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Literature summary for 1.8.4.11 extracted from

  • Kim, G.; Levine, R.L.
    A methionine residue promotes hyperoxidation of the catalytic cysteine of mouse methionine sulfoxide reductase A (2016), Biochemistry, 55, 3586-3593 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens
expression in Escherichia coli Mus musculus

Protein Variants

Protein Variants Comment Organism
M229L mutant is insensitive to hyperoxidation by H2O2 Mus musculus
M229V mutation to corresponding residue of human enzyme, which is not hyperoxidized by H2O2. Mutant is insensitive to hyperoxidation Mus musculus
V231M mutation to corresponding residue of mouse enzyme, which is hyperoxidized by H2O2. Mutant is sensitive to hyperoxidation Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
H2O2 in the mouse enzyme, the sulfenic acid formed at the catalytic Cys residue is vulnerable to irreversible oxidation to cysteine sulfinic acid resulting in inactivation. Hyperoxidation is controlled by the presence or absence of residue Met229 in the carboxyl terminal domain. Mouse msrA becomes insensitive to hyperoxidation when the Met229 is mutated. Hyperoxidation occurs so long as the methionine is located within the 14 carboxyl terminal residues. Met229 may form a stable, non-covalent bond with Trp74 at the active site, preventing formation of a protective sulfenylamide with Cys72 sulfenic acid Mus musculus
additional information contrary to the mouse enzmye, human MsrA is not sensitive to hyperoxidation by H2O2 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-
mitochondrion
-
Mus musculus 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UJ68
-
-
Mus musculus Q9D6Y7
-
-