Methionine (Met) can be oxidized to methionine sulfoxide (MetO), which exist as R-and S-
diastereomers. Present in all three domains of life, methionine sulfoxide reductases (MSR) …

Methionine residues in proteins are susceptible to oxidation by reactive oxygen species, but
can be repaired via reduction of the resulting methionine sulfoxides by methionine-S …

Msrs (methionine sulfoxide reductases), MsrA and MsrB, are repair enzymes that reduce
methionine sulfoxide residues in oxidatively damaged proteins to methionine residues in a …

Significance: Selenium is utilized in the methionine sulfoxide reduction system that occurs in
most organisms. Methionine sulfoxide reductases (Msrs), MsrA and MsrB, are the enzymes …

Selenocysteine (Sec) is found in active sites of several oxidoreductases in which this
residue is essential for catalytic activity. However, many selenoproteins have fully functional …

One of the most oxidation-sensitive amino acids is methionine. Oxidation of methionine to
methionine sulfoxide (MetO) could, on the one hand, be an important component of signal …

The mammalian methionine sulfoxide reductase B (MsrB) has been found to be a
selenoprotein which can reduce R form of both free and protein-incorporated methionine …

Protein oxidation has been linked to accelerated aging and is a contributing factor to many
diseases. Methionine residues are particularly susceptible to oxidation, but the resulting …

Abstract l‐methionine (l‐Met) is the only sulphur‐containing proteinogenic amino acid
together with cysteine. Its importance is highlighted by it being the initiator amino acid for …

Methionine residues are susceptible to oxidation, but this damage may be reversed by
methionine sulfoxide reductases MsrA and MsrB. Mammals contain one MsrA and three …