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IUBMB CommentsThe reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid . On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, are found within the same protein whereas, in other species, they are separate proteins [1,4]. The reaction proceeds via a sulfenic-acid intermediate [5,10].
Synonyms
methionine sulfoxide reductase a, msra1, msra2, methionine sulfoxide reductases a, msra-1, methionine-s-sulfoxide reductase, peptide methionine sulphoxide reductase, methionine sulphoxide reductase a, peptide methionine sulfoxide reductase a, protein-methionine-s-oxide reductase,
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N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
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peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
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calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
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synthetic substrate
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dimethylsulfide + thioredoxin disulfide + H2O
dimethylsulfoxide + thioredoxin
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L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrA is specific for the S-form
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protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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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calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
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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
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calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
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MsrA is specific for the S-form, recombinant human calmodulin, recombinant rat enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview
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protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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MsrA is specific for the S-form
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protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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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
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calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
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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
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L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrA is specific for the S-form
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protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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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
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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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?
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
brenda
maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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maximal expression level of MsrA in kidney and liver, followed by heart, lung, brain, skeletal muscle, retina, testis, bone marrow, and blood
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splice variant msrA2a. Multiple MSRA variants participate in the repair of oxidized proteins in vascular smooth muscle cells mitochondria
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MsrA
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retinal pigment epithelium
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retinal pigment epithelium
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additional information
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organ-specific expression patterns
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MsrA
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MsrA
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Vougier, S.; Mary, J.; Friguet, B.
Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells
Biochem. J.
373
531-537
2003
Rattus norvegicus
brenda
Petropoulos, I.; Friguet, B.
Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases
Biochim. Biophys. Acta
1703
261-266
2005
Saccharomyces cerevisiae, Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
Vougier, S.; Mary, J.; Dautin, N.; Vinh, J.; Friguet, B.; Ladant, D.
Essential role of methionine residues in calmodulin binding to Bordetelle pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases
J. Biol. Chem.
279
30210-30218
2004
Rattus norvegicus
brenda
Picot, C.R.; Moreau, M.; Juan, M.; Noblesse, E.; Nizard, C.; Petropoulos, I.; Friguet, B.
Impairment of methionine sulfoxide reductase during UV irradiation and photoaging
Exp. Gerontol.
42
859-863
2007
Mus musculus, Rattus norvegicus, Homo sapiens (Q9UJ68), Homo sapiens
brenda
Haenold, R.; Wassef, R.; Hansel, A.; Heinemann, S.H.; Hoshi, T.
Identification of a new functional splice variant of the enzyme methionine sulphoxide reductase A (MSRA) expressed in rat vascular smooth muscle cells
Free Radic. Res.
41
1233-1245
2007
Rattus norvegicus (Q923M1)
brenda
Le, H.T.; Chaffotte, A.F.; Demey-Thomas, E.; Vinh, J.; Friguet, B.; Mary, J.
Impact of hydrogen peroxide on the activity, structure, and conformational stability of the oxidized protein repair enzyme methionine sulfoxide reductase A
J. Mol. Biol.
393
58-66
2009
Rattus norvegicus (Q923M1)
brenda
Guan, X.L.; Wu, P.F.; Wang, S.; Zhang, J.J.; Shen, Z.C.; Luo, H.; Chen, H.; Long, L.H.; Chen, J.G.; Wang, F.
Dimethyl sulfide protects against oxidative stress and extends lifespan via a methionine sulfoxide reductase A-dependent catalytic mechanism
Aging Cell
16
226-236
2017
Drosophila melanogaster, Rattus norvegicus, Caenorhabditis elegans (O02089)
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Wu, P.; Zhang, Z.; Guan, X.; Li, Y.; Zeng, J.; Zhang, J.; Long, L.; Hu, Z.; Wang, F.; Chen, J.
A specific and rapid colorimetric method to monitor the activity of methionine sulfoxide reductase A
Enzyme Microb. Technol.
53
391-397
2013
Rattus norvegicus (Q923M1)
brenda
Dun, Y.; Vargas, J.; Brot, N.; Finnemann, S.C.
Independent roles of methionine sulfoxide reductase A in mitochondrial ATP synthesis and as antioxidant in retinal pigment epithelial cells
Free Radic. Biol. Med.
65
1340-1351
2013
Rattus norvegicus
brenda
Lourenco Dos Santos, S.; Petropoulos, I.; Friguet, B.
The oxidized protein repair enzymes methionine sulfoxide reductases and their roles in protecting against oxidative stress, in ageing and in regulating protein function
Antioxidants (Basel)
7
191
2018
Rattus norvegicus (Q923M1), Mus musculus (Q9D6Y7), Homo sapiens (Q9UJ68)
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Liu, Y.; Chong, L.; Li, X.; Tang, P.; Liu, P.; Hou, C.; Zhang, X.; Li, R.
Astragaloside IV rescues MPP+-induced mitochondrial dysfunction through upregulation of methionine sulfoxide reductase A
Exp. Ther. Med.
14
2650-2656
2017
Rattus norvegicus
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