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 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 | 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 | 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 | 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 | 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 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Rattus norvegicus |
8 | - |
- |
Homo sapiens |
8 | - |
- |
Monosiga brevicollis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Nematostella vectensis |
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 |