Abstract
Background: Dual oxidases (DUOXs) are membrane-bound ROS-generating enzymes. Results: Conserved DUOX cysteines localized in an N-terminal domain contribute to enzymatic maturation, independent of structural stabilization. Conclusion: Intermolecular disulfides support the interaction between DUOX enzymes and their maturation factors. Significance: This study reflects a complex profile of protein interactions required for activity and localization of the DUOX enzymes. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Meitzler, J. L., Hinde, S., Bánfi, B., Nauseef, W. M., & De Montellano, P. R. O. (2013). Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) Proteins. Journal of Biological Chemistry, 288(10), 7147–7157. https://doi.org/10.1074/jbc.M112.414797
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