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IUBMB Comments Requires NADPH. Unlike EC 1.8.4.12 , peptide-methionine (R )-S -oxide reductase, this enzyme cannot use peptide-bound methionine (R )-S -oxide as a substrate . Differs from EC 1.8.4.13 , L -methionine (S )-S -oxide in that L -methionine (S )-S -oxide is not a substrate.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms tafrmsr, more
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EC 1.8.4.5
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formerly, part transferred
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methionine sulfoxide reductase
methionine-R-sulfoxide reductase
fRMsr
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methionine sulfoxide reductase
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methionine sulfoxide reductase
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methionine-R-sulfoxide reductase
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methionine-R-sulfoxide reductase
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NMV_2074
locus name
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L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin
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L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (R)-S-oxide-forming]
Requires NADPH. Unlike EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, this enzyme cannot use peptide-bound methionine (R)-S-oxide as a substrate [1]. Differs from EC 1.8.4.13, L-methionine (S)-S-oxide in that L-methionine (S)-S-oxide is not a substrate.
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-S-oxide + thioredoxin
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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Substrates: - Products: -
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additional information
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: fRMsr exhibits the highest Met-(R)-O reductase activity when all components of the NADPHTrxR-Trx system are present in the reaction. The enzyme is not able to reduce L-methionine (S)-S-oxide, Met sulfone, dimethyl sulfoxide, or MetO when present in the synthetic peptide NH2-Pro-Thr-Ser-Met-(RS)-O-Glu-His-Val-NH2. Escherichia coli fRMsr is the first GAF domain family member to show enzymatic activity Products: -
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: - Products: -
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: - Products: -
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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Substrates: the enzyme only reduces the free form of methionine-R-sulfoxide Products: -
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: the enzyme exhibits strict substrate specificity toward free L-methionine (R)-S-oxide and is unable to reduce dabsylated (peptidyl) L-methionine (R)-S-oxide, free L-methionine S-oxide, or dimethylsulfoxide Products: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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Substrates: - Products: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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Substrates: - Products: -
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L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-S-oxide + thioredoxin
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Substrates: enzyme specific for free L-methionine-(R)-sulfoxide and not met-R-(o) in peptide linkage Products: -
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L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-S-oxide + thioredoxin
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Substrates: enzyme specific for free L-methionine-(R)-sulfoxide and not met-R-(o) in peptide linkage Products: -
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additional information
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Substrates: no activity with peptide-L-methionine-(R)-S-oxide Products: -
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additional information
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Substrates: in the absence of thioredoxin, 1 mol of Met/subunit is formed Products: -
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additional information
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Substrates: in the absence of thioredoxin, 1 mol of Met/subunit is formed Products: -
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dithiothreitol
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DTT can replace NADPH, but is much less effective
NADPH
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absolute requirement
thioredoxin
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omission results in a 70% drop in activity
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0.33 - 32
L-methionine (R)-S-oxide
0.0098 - 0.05
thioredoxin
0.33
L-methionine (R)-S-oxide
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pH 7.5, 25°C, mutant enzyme C60S
0.33
L-methionine (R)-S-oxide
pH 7.5, 25°C, mutant enzyme C60S
0.4
