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Literature summary for 1.13.11.11 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)
| Cloned (Comment) | Organism |
|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Strongylocentrotus purpuratus | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Rattus norvegicus | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Homo sapiens | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Drosophila melanogaster | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Nematostella vectensis | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Monosiga brevicollis | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Branchiostoma floridae | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Caenorhabditis elegans | |
| 0.0825 | - |
L-tryptophan | pH 8.0, 37°C | Homo sapiens |  |
| 0.221 | - |
L-tryptophan | pH 7.0, 37°C | Rattus norvegicus | |
| 0.277 | - |
L-tryptophan | pH 8.0, 37°C | Monosiga brevicollis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-tryptophan + O2 | Strongylocentrotus purpuratus | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Rattus norvegicus | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Homo sapiens | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Drosophila melanogaster | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Nematostella vectensis | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Monosiga brevicollis | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Branchiostoma floridae | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Caenorhabditis elegans | - |
N-formyl-L-kynurenine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Branchiostoma floridae | C3XXE6 | - |
- |
| Caenorhabditis elegans | Q09474 | - |
- |
| Drosophila melanogaster | P20351 | - |
- |
| Homo sapiens | P48775 | - |
- |
| Monosiga brevicollis | A9V766 | - |
- |
| Nematostella vectensis | A7RFF0 | - |
- |
| no activity in Brugia malayi | - |
- |
- |
| no activity in Saccharomyces cerevisiae | - |
- |
- |
| no activity in Schistosoma mansoni | - |
- |
- |
| Rattus norvegicus | P21643 | - |
- |
| Strongylocentrotus purpuratus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-tryptophan + O2 | - |
Strongylocentrotus purpuratus | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Rattus norvegicus | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Homo sapiens | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Drosophila melanogaster | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Nematostella vectensis | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Monosiga brevicollis | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Branchiostoma floridae | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Caenorhabditis elegans | N-formyl-L-kynurenine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 33737 | - |
Monosiga brevicollis |
| BRAFLDRAFT_210874 | - |
Branchiostoma floridae |
| C28H8.11 | - |
Caenorhabditis elegans |
| TDO | - |
Strongylocentrotus purpuratus |
| TDO | - |
Rattus norvegicus |
| TDO | - |
Homo sapiens |
| TDO | - |
Drosophila melanogaster |
| TDO | - |
Nematostella vectensis |
| TDO | - |
Monosiga brevicollis |
| TDO | - |
Branchiostoma floridae |
| TDO | - |
Caenorhabditis elegans |
| TDOa | - |
Strongylocentrotus purpuratus |
| v1g157887 | - |
Nematostella vectensis |
| vCG5163 | - |
Drosophila melanogaster |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Strongylocentrotus purpuratus |
| 37 | - |
assay at | Rattus norvegicus |
| 37 | - |
assay at | Homo sapiens |
| 37 | - |
assay at | Drosophila melanogaster |
| 37 | - |
assay at | Nematostella vectensis |
| 37 | - |
assay at | Monosiga brevicollis |
| 37 | - |
assay at | Branchiostoma floridae |
| 37 | - |
assay at | Caenorhabditis elegans |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Rattus norvegicus |
| 8 | - |
- |
Homo sapiens |
| 8 | - |
- |
Monosiga brevicollis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Nematostella vectensis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
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