Methionine sulfoxide reductase A is a stereospecific methionine oxidase
Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide. The enzyme participates in defense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methionine. Beca...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 108; no. 26; pp. 10472 - 10477 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
National Academy of Sciences
28.06.2011
National Acad Sciences |
Subjects | |
Online Access | Get full text |
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Summary: | Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide. The enzyme participates in defense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methionine. Because oxidation of methionine residues is reversible, this covalent modification could also function as a mechanism for cellular regulation, provided there exists a stereospecific methionine oxidase. We show that MsrA itself is a stereospecific methionine oxidase, producing S-methionine sulfoxide as its product. MsrA catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins. When functioning as a reductase, MsrA fully reverses the oxidations which it catalyzes. |
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Bibliography: | http://dx.doi.org/10.1073/pnas.1101275108 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Edited by Irwin Fridovich, Duke University Medical Center, Durham, NC, and approved May 10, 2011 (received for review February 10, 2011) Author contributions: J.C.L., Z.Y., G.K., and R.L.L. designed research; J.C.L., Z.Y., G.K., and R.L.L. performed research; J.C.L., Z.Y., G.K., and R.L.L. analyzed data; and J.C.L. and R.L.L. wrote the paper. |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.1101275108 |