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Literature summary for 1.13.11.52 extracted from

  • Gupta, R.; Fu, R.; Liu, A.; Hendrich, M.P.
    EPR and Moessbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase (2010), J. Am. Chem. Soc., 132, 1098-1109.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Cupriavidus metallidurans

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Cupriavidus metallidurans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Superdex 200 gel filtration Cupriavidus metallidurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + O2
-
Cupriavidus metallidurans N-formyl-L-kynurenine
-
?

Subunits

Subunits Comment Organism
homotetramer x-ray crystallography Cupriavidus metallidurans

Synonyms

Synonyms Comment Organism
TDO
-
Cupriavidus metallidurans

Cofactor

Cofactor Comment Organism Structure
heme
-
Cupriavidus metallidurans

General Information

General Information Comment Organism
metabolism tryptophan 2,3-dioxygenase is an essential enzyme in the pathway of NAD biosynthesis Cupriavidus metallidurans