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| Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation |
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| Author(s): Levine RL, Moskovitz J, Stadtman ER |
| Source: IUBMB LIFE Volume: 50 Issue: 4-5 Pages: 301-307 Published: OCT-NOV 2000 |
| Times Cited: 106 References: 98 |
| 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. |
| Document Type: Review |
| Language: English |
| Reprint Address: Levine, RL (reprint author), NHLBI, Biochem Lab, NIH, Bldg 3,Room 106,MSC 0320, Bethesda, MD 20892 USA |
Addresses:
1. NHLBI, Biochem Lab, NIH, Bethesda, MD 20892 USA |
| Publisher: TAYLOR & FRANCIS INC, 325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USA |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: 420JQ |
| ISSN: 1521-6543 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |