EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.11 | additional information | chronic dietary intake of soybean protein induces the expression of MsrA | Sus scrofa | |
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 | 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 | |
1.8.4.12 | additional information | heat shock, dehydration, and reactive oxygen species like H2O2 induce the expression of MsrB | Arabidopsis thaliana | |
1.8.4.12 | additional information | starvation induces MsrB expression, also heat treatment and methylmethanesulfonate induce the enzyme | Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
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 |
1.8.4.11 | 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 | 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 | yeast cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(S)-S-oxide accumulation | Saccharomyces cerevisiae |
1.8.4.12 | additional information | cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation | Arabidopsis thaliana |
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 | yeast cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation | Saccharomyces cerevisiae |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.8.4.12 | cytosol | isozyme MsrB1 | Mus musculus | 5829 | - |
1.8.4.12 | cytosol | isozyme MsrB1 | Homo sapiens | 5829 | - |
1.8.4.12 | endoplasmic reticulum | isozyme MsrB3 | Mus musculus | 5783 | - |
1.8.4.12 | endoplasmic reticulum | isozyme MsrB3 | Homo sapiens | 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 | Mus musculus | 5739 | - |
1.8.4.12 | mitochondrion | isozymes MsrB2 and MsrB3 | Homo sapiens | 5739 | - |
1.8.4.12 | additional information | subcellular targeting is determined by alternative splicing | Mus musculus | - |
- |
1.8.4.12 | additional information | subcellular targeting is determined by alternative splicing | Homo sapiens | - |
- |
1.8.4.12 | nucleus | isozyme MsrB1 | Mus musculus | 5634 | - |
1.8.4.12 | nucleus | isozyme MsrB1 | Homo sapiens | 5634 | - |
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 | Mus musculus | |
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 | Saccharomyces cerevisiae | |
1.8.4.12 | additional information | the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB | Arabidopsis thaliana |
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 | Staphylococcus aureus | - |
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 | Sus scrofa | - |
L-methionine + thioredoxin disulfide + H2O | - |
? | |
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 | Arabidopsis thaliana | - |
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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | Homo sapiens | - |
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 | Saccharomyces cerevisiae | - |
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 | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | Mus musculus | - |
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 | 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 | 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 | 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 | ? | - |
? | |
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 | 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 | ? | - |
? |
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 | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.8.4.11 | brain | - |
Mus musculus | - |
1.8.4.12 | brain | - |
Mus musculus | - |
1.8.4.12 | brain | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
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 | - |
Sus scrofa | L-methionine + thioredoxin disulfide + H2O | - |
? | |
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 | - |
Arabidopsis thaliana | 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 | 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 | Homo sapiens | 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 | 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 | Arabidopsis thaliana | 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 | 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 | 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 | 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 | 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 | 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 | Arabidopsis thaliana | ? | - |
? | |
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 | - |
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 | - |
Homo sapiens | 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 | - |
Saccharomyces cerevisiae | 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 | - |
? | |
1.8.4.11 | 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 | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | - |
Mus musculus | 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 | stereospecific reduction | Mus musculus | 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 | Saccharomyces cerevisiae | 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 | 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 | 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 | 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 | 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, 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 | 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 | 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 | 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 | Arabidopsis thaliana | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.4.11 | methionine sulfoxide reductase A | - |
Staphylococcus aureus |
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 | - |
Homo sapiens |
1.8.4.11 | methionine sulfoxide reductase A | - |
Sus scrofa |
1.8.4.11 | methionine sulfoxide reductase A | - |
Saccharomyces cerevisiae |
1.8.4.11 | methionine sulfoxide reductase A | - |
Arabidopsis thaliana |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | Staphylococcus aureus |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | Mus musculus |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | Escherichia coli |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | Homo sapiens |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | Sus scrofa |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | Saccharomyces cerevisiae |
1.8.4.11 | More | the enzyme belongs to the Msr family of enzymes | 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 B | - |
Mus musculus |
1.8.4.12 | methionine sulfoxide reductase B | - |
Homo sapiens |
1.8.4.12 | methionine sulfoxide reductase B | - |
Saccharomyces cerevisiae |
1.8.4.12 | methionine sulfoxide reductase B | - |
Arabidopsis thaliana |
1.8.4.12 | More | the enzyme belongs to the Msr family of enzymes | Mus musculus |
1.8.4.12 | More | the enzyme belongs to the Msr family of enzymes | Homo sapiens |
1.8.4.12 | More | the enzyme belongs to the Msr family of enzymes | Saccharomyces cerevisiae |
1.8.4.12 | More | the enzyme belongs to the Msr family of enzymes | Arabidopsis thaliana |
1.8.4.12 | MsrB | - |
Mus musculus |
1.8.4.12 | MsrB | - |
Homo sapiens |
1.8.4.12 | MsrB | - |
Saccharomyces cerevisiae |
1.8.4.12 | MsrB | - |
Arabidopsis thaliana |
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 | - |
Mus musculus | |
1.8.4.12 | thioredoxin | - |
Homo sapiens | |
1.8.4.12 | thioredoxin | - |
Saccharomyces cerevisiae | |
1.8.4.12 | thioredoxin | - |
Arabidopsis thaliana |