Sulfhydryl oxidase

From Proteopedia

spinqualitylabelsall models Baculovirus sulfhydryl oxidase complex with acetate and imidazole, showing the FAD, 3p0k Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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]. in Baculovirus sulfhydryl oxidase (3p0k). Water molecules are shown as red spheres. 3D structures of sulfhydryl oxidase Sulfhydryl oxidase 3D structures

References

1. ↑ 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
2. ↑ 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
3. ↑ 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
4. ↑ 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