Oxidative Protein Folding and the Quiescin–Sulfhydryl Oxidase Family of Flavoproteins
- 15 October 2010
- journal article
- review article
- Published by Mary Ann Liebert Inc in Antioxidants and Redox Signaling
- Vol. 13 (8), 1217-1230
- https://doi.org/10.1089/ars.2010.3098
Abstract
Flavin-linked sulfhydryl oxidases participate in the net generation of disulfide bonds during oxidative protein folding in the endoplasmic reticulum. Members of the Quiescin-sulfhydryl oxidase (QSOX) family catalyze the facile direct introduction of disulfide bonds into unfolded reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Current progress in dissecting the mechanism of QSOX enzymes is reviewed, with emphasis on the CxxC motifs in the thioredoxin and Erv/ALR domains and the involvement of the flavin prosthetic group. The tissue distribution and intra- and extracellular location of QSOX enzymes are discussed, and suggestions for the physiological role of these enzymes are presented. The review compares the substrate specificity and catalytic efficiency of the QSOX enzymes with members of the Ero1 family of flavin-dependent sulfhydryl oxidases: enzymes believed to play key roles in disulfide generation in yeast and higher eukaryotes. Finally, limitations of our current understanding of disulfide generation in metazoans are identified and questions posed for the future. Antioxid. Redox Signal. 13, 1217–1230.Keywords
This publication has 112 references indexed in Scilit:
- Arsenic(III) Species Inhibit Oxidative Protein Folding in VitroBiochemistry, 2008
- Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidationThe EMBO Journal, 2008
- Oxidative Protein Folding in Vitro: A Study of the Cooperation between Quiescin-Sulfhydryl Oxidase and Protein Disulfide IsomeraseBiochemistry, 2008
- A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cellsThe EMBO Journal, 2008
- Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formationProceedings of the National Academy of Sciences of the United States of America, 2008
- Generating disulfides with the Quiescin-sulfhydryl oxidasesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2008
- Human Quiescin-Sulfhydryl Oxidase, QSOX1: Probing Internal Redox Steps by MutagenesisBiochemistry, 2008
- A Flavin-Dependent Sulfhydryl Oxidase in Bovine MilkBiochemistry, 2007
- Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1Biochemical Journal, 2007
- An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative StressMolecular Cell, 2003