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Literature summary extracted from

  • Moskovitz, J.
    Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival (2005), Curr. Pharm. Des., 11, 1451-1457.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.4.11 additional information the calcium phospholipid-binding protein, CPBP, is an analogue of the elongation factor 1-gamma and regulates MsrA expression by binding to the MsrA promoter, starvation induces MsrA expression, also diamide treatment and gamma-irradiation induce the enzyme Saccharomyces cerevisiae
1.8.4.11 additional information starvation induces the expression of MsrA Escherichia coli
1.8.4.11 additional information the antibiotic oxacillin induces MsrA expression Staphylococcus aureus
1.8.4.11 additional information chronic dietary intake of soybean protein induces the expression of MsrA Sus scrofa
1.8.4.12 additional information starvation induces MsrB expression, also heat treatment and methylmethanesulfonate induce the enzyme Saccharomyces cerevisiae
1.8.4.12 additional information heat shock, dehydration, and reactive oxygen species like H2O2 induce the expression of MsrB Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 additional information yeast cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(S)-S-oxide accumulation Saccharomyces cerevisiae
1.8.4.11 additional information msrA gene disruption leads to a shortened life span both under normoxic and hyperoxic conditions, MsrA null mutant mice shows greater sensitivity to hyperoxic conditions compared to wild-type mice, construction of MsrA overexpressing strains, phenotypes, overview Mus musculus
1.8.4.11 additional information bacterial cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(R)-S-oxide accumulation Escherichia coli
1.8.4.11 additional information bacterial cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(R)-S-oxide accumulation Staphylococcus aureus
1.8.4.12 additional information yeast cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation Saccharomyces cerevisiae
1.8.4.12 additional information construction of MsrB null mutant and of overexpressing strains, phenotypes, overview Mus musculus
1.8.4.12 additional information cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.12 cytosol isozyme MsrB1 Homo sapiens 5829
-
1.8.4.12 cytosol isozyme MsrB1 Mus musculus 5829
-
1.8.4.12 endoplasmic reticulum isozyme MsrB3 Homo sapiens 5783
-
1.8.4.12 endoplasmic reticulum isozyme MsrB3 Mus musculus 5783
-
1.8.4.12 intracellular
-
 Saccharomyces cerevisiae 5622
-
1.8.4.12 intracellular
-
 Arabidopsis thaliana 5622
-
1.8.4.12 mitochondrion isozymes MsrB2 and MsrB3 Homo sapiens 5739
-
1.8.4.12 mitochondrion isozymes MsrB2 and MsrB3 Mus musculus 5739
-
1.8.4.12 additional information subcellular targeting is determined by alternative splicing Homo sapiens
-
-
1.8.4.12 additional information subcellular targeting is determined by alternative splicing Mus musculus
-
-
1.8.4.12 nucleus isozyme MsrB1 Homo sapiens 5634
-
1.8.4.12 nucleus isozyme MsrB1 Mus musculus 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.12 additional information the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB Arabidopsis thaliana
1.8.4.12 additional information the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB Homo sapiens
1.8.4.12 additional information the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB Mus musculus
1.8.4.12 additional information the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB Saccharomyces cerevisiae

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)-S-oxide + thioredoxin Saccharomyces cerevisiae
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin Homo sapiens substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin Mus musculus
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin Escherichia coli
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin Staphylococcus aureus
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin Arabidopsis thaliana
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin Sus scrofa
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 additional information Saccharomyces cerevisiae roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway ?
-
 ?
1.8.4.11 additional information Homo sapiens roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.11 additional information Mus musculus roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.11 additional information Escherichia coli roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.11 additional information Staphylococcus aureus roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.11 additional information Arabidopsis thaliana roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.11 additional information Sus scrofa roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Saccharomyces cerevisiae
-
 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Homo sapiens
-
 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Mus musculus
-
 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Escherichia coli
-
 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Staphylococcus aureus
-
 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Arabidopsis thaliana substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin Sus scrofa
-
 peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin Saccharomyces cerevisiae
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin Homo sapiens substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin Mus musculus
-
 L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin Arabidopsis thaliana substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 additional information Saccharomyces cerevisiae roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, regulation of MsrB expression, overview ?
-
 ?
1.8.4.12 additional information Homo sapiens roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.12 additional information Mus musculus roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview ?
-
 ?
1.8.4.12 additional information Arabidopsis thaliana roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, 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
-
 isozymes MsrB1-3
-
1.8.4.12 Homo sapiens
-
 isozymes MsrB1-3
-
1.8.4.12 Mus musculus
-
 isozymes MsrB1-3
-
1.8.4.12 Saccharomyces cerevisiae
-
 isozymes MsrB1-3
-

