Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.11.52 extracted from

  • Fu, R.; Gupta, R.; Geng, J.; Dornevil, K.; Wang, S.; Zhang, Y.; Hendrich, M.P.; Liu, A.
    Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase (2011), J. Biol. Chem., 286, 26541-26554.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
H2O2 hydrogen peroxide-triggered enzyme reactivation from the resting ferric oxidation state to the catalytically active ferrous form, modeling, overview Cupriavidus metallidurans

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant His-tagged enzyme Cupriavidus metallidurans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required, hydrogen peroxide-triggered enzyme reactivation from the resting ferric oxidation state to the catalytically active ferrous form, modeling, overviews 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
recombinant His-tagged enzyme by nickel affinity chromatography and 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
-
?

Synonyms

Synonyms Comment Organism
TDO
-
Cupriavidus metallidurans
tryptophan dioxygenase
-
Cupriavidus metallidurans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Cupriavidus metallidurans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Cupriavidus metallidurans