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Literature summary extracted from
- Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of D-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice (2014), Biosci. Biotechnol. Biochem., 78, 878-881 .
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | additional information | construction of TDO-knockout mice, phenotype, overview. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low | Mus musculus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.11 | D-tryptophan + O2 | Mus musculus | low activity | N-formyl-D-kynurenine | - |
? |  |
| 1.13.11.11 | D-tryptophan + O2 | Mus musculus C57BL/6 | low activity | N-formyl-D-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Mus musculus | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | Mus musculus C57BL/6 | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | additional information | Mus musculus | in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice | ? | - |
? | |
| 1.13.11.11 | additional information | Mus musculus C57BL/6 | in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice | ? | - |
? | |
| 1.13.11.52 | D-tryptophan + O2 | Mus musculus | - |
N-formyl-D-kynurenine | - |
? | |
| 1.13.11.52 | D-tryptophan + O2 | Mus musculus C57BL/6 | - |
N-formyl-D-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Mus musculus | - |
N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | Mus musculus C57BL/6 | - |
N-formyl-L-kynurenine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.11 | Mus musculus | P48776 | - |
- |
| 1.13.11.11 | Mus musculus C57BL/6 | P48776 | - |
- |
| 1.13.11.52 | Mus musculus | P28776 | - |
- |
| 1.13.11.52 | Mus musculus C57BL/6 | P28776 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.13.11.11 | liver | - |
Mus musculus | - |
| 1.13.11.52 | liver | - |
Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.11 | D-tryptophan + O2 | low activity | Mus musculus | N-formyl-D-kynurenine | - |
? | |
| 1.13.11.11 | D-tryptophan + O2 | low activity | Mus musculus C57BL/6 | N-formyl-D-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Mus musculus | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | L-tryptophan + O2 | - |
Mus musculus C57BL/6 | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.11 | additional information | in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice | Mus musculus | ? | - |
? | |
| 1.13.11.11 | additional information | the kcat of tryptophan-2,3-dioxygenase (TDO) is 10 times lower for D-Trp than that for L-Trp in vitro | Mus musculus | ? | - |
? | |
| 1.13.11.11 | additional information | in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice | Mus musculus C57BL/6 | ? | - |
? | |
| 1.13.11.11 | additional information | the kcat of tryptophan-2,3-dioxygenase (TDO) is 10 times lower for D-Trp than that for L-Trp in vitro | Mus musculus C57BL/6 | ? | - |
? | |
| 1.13.11.52 | D-tryptophan + O2 | - |
Mus musculus | N-formyl-D-kynurenine | - |
? | |
| 1.13.11.52 | D-tryptophan + O2 | - |
Mus musculus C57BL/6 | N-formyl-D-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Mus musculus | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | L-tryptophan + O2 | - |
Mus musculus C57BL/6 | N-formyl-L-kynurenine | - |
? | |
| 1.13.11.52 | additional information | although the kcat of indoleamine-2,3-dioxygenase (IDO) is similar for D-Trp and L-Trp, the Km of IDO is approximately 170fold higher for L-Trp than that for D-Trp | Mus musculus | ? | - |
? | |
| 1.13.11.52 | additional information | although the kcat of indoleamine-2,3-dioxygenase (IDO) is similar for D-Trp and L-Trp, the Km of IDO is approximately 170fold higher for L-Trp than that for D-Trp | Mus musculus C57BL/6 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | TDO | - |
Mus musculus |
| 1.13.11.11 | TDO2 | - |
Mus musculus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.11 | malfunction | TDO knockout mice require a minimum of 0.06% dietary L-Trp, which value is about 2 mg/d/mouse | Mus musculus |
| 1.13.11.11 | metabolism | comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice | Mus musculus |
| 1.13.11.11 | physiological function | the enzyme is involved in nicotinamide biosynthesis. Comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice | Mus musculus |
| 1.13.11.52 | metabolism | comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) and indoleamine 2,3-dioxygenase (IDO) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice | Mus musculus |
| 1.13.11.52 | physiological function | the enzyme is involved in nicotinamide biosynthesis. Comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO, EC 1.13.11.11) and indoleamine 2,3-dioxygenase (IDO) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice | Mus musculus |
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