Sulfhydryl oxidase: Difference between revisions
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Michal Harel (talk | contribs) New page: '''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 perox... |
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{{STRUCTURE_2hj3| PDB=2hj3 | SIZE=400| SCENE= |right|CAPTION=Sulfhydryl oxidase, [[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. | ||
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==3D structures of sulfhydryl oxidase== | ==3D structures of sulfhydryl oxidase== | ||
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[[3mbg]] – hALR residues 81-205 | [[3mbg]] – hALR residues 81-205 | ||
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Revision as of 22:26, 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 oxidase3D structures of sulfhydryl oxidase
Erv2pErv2p
1jr8, 1jra – ySOX protease-resistant domain – yeast
Erv1pErv1p
2hj3 – SOX – Arabidopsis thaliana
ASFVASFV
3gwl – SOX residues 1-103 – African swine fever virus
QSOX1QSOX1
3lli, 3llk – hSOX-1 residues 286-546 – human
ALRALR
3mbg – hALR residues 81-205