Literature summary for 1.13.11.52 extracted from

Zhang, Y.; Kang, S.A.; Mukherjee, T.; Bale, S.; Crane, B.R.; Begley, T.P.; Ealick, S.E.
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis (2007), Biochemistry, 46, 145-155.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
vapour-diffusion method, structure of the enzyme with cofactor heme bound in the active site, 2.4 A resolution	Cupriavidus metallidurans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-tryptophan + O2	Cupriavidus metallidurans	the enzyme is involved in tryptophan catabolism and in quinolinate biosynthesis	N-formyl-L-kynurenine	-	ir

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus metallidurans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Cupriavidus metallidurans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-tryptophan + O2	-	Cupriavidus metallidurans	N-formyl-L-kynurenine	-	ir
L-tryptophan + O2	the enzyme is involved in tryptophan catabolism and in quinolinate biosynthesis	Cupriavidus metallidurans	N-formyl-L-kynurenine	-	ir

Synonyms

Synonyms	Comment	Organism
TDO	-	Cupriavidus metallidurans

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Cupriavidus metallidurans

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Release 2023.1 (January 2023)