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Information on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase and Organism(s) Escherichia coli and UniProt Accession P0A744

for references in articles please use BRENDA:EC1.8.4.11
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IUBMB 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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Escherichia coli
UNIPROT: P0A744
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methionine sulfoxide reductase
-
peptide methionine sulfoxide reductase type A
-
methionine S-oxide reductase (S-form oxidizing)
-
-
-
-
methionine sulfoxide reductase
-
-
methionine sulfoxide reductase A
-
-
MetSO-L12 reductase
-
-
peptide methionine sulfoxide reductase
-
-
additional information
-
the enzyme belongs to the Msr family of enzymes
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism and structural features, roles of cysteine residues, active site structure
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin
acetyl-L-methionine-NHMe + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
show the reaction diagram
-
FMsr is specific for the S-isomer
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
FMsr is specific for the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the membrane-associated isozyme reduces both R- and S-stereoisomer of methionine sulfoxide in proteins
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
show the reaction diagram
-
enzyme reduces L-methionine (S)-sulfoxide of the protein substrate
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
show the reaction diagram
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
NADPH
-
membrane-bound enzyme form Mem-R,S-Msr
thioredoxin
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
enzyme prefers high ionic strength, activation
Mg2+
-
activates
Na2SO4
-
enzyme prefers high ionic strength, activation
NaCl
-
enzyme prefers high ionic strength, activation
NaF
-
enzyme prefers high ionic strength, activation
selenium
-
selenocysteine-containing
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
dimedone
-
binds specifically to the sulfenic acid reaction intermediate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
thioredoxin
mutant C86S/C206S, pH 8.0, 25°C
0.12 - 1.9
L-methionine (S)-sulfoxide
0.01
thioredoxin
-
pH 8.0, 25°C, substrate L-methionine (S)-sulfoxide
additional information
additional information
-
kinetic mechanism
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.088
thioredoxin
mutant C86S/C206S, pH 8.0, 25°C
3.7
L-methionine (S)-sulfoxide
-
pH 8.0, 25°C, cofactor thioredoxin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00009
-
enzyme form Mem-R,S-Msr, substrate sulindac
0.00019
0.0004
-
membrane vesicles, substrate N-acetyl-L-methionine-(R)-sulfoxide
0.00044
-
MsrA, substrate N-acetyl-L-methionine-(S)-sulfoxide
0.00047
-
membrane vesicles, substrate N-acetyl-L-methionine-(S)-sulfoxide
0.0018
-
wild-type strain, substrate L-methionine (S)-sulfoxide
0.33
-
in vitro, substrate free L-methionine (R)-sulfoxide
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
soluble isozyme MsrA1
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
x * 25000, MsrA
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 25000, MsrA
monomer
-
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
15-50 mg/ml purified recombinant MsrA in 50 mM Tris-HCl, pH 8.0, 2 mM EDTA, and 10 mM DTT, hanging drop vapour diffusion method, droplet size is 0.004-0.008 ml, equal volumes of protein and precipitant solution, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C86S/C206S
KM and kcat value are 19fold higher and 40fold slower compared to wild type, respectively. The Cys198-Cys206 disulfide bond is rather reduced by thioredoxin under steady-state conditions instead of the Cys51-Cys198 disulfide bond
C198S
-
MsrA mutant, mutation of one recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, probably due to formation of a nonproductive complex between sulfenic intermediate and thioredoxin
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration
-
partially
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
-
recombinant MsrA
-
recombinant MsrA from strain B834(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene msrA
-
gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, functional overexpression of MsrB from gene msrB or yeaA
-
gene msrA, expression in an msrA-deficient Escherichia coli mutant strain Tn903::msrA conferring resistance against oxidative damage from reactive nitrogen intermediates
-
gene msrA, expression in Escherichia coli strain BL21(DE3) as His-tagged enzyme
-
gene msrA, expression in strain B834(DE3)
-
gene msrA, located in the chromosome at 95.69 min, respectively, recombinant expression of msrA, regulation mechanism of gene expression, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
with MsrA adsorbed on glassy carbon and boron doped diamond electrodes surface, the first step reaction step corresponds to the oxidation of tyrosine and tryptophan residues and occurs for the same potential. The second step is histidine oxidation, and the third, at higher potentials, the second tryptophan oxidation. MsrA adsorbs on the hydrophobic carbon electrode surface preferentially through the three hydrophobic domains, C1, C2 and C3, which contain the tyrosine, tryptophan and histidine residues
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
Manually annotated by BRENDA team
Brot, N.; Weissbach, L.; Werth, J.; Weissbach, H.
