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Literature summary for 1.13.11.52 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]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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

Synonyms Comment Organism
hTDO
-
Homo sapiens

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
heme
-
Homo sapiens