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Peptide methionine sulfoxide reductase: Biochemistry and physiological role
Author(s) -
Brot Nathan,
Weissbach Herbert
Publication year - 2000
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)55:4<288::aid-bip1002>3.0.co;2-m
Subject(s) - chemistry , methionine sulfoxide reductase , biochemistry , sulfoxide , methionine sulfoxide , methionine , peptide , reductase , enzyme , amino acid , organic chemistry
The oxidation of methionine to methionine sulfoxide both in vivo and in vitro can lead to the loss of biological activity in a variety of proteins. This loss of activity can be reversed by an enzyme called methionine sulfoxide reductase. The gene for this enzyme has been cloned and sequenced from a variety of prokaryotic and eukaryotic cells, and the deduced amino acid sequence is very highly conserved. The mechanism of action of the bovine enzyme has been shown to involve a critical cysteine residue located at position 72 of the protein. In addition to its role as a “repair” enzyme, other evidence suggests that the enzyme may be involved in bacterial adherence and regulation of protein activity. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 55: 288–296, 2000