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Literature summary for 1.13.11.52 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 |
|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0191 | - |
L-tryptophan | pH 6.5, 37°C | Mus musculus |  |
| 0.074 | - |
L-tryptophan | pH 6.5, 37°C | Homo sapiens | |
| 3.2 | - |
L-tryptophan | pH 7.5, 37°C | Nematostella vectensis | |
| 7.4 | - |
L-tryptophan | pH 7.5, 37°C | Xenopus laevis | |
| 29.9 | - |
L-tryptophan | pH 7.0, 37°C | Haliotis diversicolor | |
| 33.9 | - |
L-tryptophan | pH 7.5, 37°C | Danio rerio | |
| 42.7 | - |
L-tryptophan | pH 7.0, 37°C | Monosiga brevicollis | |
| 45.9 | - |
L-tryptophan | pH 7.5, 37°C | Mus musculus | |
| 55.4 | - |
L-tryptophan | pH 7.5, 37°C | Branchiostoma floridae | |
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 | Mus musculus | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Homo sapiens | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Nematostella vectensis | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Branchiostoma floridae | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Monosiga brevicollis | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Haliotis diversicolor | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Xenopus laevis | - |
N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | Danio rerio | - |
N-formyl-L-kynurenine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Branchiostoma floridae | C3Y9Y8 | - |
- |
| Danio rerio | B0V1K8 | - |
- |
| Haliotis diversicolor | Q6F3I3 | MIP-I; no activity by IDO-like Mb | - |
| Homo sapiens | P14902 | - |
- |
| Monosiga brevicollis | A9UVU0 | - |
- |
| Mus musculus | P28776 | - |
- |
| Mus musculus | Q8R0V5 | - |
- |
| Nematostella vectensis | A7SDW8 | - |
- |
| Strongylocentrotus purpuratus | - |
- |
- |
| Xenopus laevis | A2BD60 | - |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
low IDO activity of MIP protein, no activity by IDO-like Mb protein | Haliotis diversicolor |
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 | - |
Mus musculus | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Homo sapiens | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Nematostella vectensis | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Branchiostoma floridae | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Monosiga brevicollis | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Haliotis diversicolor | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Xenopus laevis | N-formyl-L-kynurenine | - |
? | |
| L-tryptophan + O2 | - |
Danio rerio | N-formyl-L-kynurenine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 31854 | - |
Monosiga brevicollis |
| BRAFLDRAFT_126354 | - |
Branchiostoma floridae |
| IDO | - |
Strongylocentrotus purpuratus |
| IDO | - |
Homo sapiens |
| IDO | - |
Nematostella vectensis |
| IDO | - |
Branchiostoma floridae |
| IDO | - |
Monosiga brevicollis |
| IDO | - |
Haliotis diversicolor |
| IDO | - |
Danio rerio |
| IDO1 | - |
Mus musculus |
| IDO1 | - |
Xenopus laevis |
| IDO1 | - |
Homo sapiens |
| IDO1 | - |
Danio rerio |
| IDO2 | - |
Mus musculus |
| v1g244579 | - |
Nematostella vectensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Strongylocentrotus purpuratus |
| 37 | - |
assay at | Mus musculus |
| 37 | - |
assay at | Homo sapiens |
| 37 | - |
assay at | Nematostella vectensis |
| 37 | - |
assay at | Branchiostoma floridae |
| 37 | - |
assay at | Monosiga brevicollis |
| 37 | - |
assay at | Haliotis diversicolor |
| 37 | - |
assay at | Xenopus laevis |
| 37 | - |
assay at | Danio rerio |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
assay at | Mus musculus |
| 6.5 | - |
assay at | Homo sapiens |
| 7 | - |
assay at | Monosiga brevicollis |
| 7 | - |
assay at | Haliotis diversicolor |
| 7.5 | - |
assay at | Mus musculus |
| 7.5 | - |
assay at | Nematostella vectensis |
| 7.5 | - |
assay at | Branchiostoma floridae |
| 7.5 | - |
assay at | Xenopus laevis |
| 7.5 | - |
assay at | Danio rerio |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Strongylocentrotus purpuratus | |
| heme | - |
Mus musculus | |
| heme | - |
Homo sapiens | |
| heme | - |
Nematostella vectensis | |
| heme | - |
Branchiostoma floridae | |
| heme | - |
Monosiga brevicollis | |
| heme | - |
Haliotis diversicolor | |
| heme | - |
Xenopus laevis | |
| heme | - |
Danio rerio | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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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