| Literature DB >> 11169920 |
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.Entities:
Mesh:
Substances:
Year: 2000 PMID: 11169920 DOI: 10.1002/1097-0282(2000)55:4<288::AID-BIP1002>3.0.CO;2-M
Source DB: PubMed Journal: Biopolymers ISSN: 0006-3525 Impact factor: 2.505