Sulfhydryl oxidase: Difference between revisions

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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]] }}
<StructureSection load='3p0k' size='350' side='right' scene='' 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:8528769</ref>. 


*'''Erv1p''' is involved in the biogenesis of Fe/S clusters.<br />
'''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>.   
*'''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==
*'''Erv1p''' is involved in the biogenesis of Fe/S clusters<ref>PMID:10899311</ref>.<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<ref>PMID:18393449</ref>.


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
*<scene name='46/468158/Cv/3'>FAD binding site</scene> in Baculovirus sulfhydryl oxidase ([[3p0k]]). Water molecules are shown as red spheres.
{{#tree:id=OrganizedByTopic|openlevels=0|


*Sulfhydryl oxidase Erv2p
==3D structures of sulfhydryl oxidase==
 
[[Sulfhydryl oxidase 3D structures]]
**[[1jr8]], [[1jra]] – ySOX  protease-resistant domain – yeast
 
*Sulfhydryl oxidase Erv1
 
**[[4e0h]], [[3w4y]] – ySOX FAD-binding domain<br />
**[[4e0i]] – ySOX FAD-binding domain (mutant)
 
*Sulfhydryl oxidase Erv1p
 
**[[2hj3]] – SOX – ''Arabidopsis thaliana''
 
*Sulfhydryl oxidase Erv
 
**[[3p0k]], [[3qzy]] – SOX – Autographa californica nucleopolyhedrovirus
 
*Sulfhydryl oxidase ASFV
 
**[[3gwl]] – SOX residues 1-103 – African swine fever virus
 
*Sulfhydryl oxidase QSOX1
 
**[[3lli]], [[3llk]] – hSOX-1 residues 286-546 – human<br />
**[[3q6o]] - hSOX-1 residues 33-272<br />
**[[4ij3]] - hSOX-1 residues 33-272 + antibody<br />
**[[3t58]], [[3t59]] - mSOX-1 residues 36-550 (mutant) - mouse<br />
**[[4p2l]] - rSOX-1 residues 27-544 - rat<br />
 
*Sulfhydryl oxidase ALR
 
**[[3mbg]], [[3tk0]] – hALR oxidase domain<br />
**[[3u2l]], [[3u2m]], [[3u5s]], [[4ldk]] – hALR oxidase domain (mutant)<br />
**[[3r7c]] - rALR


*FAD-linked sulfhydryl oxidase
</StructureSection>


**[[3td7]] – SOX (mutant) – Acanthamoeba polyphaga minivirus
== References ==
}}
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:56, 11 February 2020


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


Baculovirus sulfhydryl oxidase complex with acetate and imidazole, showing the FAD, 3p0k

Drag the structure with the mouse to rotate

ReferencesReferences

  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

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