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Literature summary for 1.13.11.52 extracted from

  • Maeta, A.; Sano, M.; Fukuwatari, T.; Funakoshi, H.; Nakamura, T.; Shibata, K.
    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 .
    View publication on PubMed
Search for more literature for 1.13.11.52

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-tryptophan + O2 Mus musculus
-
 N-formyl-D-kynurenine
-
 ?
D-tryptophan + O2 Mus musculus C57BL/6
-
 N-formyl-D-kynurenine
-
 ?
L-tryptophan + O2 Mus musculus
-
 N-formyl-L-kynurenine
-
 ?
L-tryptophan + O2 Mus musculus C57BL/6
-
 N-formyl-L-kynurenine
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P28776
-
-
Mus musculus C57BL/6 P28776
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-tryptophan + O2
-
 Mus musculus N-formyl-D-kynurenine
-
 ?
D-tryptophan + O2
-
 Mus musculus C57BL/6 N-formyl-D-kynurenine
-
 ?
L-tryptophan + O2
-
 Mus musculus N-formyl-L-kynurenine
-
 ?
L-tryptophan + O2
-
 Mus musculus C57BL/6 N-formyl-L-kynurenine
-
 ?
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 ?
-
 ?
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 ?
-
 ?

General Information

General Information Comment Organism
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
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