Sulfhydryl oxidase
From Proteopedia
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| - | {{STRUCTURE_2hj3| PDB=2hj3 | SIZE=400| SCENE= |right|CAPTION=Sulfhydryl oxidase, [[2hj3]] }} | + | {{STRUCTURE_2hj3| PDB=2hj3 | SIZE=400| SCENE= |right|CAPTION=Sulfhydryl oxidase complex with sulfate, showing the FAD, [[2hj3]] }} |
'''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 19:27, 18 October 2011
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
Erv2p
1jr8, 1jra – ySOX protease-resistant domain – yeast
Erv1p
2hj3 – SOX – Arabidopsis thaliana
ASFV
3gwl – SOX residues 1-103 – African swine fever virus
QSOX1
3lli, 3llk – hSOX-1 residues 286-546 – human
ALR
3mbg – hALR residues 81-205
