The oxidation of methionine to methionine sulfoxide both in vivo and in vit
ro can lead to the loss of biological activity in a variety of proteins. Th
is loss of activity can be reversed by an enzyme called methionine sulfoxid
e reductase. The gene for this enzyme has been cloned and sequenced from a
variety of prokaryotic and eukaryotic cells, and the deduced amino acid seq
uence is very highly conserved. The mechanism of action of the bovine enzym
e 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 evi
dence suggests that the enzyme may be involved in bacterial adherence and r
egulation of protein activity. (C) 2001 John Wiley & Sons, Inc.