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

BRENDA support

Literature summary for 1.13.11.20 extracted from

  • Gardner, J.D.; Pierce, B.S.; Fox, B.G.; Brunold, T.C.
    Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications (2010), Biochemistry, 49, 6033-6041.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)pLysS cells Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ CDO is a mononuclear non-heme Fe2+-dependent dioxygenase Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose column chromatography and Superdex 200 gel filtration Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
Mus musculus 3-sulfino-L-alanine
-
?
additional information CDO cannot catalyze the oxidation of selenocysteine Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
CDO
-
Mus musculus