1.8.4.11: peptide-methionine (S)-S-oxide reductase
This is an abbreviated version!
For detailed information about peptide-methionine (S)-S-oxide reductase, go to the full flat file.
Reaction
Synonyms
EC 1.8.4.6, ecdysone-induced protein 28/29 kDa, FMsr, LIC_10545, LIC_12978, linmsra1, linmsra2, LMJF_07_1140, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase, methionine sulfoxide reductase A, methionine sulfoxide reductases A, methionine sulfoxide-S-reductase, methionine sulphoxide reductase, methionine sulphoxide reductase A, methionine-S-sulfoxide reductase, MetSO-L12 reductase, More, mrsA, MSR, MSR10, MSR180, MsrA, MSRA-1, MsrA/B, MsrA/MsrB, MsrA1, MSRA2, MSRA4, msrAB, MsrABTk, MsrBA, Peptide Met(O) reductase, peptide methionine S-sulfoxide reductase, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase A, peptide methionine sulfoxide reductase type A, peptide methionine sulphoxide reductase, peptide-methionine (S)-S-oxide reductase, peptide-methionine sulfoxide reductase, PilA, PilB, PilB protein, PMSR, PMSRA, protein-methionine-S-oxide-reductase, sulindac reductase, TbmsrA, TCDM_14270
ECTree
1.8.4.11 peptide-methionine (S)-S-oxide reductaseAdvanced search results
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Natural Substrates Products on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
-
MsrA is specific for the S-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
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
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
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
L-methionine (S)-sulfoxide + dithiothreitol
?
-
the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
MsrA suppresses dopaminergic cell death and protein aggregation induced by the complex I inhibitor rotenone or mutant alpha-synuclein, but not by the proteasome inhibitor MG132. MsrA protects against Parkinson's disease-related stresses primarily via methionine sulfoxide repair rather than by scavenging reactive oxygen species
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
Met sulfoxide residues in Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
oxidation of protein-bound methionine results in loss of protein function, but can be reversed by the enzyme activity reducing methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
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-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
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-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in oxidized protein repair
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
hormonal regulation of MsrA is implicated in conferring protection against oxidative stress in the Drosophila. Cells that are able to express MsrA were twice as resistant to H2O2 in comparison with cells that are not able to express this gene
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, the enzyme is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized A-type potassium channel ShC/B whose activity strongly depends on the oxidative state of a methionine residue in the N-terminal part of the polypeptide
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
the enzyme protects the epidermis cells against irradiation and oxidative damages, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in repair of oxidized proteins by reducing oxidized methionine residues, which is required for resistance to hydrogen peroxide and other reactive oxygen species, and for adherence to host cell surfaces
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
physiological role, overview
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
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
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
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
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, mutation of gene msrA has no effect on virulence, and on resistance to oxidative agents, and causes no defect in cell envelope, msrA is probably linked to biofilm formation, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
?
additional information
?
-
the enzyme is not a major virulence determinant in the oral pathogen, MsrA is required for protein repair and protection against oxidative damage as well as for the proper expression or maintenance of functional adhesins
-
-
?
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
?
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, 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
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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 protects neuronal cells against brief hypoxia/reoxygenation, the enzyme is involved in oxidized protein repair and protects cells against reactive oxygen species and oxidative damage preventing apoptosis, 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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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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MsrA is a virulence determinant for the plant pathogen required for full virulence
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additional information
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MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
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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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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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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 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, MsrA has several different physiological repair and regulatory functions, overview
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additional information
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the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
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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, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
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additional information
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MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
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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, 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
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additional information
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the enzyme contributes to the maintenance of adhesins in the pathogen, overview
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additional information
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MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
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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 MsrA 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, MsrA has several different physiological repair and regulatory functions, overview
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additional information
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the enzyme is an essential regulator of longevity and is important for lens cell viability and resistance to oxidative stress, methionine sulfoxide is the major oxidative stress product, up to 60%, in cataract while being essentially absent in clear lens
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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, 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
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additional information
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identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
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additional information
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identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
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additional information
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MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
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additional information
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MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
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additional information
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the enzyme catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins
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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, MsrA can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells
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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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MsrA is a regulator of antioxidant defense and lifespan in mammals
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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, 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
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additional information
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MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking
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additional information
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MsrA null mutant mice exhibit a shortened lifespan and present higher levels of protein carbonyls when exposed to hyperoxia, which indicates an increased sensitivity towards oxidative stress
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additional information
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the lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
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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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MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
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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
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additional information
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MsrA is a virulence determinant for the plant pathogen required for full virulence
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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 enzyme contributes to the maintenance of adhesins in the pathogen, overview
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additional information
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the enzyme contributes to the maintenance of adhesins in the pathogen, overview
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additional information
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enzymes 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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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, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
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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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MsrA protects the cell against damage caused by oxidative stress through treatment with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
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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, 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
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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, MsrA is important for virulence in mice
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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, MsrA 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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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
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additional information
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the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
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additional information
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the enzyme contributes to the maintenance of adhesins in the pathogen, overview
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additional information
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MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60%
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additional information
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the enzyme contributes to the maintenance of adhesins in the pathogen, 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, MsrA has several different physiological repair and regulatory functions, overview
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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, 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
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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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the enzyme plays an important role in the oxidative stress response
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