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

BRENDA support

Literature summary for 1.14.11.17 extracted from

  • McCusker, K.P.; Klinman, J.P.
    Modular behavior of tauD provides insight into the origin of specificity in alpha-ketoglutarate-dependent nonheme iron oxygenases (2009), Proc. Natl. Acad. Sci. USA, 106, 19791-19795.
    View publication on PubMed
Search for more literature for 1.14.11.17

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
F159A decrease in coupling of oxygen activation to C-H cleavage Escherichia coli
F159G decrease in coupling of oxygen activation to C-H cleavage Escherichia coli
F159L decrease in coupling of oxygen activation to C-H cleavage Escherichia coli
F159V decrease in coupling of oxygen activation to C-H cleavage Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P37610
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2 assay at pH 6.2, 30°C Escherichia coli methylaminoacetaldehyde + succinate + sulfite + CO2
-
 ?

Synonyms

Synonyms Comment Organism
TauD
-
 Escherichia coli
taurine alpha-ketoglutarate dioxygenase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
 assay at Escherichia coli