ArticleThe Biochemical journal2018
Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase.
Article in The Biochemical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Theoretical Evaluation of Sulfur-Based Reactions as a Model for Biological Antioxidant Defense.International journal of molecular sciences · 2022Article
- Effects of Environmental and Electric Perturbations on the pKa of Thioredoxin Cysteine 35: A Computational Study.Molecules (Basel, Switzerland) · 2022Article
- Structure and Electron-Transfer Pathway of the Human Methionine Sulfoxide Reductase MsrB3.Antioxidants & redox signaling · 2020Article
- The mammalian cytosolic thioredoxin reductase pathway acts via a membrane protein to reduce ER-localised proteins.Journal of cell science · 2020Article
- Methionine sulfoxide reductase B fromThe Journal of biological chemistry · 2020Article
- Reactive species and pathogen antioxidant networks during phagocytosis.The Journal of experimental medicine · 2019Review
- Drosophila methionine sulfoxide reductase A (MSRA) lacks methionine oxidase activity.Free radical biology & medicine · 2019Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
The oxidation of methionine residues in proteins occurs during oxidative stress and can lead to an alteration in protein function. The enzyme methionine sulfoxide reductase (Msr) reverses this modification. Here, we characterise the mammalian enzyme Msr B3. There are two splice variants of this enzyme that differ only in their N-terminal signal sequence, which directs the protein to either the endoplasmic reticulum (ER) or mitochondria. We demonstrate here that the enzyme can complement a bacterial strain, which is dependent on methionine sulfoxide reduction for growth, that the purified recombinant protein is enzymatically active showing stereospecificity towards
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