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 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 | 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 | 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 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 | 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 | 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 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 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 | 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 | 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 |