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Mus musculus | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Homo sapiens | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Nematostella vectensis | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Branchiostoma floridae | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Monosiga brevicollis | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Haliotis diversicolor | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Xenopus laevis | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Danio rerio | - |
N-formyl-L-kynurenine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.11 | Branchiostoma floridae | C3XXE6 | - |
- |
| 1.13.11.11 | Caenorhabditis elegans | Q09474 | - |
- |
| 1.13.11.11 | Drosophila melanogaster | P20351 | - |
- |
| 1.13.11.11 | Homo sapiens | P48775 | - |
- |
| 1.13.11.11 | Monosiga brevicollis | A9V766 | - |
- |
| 1.13.11.11 | Nematostella vectensis | A7RFF0 | - |
- |
| 1.13.11.11 | no activity in Brugia malayi | - |
- |
- |
| 1.13.11.11 | no activity in Saccharomyces cerevisiae | - |
- |
- |
| 1.13.11.11 | no activity in Schistosoma mansoni | - |
- |
- |
| 1.13.11.11 | Rattus norvegicus | P21643 | - |
- |
| 1.13.11.11 | Strongylocentrotus purpuratus | - |
- |
- |
| 1.13.11.52 | Branchiostoma floridae | C3Y9Y8 | - |
- |
| 1.13.11.52 | Danio rerio | B0V1K8 | - |
- |
| 1.13.11.52 | Haliotis diversicolor | Q6F3I3 | MIP-I; no activity by IDO-like Mb | - |
| 1.13.11.52 | Homo sapiens | P14902 | - |
- |
| 1.13.11.52 | Monosiga brevicollis | A9UVU0 | - |
- |
| 1.13.11.52 | Mus musculus | P28776 | - |
- |
| 1.13.11.52 | Mus musculus | Q8R0V5 | - |
- |
| 1.13.11.52 | Nematostella vectensis | A7SDW8 | - |
- |
| 1.13.11.52 | Strongylocentrotus purpuratus | - |
- |
- |
| 1.13.11.52 | Xenopus laevis | A2BD60 | - |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.52 | additional information | - |
low IDO activity of MIP protein, no activity by IDO-like Mb protein | Haliotis diversicolor |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.11 | L-tryptophan + O2 | - |
Strongylocentrotus purpuratus | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Rattus norvegicus | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Homo sapiens | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Drosophila melanogaster | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Nematostella vectensis | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Monosiga brevicollis | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Branchiostoma floridae | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Caenorhabditis elegans | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Strongylocentrotus purpuratus | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Mus musculus | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Homo sapiens | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Nematostella vectensis | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Branchiostoma floridae | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Monosiga brevicollis | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Haliotis diversicolor | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Xenopus laevis | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Danio rerio | N-formyl-L-kynurenine | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | 33737 | - |
Monosiga brevicollis |
| 1.13.11.11 | BRAFLDRAFT_210874 | - |
Branchiostoma floridae |
| 1.13.11.11 | C28H8.11 | - |
Caenorhabditis elegans |
| 1.13.11.11 | TDO | - |
Strongylocentrotus purpuratus |
| 1.13.11.11 | TDO | - |
Rattus norvegicus |
| 1.13.11.11 | TDO | - |
Homo sapiens |
| 1.13.11.11 | TDO | - |
Drosophila melanogaster |
| 1.13.11.11 | TDO | - |
Nematostella vectensis |
| 1.13.11.11 | TDO | - |
Monosiga brevicollis |
| 1.13.11.11 | TDO | - |
Branchiostoma floridae |
| 1.13.11.11 | TDO | - |
Caenorhabditis elegans |
| 1.13.11.11 | TDOa | - |
Strongylocentrotus purpuratus |
| 1.13.11.11 | v1g157887 | - |
Nematostella vectensis |
| 1.13.11.11 | vCG5163 | - |
Drosophila melanogaster |
| 1.13.11.52 | 31854 | - |
Monosiga brevicollis |
| 1.13.11.52 | BRAFLDRAFT_126354 | - |
Branchiostoma floridae |
| 1.13.11.52 | IDO | - |
Strongylocentrotus purpuratus |
| 1.13.11.52 | IDO | - |
Homo sapiens |
| 1.13.11.52 | IDO | - |
Nematostella vectensis |
| 1.13.11.52 | IDO | - |
Branchiostoma floridae |
| 1.13.11.52 | IDO | - |
Monosiga brevicollis |
| 1.13.11.52 | IDO | - |
Haliotis diversicolor |
| 1.13.11.52 | IDO | - |
Danio rerio |
| 1.13.11.52 | IDO1 | - |
Mus musculus |
| 1.13.11.52 | IDO1 | - |
Xenopus laevis |
