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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics of recombinant CDO, overview | Mus musculus |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | Mus musculus | - |
3-sulfinoalanine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
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 | 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 |
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 | Comment | Organism |
---|---|---|
CDO | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Mus musculus |
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 |