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Staphylococcus aureus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Arabidopsis thaliana L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Sus scrofa L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Staphylococcus aureus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Arabidopsis thaliana L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Sus scrofa L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway Saccharomyces cerevisiae ?
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Homo sapiens ?
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Mus musculus ?
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Escherichia coli ?
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Staphylococcus aureus ?
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Arabidopsis thaliana ?
-
 ?
1.8.4.11 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Sus scrofa ?
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Saccharomyces cerevisiae peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Homo sapiens peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Mus musculus peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Escherichia coli peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Staphylococcus aureus peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation Arabidopsis thaliana peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Sus scrofa peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin stereospecific reduction Arabidopsis thaliana peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin
-
 Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin
-
 Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation Arabidopsis thaliana L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin stereospecific reduction Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin stereospecific reduction Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin stereospecific reduction Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine-(R)-S-oxide + thioredoxin stereospecific reduction Arabidopsis thaliana L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, regulation of MsrB expression, overview Saccharomyces cerevisiae ?
-
 ?
1.8.4.12 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Homo sapiens ?
-
 ?
1.8.4.12 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview Mus musculus ?
-
 ?
1.8.4.12 additional information roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview Arabidopsis thaliana ?
-
 ?
1.8.4.12 additional information the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO Saccharomyces cerevisiae ?
-
 ?
1.8.4.12 additional information the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO Homo sapiens ?
-
 ?
1.8.4.12 additional information the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO Mus musculus ?
-
 ?
1.8.4.12 additional information the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO Arabidopsis thaliana ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 methionine sulfoxide reductase A
-
 Saccharomyces cerevisiae
1.8.4.11 methionine sulfoxide reductase A
-
 Homo sapiens
1.8.4.11 methionine sulfoxide reductase A
-
 Mus musculus
1.8.4.11 methionine sulfoxide reductase A
-
 Escherichia coli
1.8.4.11 methionine sulfoxide reductase A
-
 Staphylococcus aureus
1.8.4.11 methionine sulfoxide reductase A
-
 Arabidopsis thaliana
1.8.4.11 methionine sulfoxide reductase A
-
 Sus scrofa
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Saccharomyces cerevisiae
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Homo sapiens
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Mus musculus
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Escherichia coli
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Staphylococcus aureus
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Arabidopsis thaliana
1.8.4.11 additional information the enzyme belongs to the Msr family of enzymes Sus scrofa
1.8.4.11 MsrA
-
 Saccharomyces cerevisiae
1.8.4.11 MsrA
-
 Homo sapiens
1.8.4.11 MsrA
-
 Mus musculus
1.8.4.11 MsrA
-
 Escherichia coli
1.8.4.11 MsrA
-
 Staphylococcus aureus
1.8.4.11 MsrA
-
 Arabidopsis thaliana
1.8.4.11 MsrA
-
 Sus scrofa
1.8.4.12 methionine sulfoxide reductase B
-
 Saccharomyces cerevisiae
1.8.4.12 methionine sulfoxide reductase B
-
 Homo sapiens
1.8.4.12 methionine sulfoxide reductase B
-
 Mus musculus
1.8.4.12 methionine sulfoxide reductase B
-
 Arabidopsis thaliana
1.8.4.12 additional information the enzyme belongs to the Msr family of enzymes Saccharomyces cerevisiae
1.8.4.12 additional information the enzyme belongs to the Msr family of enzymes Homo sapiens
1.8.4.12 additional information the enzyme belongs to the Msr family of enzymes Mus musculus
1.8.4.12 additional information the enzyme belongs to the Msr family of enzymes Arabidopsis thaliana
1.8.4.12 MsrB
-
 Saccharomyces cerevisiae
1.8.4.12 MsrB
-
 Homo sapiens
1.8.4.12 MsrB
-
 Mus musculus
1.8.4.12 MsrB
-
 Arabidopsis thaliana

Cofactor

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