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dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
dabsyl-L-methionine (R)-sulfoxide + 1,4-dithioerythritol
dabsyl-L-methionine + 1,4-dithioerythritol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine-(R)-S-oxide + DTT
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
additional information
?
-
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
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
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
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
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
enzyme provides protection for the cell against oxidative stress
-
-
?
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, 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 and age-related diseases, 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, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells
-
-
?
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
-
-
?
additional information
?
-
-
the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
-
-
?
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
additional information
?
-
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
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
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
additional information
?
-
-
enzyme provides protection for the cell against oxidative stress
-
-
?
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, 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 and age-related diseases, 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, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells
-
-
?
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB 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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0.023
in 100 mM sodium phosphate, at 37°C and pH 5.7
0.055
in 100 mM sodium phosphate, at 37°C and pH 6.5
0.074
in 50 mM carbonate-bicarbonate, at 37°C and pH 10.0
0.106
substrate: cytosolic human thioredoxin 1
0.11
in 100 mM sodium phosphate, at 37°C and pH 7.0
0.119
in 50 mM Tris-HCl, at 37°C and pH 7.6
0.128
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.142
substrate: Escherichia coli thioredoxin
0.228
in 100 mM sodium phosphate, at 37°C and pH 7.5
0.267
in 50 mM Tris-HCl, at 37°C and pH 8.0
0.272
in 50 mM carbonate-bicarbonate, at 37°C and pH 9.6
0.291
substrate: dithiothreitol
0.446
in 50 mM Tris-HCl, at 37°C and pH 8.6
0.462
in 50 mM carbonate-bicarbonate, at 37°C and pH 9.2
0.484
in 50 mM Tris-HCl, at 37°C and pH 9.0
0.000046
-
purified recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.0007
-
kidney, substrate L-methionine (R)-sulfoxide
0.0019
-
liver, substrate L-methionine (R)-sulfoxide
0.002
-
purified recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and DTT
0.01
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.045
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.17
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and DTT
0.386
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
additional information
-
tissue specific activity, activity in tissues of MsrA-deficient mutant mice
additional information
-
thioredoxin- and DTT-dependent activities of mutant enzymes, overview
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C98S
the mutant show increased Km values with dithiothreitol (1.7fold) and thioredoxin (6fold) compared to the wild type enzyme
E81V
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB1s
F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, the selenocysteine-containing mutant shows reduced activity with either cofactor thioredoxin and DTT compared to wild-type selenocysteine MsrB1, while the cysteine-containing mutant shows activity and kinetics similar to the wild-type cysteine MsrB1
G77H/E81V/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to highly reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
H77G/V81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
U95C
the mutant has a significantly decreased activity
V81E
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
additional information
-
construction of a non-selenomethionine mutant of MsrB by site-directed mutagenesis, exchange of the selenomethionine by Cys, Ala, or Ser, the Cys-enzyme shows reduced activity, the Ser- and Ala-enzymes are inactive, substrate specificity, overview
additional information
-
construction of MsrB null mutant and of overexpressing strains, phenotypes, overview
additional information
-
substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
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Kryukov, G.V.; Kumar, R.A.; Koc, A.; Sun, Z.; Gladyshev, V.N.
Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase
Proc. Natl. Acad. Sci. USA
99
4245-4250
2002
Mus musculus, Drosophila melanogaster (Q8INK9)
brenda
Moskovitz, J.; Singh, V.K.; Requena, J.; Wilkinson, B.J.; Jayaswal, R.K.; Stadtman, E.R.
Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
Biochem. Biophys. Res. Commun.
290
62-65
2002
Staphylococcus aureus, Mus musculus
brenda
Bar-Noy, S.; Moskovitz, J.
Mouse methionine sulfoxide reductase B: effect of selenocysteine incorporation on its activity and expression of the seleno-containing enzyme in bacterial and mammalian cells
Biochem. Biophys. Res. Commun.
297
956-961
2002
Mus musculus
brenda
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
brenda
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
brenda
Stadtman, E.R.; Moskovitz, J.; Berlett, B.S.; Levine, R.L.
