Sulfhydryl oxidase
From Proteopedia
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| - | {{STRUCTURE_3p0k| PDB= | + | {{STRUCTURE_3p0k| PDB=3p0k | SIZE=400| SCENE= |right|CAPTION=Baculovirus sulfhydryl oxidase complex with acetate and imidazole, showing the FAD, [[3p0k]] }} |
'''Sulfhydryl oxidase''' (SOX) is a flavin-dependent enzyme which catalyze the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O2 to hydrogen peroxide. Erv1p SOX is involved in the biogenesis of Fe/S clusters. ALR is a SOX augmenter of liver regeneration. QSOX is a quiescin SOX. QSOX contain thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR. | '''Sulfhydryl oxidase''' (SOX) is a flavin-dependent enzyme which catalyze the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O2 to hydrogen peroxide. Erv1p SOX is involved in the biogenesis of Fe/S clusters. ALR is a SOX augmenter of liver regeneration. QSOX is a quiescin SOX. QSOX contain thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR. | ||
Revision as of 14:52, 4 January 2015
Sulfhydryl oxidase (SOX) is a flavin-dependent enzyme which catalyze the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O2 to hydrogen peroxide. Erv1p SOX is involved in the biogenesis of Fe/S clusters. ALR is a SOX augmenter of liver regeneration. QSOX is a quiescin SOX. QSOX contain thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR.
3D structures of sulfhydryl oxidase
Updated on 04-January-2015
