peptide-methionine (R)-S-oxide reductase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: peptide-L-methionine + H2O + thioredoxin disulfide = peptide-L-methionine (R)-S-oxide + thioredoxin. Can act on oxidized methionine in peptide linkage with specificity for the R enantiomer. Thioredoxin disulfide is the oxidized form of thioredoxin. [EC:1.8.4.12, GOC:mah, GOC:vw, RHEA:24164]

Peptide-methionine (R)-S-oxide reductase activity is an enzyme activity that catalyzes the reduction of methionine (R)-S-oxide to methionine. This reduction is important for the repair of methionine sulfoxide residues, which can occur in proteins due to oxidative stress. Methionine sulfoxide residues are formed by the oxidation of methionine residues, and they can disrupt the structure and function of proteins. Peptide-methionine (R)-S-oxide reductase activity helps to restore the function of proteins by reducing these methionine sulfoxide residues back to methionine.

This enzyme activity is often found in bacteria, archaea, and eukaryotes. In humans, it is thought to play a role in protecting cells from oxidative damage and in maintaining protein homeostasis. Peptide-methionine (R)-S-oxide reductase activity is also important for the repair of damaged DNA and RNA.

The mechanism of peptide-methionine (R)-S-oxide reductase activity involves the use of a reducing agent, such as NADH or NADPH, to donate electrons to the methionine sulfoxide residue. This electron transfer reduces the methionine sulfoxide residue back to methionine. The specific mechanism of action may vary depending on the enzyme involved.

Peptide-methionine (R)-S-oxide reductase activity is an important enzyme activity that plays a role in a variety of cellular processes. By reducing methionine sulfoxide residues, this enzyme activity helps to protect cells from oxidative damage, maintain protein homeostasis, and repair damaged DNA and RNA.'
"

Proteins (1)

Compounds (1)