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Literature summary for 1.13.11.20 extracted from

  • Crawford, J.A.; Li, W.; Pierce, B.S.
    Single turnover of substrate-bound ferric cysteine dioxygenase with superoxide anion: enzymatic reactivation, product formation, and a transient intermediate (2011), Biochemistry, 50, 10241-10253.
    View publication on PubMed
Search for more literature for 1.13.11.20

Cloned(Commentary)

Cloned (Comment) Organism
gene cdo, expression as N-terminal maltose-binding protein fusion protein in Escherichia coli strain BL21(DE3) Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics of recombinant CDO, overview Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ catalytically active ferrous enzyme, structure, overview Mus musculus
additional information concentration of FeIII-CDO is highly variable and often does not exceed 5% relative to the catalytically active ferrous enzyme, ferric enzyme is catalytically inactive Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-cysteine + O2 Mus musculus
-
 3-sulfinoalanine
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminal maltose-binding protein fusion enzyme from Escherichia coli strain BL21(DE3) by anion exchange and amylose affinity chromatography Mus musculus

Reaction

Reaction Comment Organism Reaction ID
L-cysteine + O2 = 3-sulfinoalanine reaction mechanism with internal electron transfer involving the ferric/ferrous enzyme forms, formation of a transient substrate-bound FeIII-superoxo species, overview Mus musculus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + O2
-
 Mus musculus 3-sulfinoalanine
-
 ?
additional information CDO exhibits high specificity for L-cysteine, displaying little or no reactivity with D-cysteine, glutathione, L-cystine, or cysteamine Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
CDO
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mus musculus

General Information

General Information Comment Organism
evolution the enzyme belongs to the 2-His-1-carboxylate family of non-heme iron containing oxidases and oxygenases Mus musculus
additional information the catalytic cycle of CDO can be primed by one electron through chemical oxidation to produce CDO with ferric iron in the active site. The C93-Y157 pair of mammalian CDO is catalytically essential. The monoanionic active site contains a 5- or 6-coordinate ferrous iron with solvent molecules serving as the non-protein ligands. In the absence of substrate and/or cofactor, the reduced active site is unreactive toward O2 Mus musculus
physiological function cysteine dioxygenase is a non-heme mononuclear iron enzyme that catalyzes the O2-dependent oxidation of L-cysteine to produce cysteine sulfinic acid Mus musculus