Sulfhydryl oxidase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
{{STRUCTURE_3p0k| PDB=3p0k | SIZE=400| SCENE= |right|CAPTION=Baculovirus sulfhydryl oxidase complex with acetate and imidazole, showing the FAD, [[3p0k]] }} | {{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 | + | '''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''' is involved in the biogenesis of Fe/S clusters.<br /> | ||
| + | *'''ALR''' is a SOX augmenter of liver regeneration.<br /> | ||
| + | *'''QSOX''' is a quiescin SOX. QSOX contains thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR. | ||
==3D structures of sulfhydryl oxidase== | ==3D structures of sulfhydryl oxidase== | ||
Revision as of 09:55, 4 September 2016
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 is involved in the biogenesis of Fe/S clusters.
- ALR is a SOX augmenter of liver regeneration.
- QSOX is a quiescin SOX. QSOX contains thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR.
3D structures of sulfhydryl oxidase
Updated on 04-September-2016
