Cloned (Comment) | Organism |
---|---|
recombinant expression in Escherichia coli | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of IDO-catalyzed indole oxidation as supported by H2O2, overview. The rate of disappearance of indole as a function of [H2O2] in the IDOFe3+-catalyzed reaction exhibits Michaelis-Menten behavior, with Km of about 1.1 mM for peroxide [indole] | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | heme-containing enzyme | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-tryptophan + O2 | Homo sapiens | IDO1 | N-formyl-D-kynurenine | - |
? | |
L-tryptophan + O2 | Homo sapiens | IDO1 and IDO2 | N-formyl-L-kynurenine | - |
? | |
additional information | Homo sapiens | the enzyme catalyzes the oxidation of indole by H2O2, with generation of 2- and 3-oxoindole as the major products, in the absence of O2 and reducing agents and is not inhibited by superoxide dismutase or hydroxyl radical scavengers, although it is strongly inhibited by L-Trp. IDO inserts oxygen into indole in a reaction that is mechanistically analogous to the peroxide shunt pathway of cytochrome P450 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli involving affinity chromatography | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-tryptophan + O2 | IDO1 | Homo sapiens | N-formyl-D-kynurenine | - |
? | |
L-tryptophan + O2 | IDO1 and IDO2 | Homo sapiens | N-formyl-L-kynurenine | - |
? | |
additional information | the enzyme catalyzes the oxidation of indole by H2O2, with generation of 2- and 3-oxoindole as the major products, in the absence of O2 and reducing agents and is not inhibited by superoxide dismutase or hydroxyl radical scavengers, although it is strongly inhibited by L-Trp. IDO inserts oxygen into indole in a reaction that is mechanistically analogous to the peroxide shunt pathway of cytochrome P450 | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IDO | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Homo sapiens |