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Oxidation of Methionine in Proteins: Roles in Antioxidant Defense and Cellular Regulation
- Source :
- IUBMB Life. 50:301-307
- Publication Year :
- 2000
- Publisher :
- Informa UK Limited, 2000.
-
Abstract
- The roles of methionine residues in proteins have not been well defined, but a review of available studies leads to the conclusion that methionine, like cysteine, functions as an antioxidant and as a key component of a system for regulation of cellular metabolism. Methionine is readily oxidized to methionine sulfoxide by many reactive species. The oxidation of surface exposed methionines thus serves to protect other functionally essential residues from oxidative damage. Methionine sulfoxide reductases have the potential to reduce the residue back to methionine, increasing the scavenging efficiency of the system. Reversible covalent modification of amino acids in proteins provides the mechanistic basis for most systems of cellular regulation. Interconversion of methionine and methionine sulfoxide can function to regulate the biological activity of proteins, through alteration in catalytic efficiency and through modulation of the surface hydrophobicity of the protein.
- Subjects :
- Antioxidant
Cells
medicine.medical_treatment
Clinical Biochemistry
Biochemistry
Antioxidants
chemistry.chemical_compound
Methionine
Ubiquitin
medicine
Genetics
Animals
Humans
Molecular Biology
chemistry.chemical_classification
biology
Methionine sulfoxide
Proteins
Sulfoxide
Cell Biology
Amino acid
chemistry
Methionine Sulfoxide Reductases
biology.protein
Methionine sulfoxide reductase
Oxidoreductases
Oxidation-Reduction
Cysteine
Subjects
Details
- ISSN :
- 15216551 and 15216543
- Volume :
- 50
- Database :
- OpenAIRE
- Journal :
- IUBMB Life
- Accession number :
- edsair.doi.dedup.....873920d8a1e7c895ee70ef984af8dc02