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Literature summary extracted from

  • Moskovitz, J.
    Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases (2005), Biochim. Biophys. Acta, 1703, 213-219.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.4.11 additional information MsrA expression and enzyme formation is induced in the stationary growth phase or on starvation for amino acids, glucose, or nitrogen Escherichia coli
1.8.4.11 additional information MsrA expression is induced by oxidizing diamide treatment and gamma-irradiation, the factor calcium-phosphate-binding protein CPBP, a homologue of elongation factor 1-gamma participates in transcription of gene msrA as part of a transcription regulation complex Saccharomyces cerevisiae
1.8.4.11 additional information oxacillin induces MsrA expression and enzyme formation Staphylococcus aureus
1.8.4.12 additional information expression of MsrB is induced by dehydration and H2O2 Arabidopsis thaliana
1.8.4.12 additional information MsrB expression is induced by heat shock and alkylating methyl-methanesulfonate treatment Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 additional information construction of a MsrA null mutant which exhibits a neurological disorder in the form of ataxia, is more sensitive to oxidative stress, and has by about 40% shorter life span than the wild-type mice at normal oxygen conditions and 10% at hyperoxic conditions Mus musculus
1.8.4.11 additional information H2O2 shortens the life span of cells in constructed null mutants Staphylococcus aureus
1.8.4.11 additional information H2O2 shortens the life span of cells in constructed null mutants Escherichia coli
1.8.4.11 additional information H2O2 shortens the life span of cells in constructed null mutants Saccharomyces cerevisiae
1.8.4.12 additional information H2O2 shortens the life span of cells in constructed null mutants Staphylococcus aureus
1.8.4.12 additional information H2O2 shortens the life span of cells in constructed null mutants Escherichia coli
1.8.4.12 additional information H2O2 shortens the life span of cells in constructed null mutants, the mutants show decreased MsrB activity with age compared to the wild-type enzyme Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.4.12 additional information selenium-adequate diet retains MsrB mRNA and protein expression at basal levels Mus musculus
1.8.4.12 additional information selenium-adequate diet retains MsrB mRNA and protein expression at basal levels Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Staphylococcus aureus MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Mus musculus MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Escherichia coli MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Homo sapiens MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Sus scrofa MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Saccharomyces cerevisiae MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Arabidopsis thaliana MsrA is specific for the S-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 additional information Arabidopsis thaliana recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins ?
-
?
1.8.4.11 additional information Homo sapiens recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.11 additional information Sus scrofa recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.11 additional information Mus musculus recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, MsrA can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells ?
-
?
1.8.4.11 additional information Staphylococcus aureus recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.11 additional information Escherichia coli recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.11 additional information Saccharomyces cerevisiae recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Staphylococcus aureus MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Mus musculus MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Escherichia coli MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Homo sapiens MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Sus scrofa MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Saccharomyces cerevisiae MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Arabidopsis thaliana MsrB is specific for the R-form L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 additional information Arabidopsis thaliana recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins ?
-
?
1.8.4.12 additional information Homo sapiens recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.12 additional information Sus scrofa recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.12 additional information Mus musculus recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells ?
-
?
1.8.4.12 additional information Staphylococcus aureus recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.12 additional information Escherichia coli recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview ?
-
?
1.8.4.12 additional information Saccharomyces cerevisiae recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Arabidopsis thaliana
-
-
-
1.8.4.11 Escherichia coli
-
-
-
1.8.4.11 Homo sapiens
-
-
-
1.8.4.11 Mus musculus
-
-
-
1.8.4.11 Saccharomyces cerevisiae
-
-
-
1.8.4.11 Staphylococcus aureus
-
-
-
1.8.4.11 Sus scrofa
-
-
-
1.8.4.12 Arabidopsis thaliana
-
-
-
1.8.4.12 Escherichia coli
-
-
-
1.8.4.12 Homo sapiens
-
-
-
1.8.4.12 Mus musculus
-
-
-
1.8.4.12 Saccharomyces cerevisiae
-
-
-
1.8.4.12 Staphylococcus aureus
-
-
-
1.8.4.12 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.4.11 brain
-
Mus musculus
-
1.8.4.11 brain
-
Homo sapiens
-
1.8.4.11 kidney
-
Mus musculus
-
1.8.4.11 liver
-
Mus musculus
-
1.8.4.11 lung
-
Mus musculus
-
1.8.4.12 brain
-
Mus musculus
-
1.8.4.12 brain
-
Homo sapiens
-
1.8.4.12 kidney
-
Mus musculus
-
1.8.4.12 liver
-
Mus musculus
-
1.8.4.12 lung
-
Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Staphylococcus aureus L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Mus musculus L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Sus scrofa L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form Arabidopsis thaliana L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins Arabidopsis thaliana ?
