Biochemistry of methionine sulfoxide residues in proteins.
The oxidation of methionine to methionine sulfoxide constitutes one of the many post-translational modifications that proteins undergo. This non-enzymatic reaction has been shown to occur both in vivo and in vitro, and has been associated with the loss of biological activity in a wide variety of proteins and peptides. The presence of methionine sulfoxide residues in proteins is implicated in a variety of pathological conditions. An enzyme that is present in all organisms tested specifically catalyzes the reduction of the methionine sulfoxide residues in proteins. The physiological reductant for this enzyme appears to be thioredoxin.
Brot
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Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.
Weissbach
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D001426:Bacterial Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008715:Methionine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism
D001426:Bacterial Proteins; D011506:Proteins; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12; D008715:Methionine; C013111:methionine sulfoxide