Enzymatic reduction of protein-bound methionine sulfoxide
Proc. Natl. Acad. Sci. USA
78
2155-2158
1981
Escherichia coli, Escherichia coli Z19
Manually annotated by BRENDA team
Wizemann, T.M.; Moskovitz, J.; Pearce, B.J.; Cundell, D.; Arvidson, C.G.; So, M.; Weissbach, H.; Brot, N.; Masure, H.R.
Peptide methionine-sulfoxide reductase contributes to the maintenance of adhesions in three major pathogens
Proc. Natl. Acad. Sci. USA
93
7985-7990
1996
Streptococcus pneumoniae, Escherichia coli, Neisseria gonorrhoeae, Neisseria gonorrhoeae MS11A, Streptococcus pneumoniae R6x
Manually annotated by BRENDA team
Moskovitz, J.; Poston, J.M.; Berlett, B.S.; Nosworthy, N.J.; Szczepanowski, R.; Stadtman, E.R.
Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
J. Biol. Chem.
275
14167-14172
2000
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
St.John, G.; Brot, N.; Ruan, J.; Erdjument-Bromage, H.; Tempst, P.; Weissbach, H.; Nathan, C.
Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
Proc. Natl. Acad. Sci. USA
98
9901-9906
2001
Escherichia coli, Mycobacterium tuberculosis
Manually annotated by BRENDA team
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
Streptococcus pneumoniae, Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Mycoplasma genitalium, Neisseria gonorrhoeae, Neisseria meningitidis, no activity in Aquifex aeolicus, no activity in Thermotoga maritima, Sinorhizobium meliloti, Staphylococcus aureus, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Bacillus subtilis, Bos taurus (P54149), Deinococcus radiodurans, Escherichia coli (P0A744), Mycobacterium tuberculosis (P9WJM5), Mycobacterium tuberculosis H37Rv (P9WJM5), Neisseria gonorrhoeae (P14930), Neisseria meningitidis, Solanum lycopersicum
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Tete-Favier, F.; Cobessi, D.; Leonard, G.A.; Azza, S.; Talfournier, F.; Boschi-Muller, S.; Branlant, G.; Aubry, A.
Crystallization and preliminary X-ray diffraction studies of the peptide methionine sulfoxide reductase from Escherichia coli
Acta Crystallogr. Sect. D
56
1194-1197
2000
Escherichia coli
Manually annotated by BRENDA team
Moskovitz, J.
Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival
Curr. Pharm. Des.
11
1451-1457
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Staphylococcus aureus, Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Beraud, S.; Bersch, B.; Brutscher, B.; Gans, P.; Barras, F.; Blackledge, M.
Direct structure determination using residual dipolar couplings: reaction-site conformation of methionine sulfoxide reductase in solution
J. Am. Chem. Soc.
124
13709-13715
2002
Dickeya chrysanthemi, Escherichia coli (P0A744)
Manually annotated by BRENDA team
Boschi-Muller, S.; Gand, A.; Branlant, G.
The methionine sulfoxide reductases: Catalysis and substrate specificities
Arch. Biochem. Biophys.
474
266-273
2008
Escherichia coli, Neisseria meningitidis (Q9JWM8)
Manually annotated by BRENDA team
Kim, H.Y.; Gladyshev, V.N.
Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals
Biochem. J.
407
321-329
2007
Bos taurus, Escherichia coli, Homo sapiens, Mycobacterium tuberculosis, Neisseria gonorrhoeae, Neisseria meningitidis, Populus trichocarpa, Mus musculus (Q9D6Y7)
Manually annotated by BRENDA team
Kriznik, A.; Boschi-Muller, S.; Branlant, G.
Kinetic evidence that methionine sulfoxide reductase A can reveal its oxidase activity in the presence of thioredoxin
Arch. Biochem. Biophys.
548
54-59
2014
Escherichia coli (P0A744), Escherichia coli
Manually annotated by BRENDA team
Enache, T.; Oliveira-Brett, A.
Peptide methionine sulfoxide reductase A (MsrA) Direct electrochemical oxidation on carbon electrodes
Bioelectrochemistry
89
11-18
2013
Escherichia coli (P0A744)
Manually annotated by BRENDA team