Peptide methionine sulfoxide reductase: Biochemistry and physiological role
- 1 January 2000
- journal article
- review article
- Published by Wiley in Biopolymers
- Vol. 55 (4) , 288-296
- https://doi.org/10.1002/1097-0282(2000)55:4<288::aid-bip1002>3.0.co;2-m
Abstract
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, 2000Keywords
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