ArticleBiochemistry2012
Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Non-enzymatic function of QSOX2 directly regulates the JUNB-ITGB4 axis and enhanced resistance to osimertinib in EGFR-mutation lung adenocarcinoma.Cell death discovery · 2026Article
- Quiescin Sulfhydryl Oxidase 2 Overexpression Predicts Poor Prognosis and Tumor Progression in Patients With Colorectal Cancer: A Study Based on Data Mining and Clinical Verification.Frontiers in cell and developmental biology · 2021Article
- Golgi pH, Ion and Redox Homeostasis: How Much Do They Really Matter?Frontiers in cell and developmental biology · 2019Article
- Gaussia princeps luciferase: a bioluminescent substrate for oxidative protein folding.Protein science : a publication of the Protein Society · 2018Article
- Fast, irreversible modification of cysteines through strain releasing conjugate additions of cyclopropenyl ketones.Organic & biomolecular chemistry · 2018Article
- Designing Flavoprotein-GFP Fusion Probes for Analyte-Specific Ratiometric Fluorescence Imaging.Biochemistry · 2018Article
- Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.Chemical reviews · 2018Review
- Article
- Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.Annual review of chemical and biomolecular engineering · 2016Review
- Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.Free radical biology & medicine · 2015Review
- Disulfide bond generation in mammalian blood serum: detection and purification of quiescin-sulfhydryl oxidase.Free radical biology & medicine · 2014Article
- Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase.The Journal of biological chemistry · 2014Article
- Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst.The Biochemical journal · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
This work explores the substrate specificity of the quiescin sulfhydryl oxidase (QSOX) family of disulfide-generating flavoenzymes to provide enzymological context for investigation of the physiological roles of these facile catalysts of oxidative protein folding. QSOX enzymes are generally unable to form disulfide bonds within well-structured proteins. Use of a temperature-sensitive mutant of ubiquitin-conjugating enzyme 4 (Ubc4') as a model substrate shows that QSOX activity correlates with the unfolding of Ubc4' monitored by circular dichroism. Fusion of Ubc4' with the more stable glutathione-S-transferase domain demonstrates that QSOX can selectively introduce disulfides into the less stable domain of the fusion protein. In terms of intermolecular disulfide bond generation, QSOX is unable to cross-link well-folded globular proteins via their surface thiols. However, the construction of a septuple mutant of RNase A, retaining a single cysteine residue, demonstrates that flexible protein monomers can be directly coupled by the oxidase. Steady- and pre-steady-state kinetic experiments, combined with static fluorescence approaches, indicate that while QSOX is an efficient catalyst for disulfide bond formation between mobile elements of structure, it does not appear to have a significant binding site for unfolded proteins. These aspects of protein substrate discrimination by QSOX family members are rationalized in terms of the stringent steric requirements for disulfide exchange reactions.
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