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Literature summary for 1.13.11.11 extracted from

  • Nienhaus, K.; Hahn, V.; Huepfel, M.; Nienhaus, G.U.
    Substrate binding primes human tryptophan 2,3-dioxygenase for ligand binding (2017), J. Phys. Chem. B, 121, 7412-7420 .
    View publication on PubMed
Search for more literature for 1.13.11.11

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information reaction and ligand binding kinetics, two hTDO conformations exist that bind CO in a bimolecular reaction, but with very different rates, kinetic calculations, overview 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.
L-tryptophan + O2 Homo sapiens
-
 N-formyl-L-kynurenine
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P48775
-
-

Reaction

Reaction Comment Organism Reaction ID
L-tryptophan + O2 = N-formyl-L-kynurenine catalytic mechanism, modeling. hTDO exists as two discrete species with markedly different ligand binding properties. The active site environment of the slowly rebinding species is structurally very heterogeneous and ligand access to greatly hindered. Binding of the L-Trp substrate stabilizes the faster-binding species, which features a well-structured active site and offers facile access of the ligand to the heme iron. This mechanism ensures that the ternary complex forms mainly by first binding the L-Trp substrate, which primes the active site for the subsequent binding of O2, which ensures efficient enzyme action Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + O2
-
 Homo sapiens N-formyl-L-kynurenine
-
 ?
additional information enzyme-CO binding analysis, overview Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
hTDO
-
 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme ferric heme Homo sapiens

General Information

General Information Comment Organism
additional information the active site of the enzyme is highly dynamic Homo sapiens
physiological function the human heme enzyme tryptophan 2,3-dioxygenase (hTDO) catalyzes the insertion of dioxygen into its cognate substrate, L-tryptophan (L-Trp) Homo sapiens