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calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
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chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
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peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
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protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
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type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
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protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
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protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
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type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
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protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
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sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
additional information
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calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
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calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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enzyme is involved in repairing of oxidized methionine residues in proteins
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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substrates are peptides and proteins
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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Msr is specific for the R-isomer
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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protein-bound methionine residues
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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protein-bound methionine residues
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form of the substrate
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ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is stereospecific for the R-epimer of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB specifically reduces the R-form of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB specifically reduces the R-form of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the (R)-form of the substrate
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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absolute stereospecific reduction
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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stereospecific reduction
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrB is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
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r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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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
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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stereospecific reduction
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
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activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
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sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
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activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
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sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
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sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
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activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
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additional information
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role of the MsrA/MsrB repair pathway in cellular protein dynamics, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
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additional information
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enzyme has regulatory function in the plant cell
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additional information
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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
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additional information
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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
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additional information
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MsrB3 plays an important role in cold tolerance by eliminating methionine sulfoxide and reactive oxygen species that accumulate at the endoplasmic reticulum during cold acclimation
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
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additional information
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the enzyme protects cells against oxidative damage and plays a role in age-related diseases
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additional information
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MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
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additional information
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MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
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additional information
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enzyme provides protection for the cell against oxidative stress
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additional information
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
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additional information
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enzyme contributes to resistance against cadmium, physiological role
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
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additional information
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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
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additional information
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
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additional information
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downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
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additional information
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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
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additional information
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the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
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additional information
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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
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additional information
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Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
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additional information
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Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
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additional information
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the enzyme contributes to the ecological performance of Lactobacillus reuteri in gastrointestinal ecosystems together with the high-molecular-mass surface protein Lsp, enzyme expression is induced in vivo
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additional information
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the enzyme contributes to the ecological performance of Lactobacillus reuteri in gastrointestinal ecosystems together with the high-molecular-mass surface protein Lsp, enzyme expression is induced in vivo
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additional information
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enzyme provides protection for the cell against oxidative stress
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additional information
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protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
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additional information
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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
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additional information
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the enzyme protect cells against oxidative damage and plays a role in age-related diseases
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additional information
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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
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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enzyme acts on free and protein-bound methionine
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additional information
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PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
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additional information
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The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
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additional information
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PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
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additional information
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enzyme acts on free and protein-bound methionine
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additional information
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the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
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additional information
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
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additional information
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, enzyme activity is not age-related
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additional information
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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
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additional information
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the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
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additional information
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the enzyme protects cells against oxidative damage and plays a role in age-related diseases
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additional information
?
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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
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additional information
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the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
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additional information
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potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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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
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additional information
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the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
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additional information
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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
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additional information
?
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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