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Literature summary extracted from

  • Booth, E.S.; Basran, J.; Lee, M.; Handa, S.; Raven, E.L.
    Substrate oxidation by indoleamine 2,3-dioxygenase evidence for a common reaction mechanism (2015), J. Biol. Chem., 290, 30924-30930 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.11.52 L-ascorbate required Homo sapiens
1.13.11.52 methylene blue required Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.52 additional information
-
 additional information steadystate, pre-steady-state and stopped-flow kinetics Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.52 Fe2+ ferric heme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.52 D-tryptophan + O2 Homo sapiens
-
 N-formyl-D-kynurenine
-
 ?
1.13.11.52 L-tryptophan + O2 Homo sapiens
-
 N-formyl-L-kynurenine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.52 Homo sapiens P14902
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.13.11.52 L-tryptophan + O2 = N-formyl-L-kynurenine electrophilic or radical addition reaction mechanism via formation of a transient ferryl intermediate, assigned as a Compound II (ferryl) species, during oxidation of L-Trp, 1-methyl-L-Trp, and a number of other substrate analogues, overview. A common reaction mechanism for indoleamine 2,3-dioxygenase-catalyzed oxidation of tryptophan and other tryptophan analogues is determined Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.52 1-methyl-L-tryptophan + O2
-
 Homo sapiens N-methyl-N-formyl-L-kynurenine
-
 ?
1.13.11.52 5-fluoro-L-tryptophan + O2
-
 Homo sapiens 5-fluoro-N-formyl-L-kynurenine
-
 ?
1.13.11.52 5-hydroxy-L-tryptophan + O2
-
 Homo sapiens 5-hydroxy-N-formyl-L-kynurenine
-
 ?
1.13.11.52 5-methoxy-L-tryptophan + O2
-
 Homo sapiens 5-methoxy-N-formyl-L-kynurenine
-
 ?
1.13.11.52 5-methyl-DL-tryptophan + O2
-
 Homo sapiens 5-methyl-N-formyl-DL-kynurenine
-
 ?
1.13.11.52 beta-[3-benzo(b)thienyl]-L-alanine + O2
-
 Homo sapiens ?
-
 ?
1.13.11.52 D-tryptophan + O2
-
 Homo sapiens N-formyl-D-kynurenine
-
 ?
1.13.11.52 indole-3-propionic acid + O2 altered kinetics for IPA (very long lag phase) as being consistent with a role for the ammonium group in stabilizing the ferric superoxide complex (via the radical pathway). The rate-limiting steps are different from the other substrates examined so that Compound II does not accumulate, but product formation is still possible, product formation ananlysis by LC-MS Homo sapiens ?
-
 ?
1.13.11.52 L-tryptophan + O2
-
 Homo sapiens N-formyl-L-kynurenine
-
 ?
1.13.11.52 additional information formation of ferrous-oxy hIDO and comparison with the ternary complex, overview Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.52 hIDO
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.52 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.52 8
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.52 heme ferric heme Homo sapiens

General Information

EC Number General Information Comment Organism
1.13.11.52 metabolism the initial and rate-limiting step of the kynurenine pathway involves oxidation of L-Trp toN-formylkynurenine. This is an O2-dependent process and catalyzed by indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase, EC 1.13.11.11 Homo sapiens