Cyclic axidation and reduction of protein methionine residues is an important antioxidant mechanism
Mol. Cell. Biochem.
2347235
3-9
2002
Mus musculus
-
brenda
Kim, H.Y.; Gladyshev, V.N.
Characterization of mouse endoplasmic reticulum methionine-R-sulfoxide reductase
Biochem. Biophys. Res. Commun.
320
1277-1283
2004
Mus musculus (Q8BU85), Mus musculus
brenda
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, Homo sapiens, Mus musculus
brenda
Kim, H.Y.; Gladyshev, V.N.
Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases
PLoS Biol.
3
2080-2089
2005
Homo sapiens, Mus musculus
-
brenda
Kim, H.Y.; Kim, J.R.
Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine
Biochem. Biophys. Res. Commun.
371
490-494
2008
Mus musculus (Q78J03), Homo sapiens (Q8IXL7)
brenda
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
Drosophila melanogaster, Neisseria meningitidis, Bacillus subtilis (P54155), Mus musculus (Q8BU85), Homo sapiens (Q8IXL7)
brenda
Le, D.T.; Liang, X.; Fomenko, D.E.; Raza, A.S.; Chong, C.K.; Carlson, B.A.; Hatfield, D.L.; Gladyshev, V.N.
Analysis of methionine/selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized forms
Biochemistry
47
6685-6694
2008
Mus musculus (Q78J03)
brenda
Uthus, E.O.; Moskovitz, J.
Specific activity of methionine sulfoxide reductase in CD-1 mice is significantly affected by dietary selenium but not zinc
Biol. Trace Elem. Res.
115
265-276
2007
Mus musculus
brenda
Breivik, A.S.; Aachmann, F.L.; Sal, L.S.; Kim, H.Y.; Del Conte, R.; del Conte, R.; Gladyshev, V.N.; Dikiy, A.
1H, 15N and 13C NMR assignments of mouse methionine sulfoxide reductase B2
Biomol. NMR Assign.
2
199-201
2008
Mus musculus (Q78J03), Mus musculus
brenda
Uthus, E.O.
Determination of the specific activities of methionine sulfoxide reductase A and B by capillary electrophoresis
Anal. Biochem.
401
68-73
2010
Mus musculus
brenda
Cao, G.; Lee, K.P.; van der Wijst, J.; de Graaf, M.; van der Kemp, A.; Bindels, R.J.; Hoenderop, J.G.
Methionine sulfoxide reductase B1 (MsrB1) recovers TRPM6 channel activity during oxidative stress
J. Biol. Chem.
285
26081-26087
2010
Mus musculus
brenda
Aachmann, F.L.; Sal, L.S.; Kim, H.Y.; Marino, S.M.; Gladyshev, V.N.; Dikiy, A.
Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis
J. Biol. Chem.
285
33315-33323
2010
Mus musculus (Q9JLC3)
brenda
Liang, X.; Fomenko, D.E.; Hua, D.; Kaya, A.; Gladyshev, V.N.
Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing
PLoS ONE
5
e11497
2010
Mus musculus
brenda
Dobrovolska, O.; Rychkov, G.; Shumilina, E.; Nerinovski, K.; Schmidt, A.; Shabalin, K.; Yakimov, A.; Dikiy, A.
Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin
J. Biomed. Biotechnol.
2012
586539
2012
Mus musculus (Q9JLC3)
brenda
Aachmann, F.L.; Kwak, G.H.; Del Conte, R.; Kim, H.Y.; Gladyshev, V.N.; Dikiy, A.
Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2
Proteins
79
3123-3131
2011
Mus musculus (Q78J03), Mus musculus
brenda
Lee, B.; Lee, S.; Choo, M.; Kim, J.; Lee, H.; Kim, S.; Fomenko, D.; Kim, H.; Park, J.; Gladyshev, V.
Selenoprotein MsrB1 promotes anti-inflammatory cytokine gene expression in macrophages and controls immune response in vivo /631/45/612 /631/250 /38 /82 /82/80 article
Sci. Rep.
7
5119
2017
Mus musculus (Q9JLC3)
brenda