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Information on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase and Organism(s) Drosophila melanogaster and UniProt Accession P08761
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1.8.4.11 peptide-methionine (S)-S-oxide reductaseIUBMB Comments
The 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].
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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, protein-methionine-s-oxide reductase, peptide methionine sulfoxide reductase a, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methionine S-oxide reductase (S-form oxidizing)
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SYSTEMATIC NAME
IUBMB Comments
peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (S)-S-oxide-forming]
The 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 [9]. On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly [9]. 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].
SUBSTRATE
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
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
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-
?
dimethylsulfide + thioredoxin disulfide + H2O
dimethylsulfoxide + thioredoxin
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-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
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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
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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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?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrA is specific for the S-form, free and protein-bound methionine
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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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enzyme reduces oxidized methionine residues of the shaker potassium channel, which becomes reversibly inactivated upon oxidation
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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
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
-
-
?
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
-
-
?
additional information
?
-
-
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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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Eip71CD or Eip28/29; alternative splicing variants, overview
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
subcellular localization is regulated by alternative splicing, overview
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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supplement of dimethylsulfide leads to cytoprotection and extends longevity. MsrA knockdown abolishes the cytoprotective effect and the longevity benefits of dimethylsulfide
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MSRA_DROME
246
0
27698
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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overexpression of MsrA leads to extended life span of the flies up to 70%, the resistance against paraquat-induced oxidative stress is increased
additional information
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transgenic flies overexpressing MsrA show increased extended life span, with extended time of physical and sexual activity, and increased resistance to paraquat
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weissbach, H.; Resnick, L.; Brot, N.
Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
Biochim. Biophys. Acta
1703
203-212
2005
Bos taurus, Dickeya chrysanthemi, Drosophila melanogaster, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus, Neisseria gonorrhoeae, Neisseria meningitidis, Saccharomyces cerevisiae, Streptococcus gordonii, Streptococcus pneumoniae
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
Kim, H.Y.; Gladyshev, V.N.
Alternative first exon splicing regulates subcellular distribution of methionine sulfoxide reductases
BMC Mol. Biol.
7
11
2006
Homo sapiens, Homo sapiens (Q9UJ68), Drosophila melanogaster (P08761), Mus musculus (Q9D6Y7)
Roesijadi, G.; Rezvankhah, S.; Binninger, D.M.; Weissbach, H.
Ecdysone induction of MsrA protects against oxidative stress in Drosophila
Biochem. Biophys. Res. Commun.
354
511-516
2007
Drosophila melanogaster
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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