Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | non-heme iron enzyme. The enzyme contains an iron active site with an unusual 3-His ligation to the protein, which contrasts with the structural features of common nonheme iron dioxygenases | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | Homo sapiens | - |
3-sulfinoalanine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q16878 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-cysteine + O2 = 3-sulfinoalanine | reaction mechanism of cysteine oxygenation by CDO enzymes and reactivity of [TpMe,PhFe(CysOEt)] towards O2, detailed quantum mechanics/molecular mechanics calculations, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine + O2 | - |
Homo sapiens | 3-sulfinoalanine | - |
? | |
L-cysteine + O2 | structure of the sulfinato complex, overview | Homo sapiens | 3-sulfinoalanine | - |
? | |
additional information | prediction of a h2-O,O-binding mode for synthetic as well as the natural enzyme, modeling of the cysteine sulfinic product complex in the active site | Homo sapiens | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
additional information | structure and mechanism leading to formation of the cysteine sulfinate product complex of a biomimetic cysteine dioxygenase model, i.e. trispyrazolylborato iron(II) cysteinato complex, overview. The enzyme contains an iron active site with an unusual 3-His ligation to the protein, which contrasts with the structural features of common non-heme iron dioxygenases | Homo sapiens |
physiological function | the enzyme is involved in the metabolism of L-cysteine in the body | Homo sapiens |