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Literature summary for 1.13.11.52 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
Search for more literature for 1.13.11.52

Activating Compound

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P14902
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-methyl-L-tryptophan + O2
-
 Homo sapiens N-methyl-N-formyl-L-kynurenine
-
 ?
5-fluoro-L-tryptophan + O2
-
 Homo sapiens 5-fluoro-N-formyl-L-kynurenine
-
 ?
5-hydroxy-L-tryptophan + O2
-
 Homo sapiens 5-hydroxy-N-formyl-L-kynurenine
-
 ?
5-methoxy-L-tryptophan + O2
-
 Homo sapiens 5-methoxy-N-formyl-L-kynurenine
-
 ?
5-methyl-DL-tryptophan + O2
-
 Homo sapiens 5-methyl-N-formyl-DL-kynurenine
-
 ?
beta-[3-benzo(b)thienyl]-L-alanine + O2
-
 Homo sapiens ?
-
 ?
D-tryptophan + O2
-
 Homo sapiens N-formyl-D-kynurenine
-
 ?
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 ?
-
 ?
L-tryptophan + O2
-
 Homo sapiens N-formyl-L-kynurenine
-
 ?
additional information formation of ferrous-oxy hIDO and comparison with the ternary complex, overview Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
hIDO
-
 Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
heme ferric heme Homo sapiens

General Information

General Information Comment Organism
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