1.14.99.52: L-cysteinyl-L-histidinylsulfoxide synthase
This is an abbreviated version!
For detailed information about L-cysteinyl-L-histidinylsulfoxide synthase, go to the full flat file.
Reaction
Synonyms
5-histidylcysteine sulfoxide synthase, OvoA, OvoA-like protein, OvoAe, OvoAErwin, OvoAt, OvoA_1, OvoA_2, PlOvoA, short OvoA homologue, SpOvoA, sulfoxide synthase
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Reaction
Reaction on EC 1.14.99.52 - L-cysteinyl-L-histidinylsulfoxide synthase
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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
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
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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
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
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
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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
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-
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
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