| 1.13.11.52 | IDO1 | - |
Homo sapiens |
| 1.13.11.52 | IDO1 | - |
Danio rerio |
| 1.13.11.52 | IDO2 | - |
Mus musculus |
| 1.13.11.52 | v1g244579 | - |
Nematostella vectensis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.11 | 37 | - |
assay at | Strongylocentrotus purpuratus |
| 1.13.11.11 | 37 | - |
assay at | Rattus norvegicus |
| 1.13.11.11 | 37 | - |
assay at | Homo sapiens |
| 1.13.11.11 | 37 | - |
assay at | Drosophila melanogaster |
| 1.13.11.11 | 37 | - |
assay at | Nematostella vectensis |
| 1.13.11.11 | 37 | - |
assay at | Monosiga brevicollis |
| 1.13.11.11 | 37 | - |
assay at | Branchiostoma floridae |
| 1.13.11.11 | 37 | - |
assay at | Caenorhabditis elegans |
| 1.13.11.52 | 37 | - |
assay at | Strongylocentrotus purpuratus |
| 1.13.11.52 | 37 | - |
assay at | Mus musculus |
| 1.13.11.52 | 37 | - |
assay at | Homo sapiens |
| 1.13.11.52 | 37 | - |
assay at | Nematostella vectensis |
| 1.13.11.52 | 37 | - |
assay at | Branchiostoma floridae |
| 1.13.11.52 | 37 | - |
assay at | Monosiga brevicollis |
| 1.13.11.52 | 37 | - |
assay at | Haliotis diversicolor |
| 1.13.11.52 | 37 | - |
assay at | Xenopus laevis |
| 1.13.11.52 | 37 | - |
assay at | Danio rerio |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.11 | 7 | - |
- |
Rattus norvegicus |
| 1.13.11.11 | 8 | - |
- |
Homo sapiens |
| 1.13.11.11 | 8 | - |
- |
Monosiga brevicollis |
| 1.13.11.52 | 6.5 | - |
assay at | Mus musculus |
| 1.13.11.52 | 6.5 | - |
assay at | Homo sapiens |
| 1.13.11.52 | 7 | - |
assay at | Monosiga brevicollis |
| 1.13.11.52 | 7 | - |
assay at | Haliotis diversicolor |
| 1.13.11.52 | 7.5 | - |
assay at | Mus musculus |
| 1.13.11.52 | 7.5 | - |
assay at | Nematostella vectensis |
| 1.13.11.52 | 7.5 | - |
assay at | Branchiostoma floridae |
| 1.13.11.52 | 7.5 | - |
assay at | Xenopus laevis |
| 1.13.11.52 | 7.5 | - |
assay at | Danio rerio |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.11 | heme | - |
Nematostella vectensis | |
| 1.13.11.52 | heme | - |
Strongylocentrotus purpuratus | |
| 1.13.11.52 | heme | - |
Mus musculus | |
| 1.13.11.52 | heme | - |
Homo sapiens | |
| 1.13.11.52 | heme | - |
Nematostella vectensis | |
| 1.13.11.52 | heme | - |
Branchiostoma floridae | |
| 1.13.11.52 | heme | - |
Monosiga brevicollis | |
| 1.13.11.52 | heme | - |
Haliotis diversicolor | |
| 1.13.11.52 | heme | - |
Xenopus laevis | |
| 1.13.11.52 | heme | - |
Danio rerio | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Strongylocentrotus purpuratus |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Rattus norvegicus |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Homo sapiens |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Drosophila melanogaster |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Nematostella vectensis |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Monosiga brevicollis |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Branchiostoma floridae |
| 1.13.11.11 | evolution | indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview | Caenorhabditis elegans |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Strongylocentrotus purpuratus |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Mus musculus |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Homo sapiens |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Nematostella vectensis |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Branchiostoma floridae |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Monosiga brevicollis |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Haliotis diversicolor |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Xenopus laevis |
| 1.13.11.52 | evolution | indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview. Some lineages have independently generated multiple IDO paralogues through gene duplications. Only mammalian IDO1s and fungal typical IDOs have high affinity and catalytic efficiency for L-Trp catabolism, comparable to TDOs. Invertebrate IDO enzymes have low affinity and catalytic efficiency for L-Trp catabolism. Phylogenetic analysis. the phylogenetic distribution of low catalytic-efficiency IDOs indicates the ancestral IDO also had low affinity and catalytic efficiency for L-Trp catabolism. IDOs with high catalytic-efficiency for L-Trp catabolism may have evolved in certain lineages to fulfill particular biological roles. The low catalytic efficiency IDOs have been well conserved in a number of lineages throughout their evolution, although it is not clear that the enzymes contribute significantly to L-Trp catabolism in these species | Danio rerio |
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