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview Homo sapiens ?
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview Sus scrofa ?
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, MsrA can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells Mus musculus ?
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview Staphylococcus aureus ?
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview Escherichia coli ?
-
?
1.8.4.11 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview Saccharomyces cerevisiae ?
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Staphylococcus aureus L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Mus musculus L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Sus scrofa L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form Arabidopsis thaliana L-methionine + thioredoxin disulfide + H2O
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins Arabidopsis thaliana ?
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview Homo sapiens ?
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview Sus scrofa ?
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells Mus musculus ?
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview Staphylococcus aureus ?
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview Escherichia coli ?
-
?
1.8.4.12 additional information recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview Saccharomyces cerevisiae ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 methionine sulfoxide reductase
-
Staphylococcus aureus
1.8.4.11 methionine sulfoxide reductase
-
Mus musculus
1.8.4.11 methionine sulfoxide reductase
-
Escherichia coli
1.8.4.11 methionine sulfoxide reductase
-
Homo sapiens
1.8.4.11 methionine sulfoxide reductase
-
Sus scrofa
1.8.4.11 methionine sulfoxide reductase
-
Saccharomyces cerevisiae
1.8.4.11 methionine sulfoxide reductase
-
Arabidopsis thaliana
1.8.4.11 MsrA
-
Staphylococcus aureus
1.8.4.11 MsrA
-
Mus musculus
1.8.4.11 MsrA
-
Escherichia coli
1.8.4.11 MsrA
-
Homo sapiens
1.8.4.11 MsrA
-
Sus scrofa
1.8.4.11 MsrA
-
Saccharomyces cerevisiae
1.8.4.11 MsrA
-
Arabidopsis thaliana
1.8.4.12 methionine sulfoxide reductase
-
Staphylococcus aureus
1.8.4.12 methionine sulfoxide reductase
-
Mus musculus
1.8.4.12 methionine sulfoxide reductase
-
Escherichia coli
1.8.4.12 methionine sulfoxide reductase
-
Homo sapiens
1.8.4.12 methionine sulfoxide reductase
-
Sus scrofa
1.8.4.12 methionine sulfoxide reductase
-
Saccharomyces cerevisiae
1.8.4.12 methionine sulfoxide reductase
-
Arabidopsis thaliana
1.8.4.12 MsrB
-
Staphylococcus aureus
1.8.4.12 MsrB
-
Mus musculus
1.8.4.12 MsrB
-
Escherichia coli
1.8.4.12 MsrB
-
Homo sapiens
1.8.4.12 MsrB
-
Sus scrofa
1.8.4.12 MsrB
-
Saccharomyces cerevisiae
1.8.4.12 MsrB
-
Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 thioredoxin
-
Staphylococcus aureus
1.8.4.11 thioredoxin
-
Mus musculus
1.8.4.11 thioredoxin
-
Escherichia coli
1.8.4.11 thioredoxin
-
Homo sapiens
1.8.4.11 thioredoxin
-
Sus scrofa
1.8.4.11 thioredoxin
-
Saccharomyces cerevisiae
1.8.4.11 thioredoxin
-
Arabidopsis thaliana
1.8.4.12 thioredoxin
-
Staphylococcus aureus
1.8.4.12 thioredoxin
-
Mus musculus
1.8.4.12 thioredoxin
-
Escherichia coli
1.8.4.12 thioredoxin
-
Homo sapiens
1.8.4.12 thioredoxin
-
Sus scrofa
1.8.4.12 thioredoxin
-
Saccharomyces cerevisiae
1.8.4.12 thioredoxin
-
Arabidopsis thaliana