Sulfhydryl oxidase
From Proteopedia
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{{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 catalyzes the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O<sub>2</sub> to hydrogen peroxide<ref>PMID: | + | '''Sulfhydryl oxidase''' (SOX) is a flavin-dependent enzyme which catalyzes the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O<sub>2</sub> to hydrogen peroxide<ref>PMID:12176051</ref>. |
| - | *'''Erv1p''' is involved in the biogenesis of Fe/S clusters.<br /> | + | *'''Erv1p''' is involved in the biogenesis of Fe/S clusters<ref>PMID:10899311</ref>.<br /> |
| - | *'''ALR''' is a SOX augmenter of liver regeneration.<br /> | + | *'''ALR''' is a SOX augmenter of liver regeneration<ref>PMID:23186364</ref>.<br /> |
| - | *'''QSOX''' is a quiescin SOX. QSOX contains thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR. | + | *'''QSOX''' is a quiescin SOX. QSOX contains thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR<ref>PMID:18393449</ref>. |
==3D structures of sulfhydryl oxidase== | ==3D structures of sulfhydryl oxidase== | ||
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**[[3td7]] – SOX (mutant) – Acanthamoeba polyphaga minivirus | **[[3td7]] – SOX (mutant) – Acanthamoeba polyphaga minivirus | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:02, 4 September 2016
Sulfhydryl oxidase (SOX) is a flavin-dependent enzyme which catalyzes the formation of disulfide bonds from thiol groups. The reaction involves the reduction of O2 to hydrogen peroxide[1].
- Erv1p is involved in the biogenesis of Fe/S clusters[2].
- ALR is a SOX augmenter of liver regeneration[3].
- QSOX is a quiescin SOX. QSOX contains thioredoxin domain, helix-rich domain and FAD-binding domain Erv/ALR[4].
3D structures of sulfhydryl oxidase
Updated on 04-September-2016
References
- ↑ Thorpe C, Hoober KL, Raje S, Glynn NM, Burnside J, Turi GK, Coppock DL. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch Biochem Biophys. 2002 Sep 1;405(1):1-12. PMID:12176051
- ↑ Lee J, Hofhaus G, Lisowsky T. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 2000 Jul 14;477(1-2):62-6. PMID:10899311
- ↑ Sztolsztener ME, Brewinska A, Guiard B, Chacinska A. Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40. Traffic. 2013 Mar;14(3):309-20. doi: 10.1111/tra.12030. Epub 2012 Dec 16. PMID:23186364 doi:http://dx.doi.org/10.1111/tra.12030
- ↑ Heckler EJ, Alon A, Fass D, Thorpe C. Human quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesis. Biochemistry. 2008 Apr 29;47(17):4955-63. doi: 10.1021/bi702522q. Epub 2008 Apr, 5. PMID:18393449 doi:http://dx.doi.org/10.1021/bi702522q
