Cloned (Comment) | Organism |
---|---|
gene cdoA, recombinant enzyme expression in Escherichia coli strain BL21(DE3), subcloning in Escherichia cli strain DH5alpha | Bacillus subtilis |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme free or with bound substrate L-Cys, hanging drop vapour diffusion method, mixing of 0.004 ml of 10 mg/ml protein solution with 0.004 ml of reservoir solution containing 18% w/v PEG 4000, 0.1 M potassium acetate, 0.05 M 2-(N-morpholino)ethanesulfonic acid, pH 6.0, 25°C, 2-7 days, X-ray diffraction structure determination and analysis at 2.38-2.82 A resolution | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | a catalytic a non-heme iron is coordinated by three conserved residues His75, His77, and His125 | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | Bacillus subtilis | - |
3-sulfinoalanine | - |
? | |
L-cysteine + O2 | Bacillus subtilis 168 | - |
3-sulfinoalanine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O32085 | - |
- |
Bacillus subtilis 168 | O32085 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3) | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-cysteine + O2 = 3-sulfinoalanine | reaction mechanism and structure-function analysis | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | - |
Bacillus subtilis | 3-sulfinoalanine | - |
? | |
L-cysteine + O2 | - |
Bacillus subtilis 168 | 3-sulfinoalanine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Arg-type CDO | - |
Bacillus subtilis |
BsCDO | - |
Bacillus subtilis |
CDO | - |
Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
evolution | analysis of examples for two structural genomics groups of CDOs: a Bacillus subtilis Arg-type enzyme that has cysteine dioxygenase activity (BsCDO), and a Ralstonia eutropha Gln-type CDO homologue of uncharacterized activity (ReCDOhom), overview. The BsCDO active site is well conserved with mammalian CDO, and a cysteine complex captured in the active site confirms that the cysteine binding mode is also similar. The Arg position is not compatible with the mode of Cys binding seen in both Rattus norvegicus CDO and Bacillus subtilis CDO. Gln-type CDO homologues are not authentic CDOs but have substrate specificity more similar to 3-mercaptopropionate dioxygenases | Bacillus subtilis |
additional information | the BsCDO active site has a non-heme iron coordinated by three conserved residues His75, His77, and His125. Ser137, His139, andTyr141 form the catalytic triad. The bound L-Cys coordinates the iron in a bidentate fashion via its Sgamma and N atoms. Structure comparisons, overview | Bacillus subtilis |