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Literature summary extracted from

  • Batabyal, D.; Yeh, S.R.
    Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase (2007), J. Am. Chem. Soc., 129, 15690-15701.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.52 0.18
-
 D-tryptophan pH 7.0 Homo sapiens
1.13.11.52 0.19
-
 L-tryptophan pH 7.0 Homo sapiens

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.52 D-tryptophan + O2 the initial deprotonation reaction of the indole NH group in hTDO is carried out by the evolutionarily conserved distal His. stereospecificity of hTDO is determined by the efficiency of the dioxygen chemistry Homo sapiens N-formyl-D-kynurenine
-
 ?
1.13.11.52 L-tryptophan + O2 the initial deprotonation reaction of the indole NH group in hTDO is carried out by the evolutionarily conserved distal His. stereospecificity of hTDO is determined by the efficiency of the dioxygen chemistry Homo sapiens N-formyl-L-kynurenine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.52 hTDO
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.52 0.2
-
 D-tryptophan pH 7.0 Homo sapiens
1.13.11.52 2.1
-
 L-tryptophan pH 7.0 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.11.52 heme
-
 Homo sapiens