Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | nonheme iron enzyme | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | Rattus norvegicus | - |
3-sulfinoalanine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P21816 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-cysteine + O2 = 3-sulfinoalanine | catalytic mechanism of cysteine dioxygenase compared to the mechanism of sulfoxide synthase EgtB, EC 1.14.99.50, and its function of the active-site Tyr377 residue. In the sulfoxide syntase reaction, the conserved tyrosine residue reacts via proton-coupled electron transfer with the iron(III)-superoxo species and creates an iron(III)-hydroperoxo intermediate, thereby preventing the possible thiolate dioxygenation side reaction, detailed overview | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | - |
Rattus norvegicus | 3-sulfinoalanine | - |
? |
General Information | Comment | Organism |
---|---|---|
evolution | structure and catalytic mechanism comparisons of nonheme iron enzymes cysteine dioxygenase with sulfoxide synthase EgtB, EC 1.14.99.50, quantum mechanics/molecular mechanics calculations, overview | Rattus norvegicus |
additional information | the CDO enzyme active site structure comprises residues Tyr58, Arg60, His86, His88, Cys93, His140, and Tyr157, structure model | Rattus norvegicus |