EC Number   |
Reaction |
Reference |
|---|
  1.14.99.52 | L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O |
- |
- |
| 1.14.99.52 | L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O |
catalytic mechanism: C-S bond formation is initiated by formation of a histidyl sp2 radical, formation of a histidyl PI-radical, and electrophilic attack of the iron-coordinated cysteine sulfoxide on histidine. The enzyme OvoA oxidizes cysteine to access an iron(IV)-oxo state (a in Figure 2) which then mediates oxidative sulfurization of histidine |
-, 734024 |
| 1.14.99.52 | L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O |
catalytic mechanism: C-S bond formation is initiated by formation of a histidyl sp2 radical, formation of a histidyl PI-radical, and electrophilic attack of the iron-coordinated cysteine sulfoxide on histidine. The enzyme OvoA oxidizes cysteine to access an iron(IV)-oxo state which then mediates oxidative sulfurization of histidine |
734024 |
| 1.14.99.52 | L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O |
the catalytic mechanism proceeds via radical intermediate, oxidation of histidine is thermodynamically most favorable for the formation of a HisNdelta(-H). radical via a proton-coupled electron transfer process, only the ferrous peroxysulfur complexes are sufficiently powerful enough oxidants to generate a histidyl-derived radical, not the superoxo-complexes |
-, 733972 |
| 1.14.99.52 | L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O |
the enzyme catalysis follows an thiol-ene type mechanism, it catalyzes C-S bond formation through an OvoA generated L-cysteine thiyl radical that attacks the unsaturated imidazole ring of L-histidine, overview |
-, 733647 |
