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Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase and Organism(s) Escherichia coli and UniProt Accession P0A746
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1.8.4.12 peptide-methionine (R)-S-oxide reductaseIUBMB Comments
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide . While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater . 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 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well . The enzyme from some species contains selenocysteine and Zn2+.
Specify your search results
Word Map
- 1.8.4.12
- thioredoxins
-
selenoproteins
- selenium
-
msrbs
- neisseria
-
metso
- trx
-
sulfenic
- methionine-s-sulfoxide
- meningitidis
-
thioredoxin-dependent
-
selenoenzyme
-
lincosamides
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(3 overall reactions are displayed. Show all (4)>>)
Synonyms
methionine sulfoxide reductase, msrb3, msrb1, msrb2, peptide methionine sulfoxide reductase, msra/b, msrab, cbs-1, methionine-r-sulfoxide reductase, methionine sulfoxide reductase b1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MsrB
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide [9]. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater [10]. 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 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well [11]. The enzyme from some species contains selenocysteine and Zn2+.
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
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
-
-
-
?
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
-
enzyme reduces L-methionine (R)-sulfoxide of the protein substrate
-
-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
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
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
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
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are peptides and proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
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
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
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
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
highest activity by a membrane bound enzyme form Mem-R,S-Msr, which preferentially reduces the R-substrate form, no activity by enzyme forms fRMsr, fSMsr, low activity by enzyme forms MsrB
-
-
?
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
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
MsrB is specific for the R-form of the substrate
-
-
?
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, 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
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
additional information
?
-
-
substrate specificity of enzyme forms with R-form of free and protein-bound methionine sulfoxide, overview
-
-
?
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates, the membrane-associated isozyme also shows MsrA activity utilizing L-methionine (S)-sulfoxide and N-acetyl-L-methionine (S)-sulfoxide as substrates
-
-
?
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 (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
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
-
-
?
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
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
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
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are peptides and proteins
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
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
-
-
?
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
?
additional information
?
-
-
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
-
-
?
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, 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
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity
thioredoxin
-
preferred and natural cofactor, the cofactor can be recycled in vivo by reduction via zinc-containing metallothionein, Zn-MT, after removal of the zinc ion due to its high content of cysteines, mechanism, overview
additional information
-
DTT can partially substitute for thioredoxin in vitro, low activity
-
additional information
-
no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding
Zn2+
additional information
Zn2+
-
about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes
Zn2+
-
binding by residues at positions 45, 48, 94, and 97, 2 CXXC-motifs, role in catalysis
Zn2+
-
with Fe2+ in a ratio of 1 mol per mole of enzyme, tight metal binding, the metal binding site is composed of two CXXC motifs located at the opposite side of the active site, role in catalysis and structural stability, overview
additional information
-
enzyme belongs to the metal-containing MsrB group I
additional information
-
the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
additional information
-
no inhibition by EDTA, 1,10-phenanthroline, and pyridine 2,6-dicarboxylic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant MsrB
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
L-methionine (R)-sulfoxide
-
in vitro, substrate free L-methionine (R)-sulfoxide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.085
purified recombinant CBS-1, substrate L-methionine (R)-sulfoxide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
analysis of three-dimensional structure and active site structure
additional information
-
MsrB has a highly conserved sequence among organisms
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C45D/C48S/C94S/C97S
-
site-directed mutagenesis, the mutant MsrB loses binding ability for Zn2+ and Fe2+, and shows no catalytic activity in presence of thioredoxin or DTT, substitution of the two cysteine residues of MsrB results in complete loss of the enzyme's metal binding and reductase activity
additional information
additional information
-
construction of a msrA/msrB double mutant for detection of additional enzyme form activities
additional information
-
H2O2 shortens the life span of cells in constructed null mutants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene msrB, located in the chromosome at 40.09 min, respectively, regulation mechanism of gene expression, overview
-
gene msrB, overexpression of wild-type enzyme and mutant enzymes in Escherichia coli strain DH5alpha
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
sRNA RyhB is a direct regulator of the MsrB. RyhB down-regulates MsrB transcripts along with Hfq and RNaseE proteins. Mutations in the ryhB, fur, hfq, or RNaseE-encoded genes result in iron-insensitive expression of MsrB. RyhB pairing to msrB mRNA prevents efficient ribosome binding and thereby inhibits translation initiation. Both RyhB-pairing sites are required to decrease msrB expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grimaud, R.; Ezraty, B.; Mitchell, J.K.; Lafitte, D.; Briand, C.; Derrick, P.J.; Barras, F.
Repair of oxidized proteins: identification of a new methionine sulfoxide reductase
J. Biol. Chem.
276
48915-48920
2001
Escherichia coli
Weissbach, H.; Etienne, F.; Hoshi, T.; Heinemann, S.H.; Lowther, W.T.; Matthews, B.; St John, G.; Nathan, C.; Brot, N.
Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function
Arch. Biochem. Biophys.
397
172-178
2002
Escherichia coli
Spector, D.; Etienne, F.; Brot, N.; Weissbach, H.
New membrane-associated and soluble peptide methionine sulfoxide reductases in Escherichia coli
Biochem. Biophys. Res. Commun.
302
284-289
2003
Escherichia coli
Etienne, F.; Resnick, L.; Sagher, D.; Brot, N.; Weissbach, H.
Reduction of Sulindac to its active metabolite, sulindac sulfide: assay and role of the methionine sulfoxide reductase system
Biochem. Biophys. Res. Commun.
312
1005-1010
2003
Bos taurus, Escherichia coli
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, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus, Neisseria gonorrhoeae, Neisseria meningitidis, Saccharomyces cerevisiae, Streptococcus gordonii, Streptococcus gordonii (Q9LAM9), Streptococcus pneumoniae
Moskovitz, J.
Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
Biochim. Biophys. Acta
1703
213-219
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Staphylococcus aureus, Mus musculus, Sus scrofa
Ezraty, B.; Aussel, L.; Barras, F.
Methionine sulfoxide reductases in prokaryotes
Biochim. Biophys. Acta
1703
221-229
2005
Aggregatibacter actinomycetemcomitans, Bacillus subtilis, Dickeya chrysanthemi, Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Neisseria gonorrhoeae, Neisseria meningitidis, no activity in Aquifex aeolicus, no activity in Thermotoga maritima, Sinorhizobium meliloti, Staphylococcus aureus, Vibrio cholerae serotype O1
Boschi-Muller, S.; Olry, A.; Antoine, M.; Branlant, G.
The enzymology and biochemistry of methionine sulfoxide reductases
Biochim. Biophys. Acta
1703
231-238
2005
Bacillus subtilis, Escherichia coli, Neisseria meningitidis, Xanthomonas campestris
Kauffmann, B.; Aubry, A.; Favier, F.
The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions
Biochim. Biophys. Acta
1703
249-260
2005
Caulobacter vibrioides, Drosophila melanogaster, Escherichia coli, Neisseria meningitidis, Pseudomonas aeruginosa, Synechococcus elongatus, Neisseria gonorrhoeae (P14930)
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
Lowther, W.T.; Weissbach, H.; Etienne, F.; Brot, N.; Matthews, B.W.
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
Nat. Struct. Biol.
9
348-352
2002
Escherichia coli (P0A746), Neisseria gonorrhoeae (P14930), Neisseria gonorrhoeae, Homo sapiens (Q9Y3D2)
Sagher, D.; Brunell, D.; Hejtmancik, J.F.; Kantorow, M.; Brot, N.; Weissbach, H.
Thionein can serve as a reducing agent for the methionine sulfoxide reductases
Proc. Natl. Acad. Sci. USA
103
8656-8661
2006
Escherichia coli, Homo sapiens
Olry, A.; Boschi-Muller, S.; Yu, H.; Burnel, D.; Branlant, G.
Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B
Protein Sci.
14
2828-2837
2005
Escherichia coli, Neisseria meningitidis
Bos, J.; Duverger, Y.; Thouvenot, B.; Chiaruttini, C.; Branlant, C.; Springer, M.; Charpentier, B.; Barras, F.
The sRNA RyhB regulates the synthesis of the Escherichia coli methionine sulfoxide reductase MsrB but not MsrA
PLoS ONE
8
e63647
2013
Escherichia coli (P0A746), Escherichia coli
EXTERNAL LINKS (specific for EC-Number 1.8.4.12)
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