L-methionine (R)-S-oxide
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pH 7.5, 25°C, wild-type enzyme
0.4
L-methionine (R)-S-oxide
pH 7.5, 25°C, wild-type enzyme
0.47
L-methionine (R)-S-oxide
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pH 7.5, 25°C, mutant enzyme C15S
0.47
L-methionine (R)-S-oxide
pH 7.5, 25°C, mutant enzyme C15S
2
L-methionine (R)-S-oxide
wild-type, 25°C, pH 8.0
2.2
L-methionine (R)-S-oxide
mutant C136A, 25°C, pH 8.0
3.9
L-methionine (R)-S-oxide
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12
L-methionine (R)-S-oxide
mutant C84A/C136A, 25°C, pH 8.0
18
L-methionine (R)-S-oxide
mutant C94A/C136A, 25°C, pH 8.0
30
L-methionine (R)-S-oxide
mutant C84A, 25°C, pH 8.0
30
L-methionine (R)-S-oxide
mutant C84A/C94A/C136A, 25°C, pH 8.0
32
L-methionine (R)-S-oxide
mutant C94A , 25°C, pH 8.0
0.0098
thioredoxin
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0.015
thioredoxin
mutant C94A/C136A, 25°C, pH 8.0
0.016
thioredoxin
mutant C84A/C94A/C136A, 25°C, pH 8.0
0.024
thioredoxin
mutant C94A , 25°C, pH 8.0
0.027
thioredoxin
mutant C136A, 25°C, pH 8.0
0.04
thioredoxin
mutant C84A/C136A, 25°C, pH 8.0
0.04
thioredoxin
wild-type, 25°C, pH 8.0
0.05
thioredoxin
mutant C84A, 25°C, pH 8.0
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0.003 - 18
L-methionine (R)-S-oxide
0.003
L-methionine (R)-S-oxide
pH 7.5, 25°C, mutant enzyme C60S
0.0033
L-methionine (R)-S-oxide
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pH 7.5, 25°C, mutant enzyme C60S
0.268
L-methionine (R)-S-oxide
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pH 7.5, 25°C, wild-type enzyme
0.29
L-methionine (R)-S-oxide
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pH 7.5, 25°C, mutant enzyme C15S
0.29
L-methionine (R)-S-oxide
pH 7.5, 25°C, mutant enzyme C15S
1
L-methionine (R)-S-oxide
mutant C84A/C94A/C136A, 25°C, pH 8.0
1
L-methionine (R)-S-oxide
mutant C94A , 25°C, pH 8.0
2.6
L-methionine (R)-S-oxide
mutant C84A/C136A, 25°C, pH 8.0
2.8
L-methionine (R)-S-oxide
pH 7.5, 25°C, wild-type enzyme
6.9
L-methionine (R)-S-oxide
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8.5
L-methionine (R)-S-oxide
mutant C136A, 25°C, pH 8.0
13
L-methionine (R)-S-oxide
mutant C94A/C136A, 25°C, pH 8.0
14
L-methionine (R)-S-oxide
wild-type, 25°C, pH 8.0
18
L-methionine (R)-S-oxide
mutant C84A, 25°C, pH 8.0
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0.01 - 0.67
L-methionine (R)-S-oxide
0.01
L-methionine (R)-S-oxide
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pH 7.5, 25°C, mutant enzyme C60S
0.01
L-methionine (R)-S-oxide
pH 7.5, 25°C, mutant enzyme C60S
0.62
L-methionine (R)-S-oxide
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pH 7.5, 25°C, mutant enzyme C15S
0.62
L-methionine (R)-S-oxide
pH 7.5, 25°C, mutant enzyme C15S
0.67
L-methionine (R)-S-oxide
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pH 7.5, 25°C, wild-type enzyme
0.67
L-methionine (R)-S-oxide
pH 7.5, 25°C, wild-type enzyme
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brenda
serogroup C
UniProt
brenda
serogroup C
UniProt
brenda
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brenda
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Uniprot
brenda
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brenda
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UniProt
brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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15924
2 * 15924, calculated from sequence
18166
2 * 18166, calculated
36330
mass spectrometry under non-denaturing conditions
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dimer
2 * 18166, calculated
dimer
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2 * 18166, calculated
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dimer
2 * 15924, calculated from sequence
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in complex with methionine sulfoxide, to 1.25 A resolution. Residue C118 is the catalytic Cys on which a sulfenic acid is formed
hanging drop vapor diffusion method. Crystals from native and mutant enzyme grew at 20°C within 2 days. To obtain a substrate-bound form, the crystals of the C84S mutant enzyme are soaked with the mother liquid containing 10 mM Met-R-O at 22°C for 1 h
hanging-drop vapor diffusion method at 20°C. Crystal structure is determined in native form and in a complex with the substrate
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C136A
about 60% of the catalytic efficiency of wild-type
C84A
about 120% of the catalytic efficiency of wild-type
C84A/C136A
catalytic efficiency similar to wild-type
C84A/C94A/C136A
about 35% of the catalytic efficiency of wild-type
C94A
about 40% of the catalytic efficiency of wild-type
C94A/C136A
about 35% of the catalytic efficiency of wild-type
C136A
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about 60% of the catalytic efficiency of wild-type
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C84A
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about 120% of the catalytic efficiency of wild-type
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C84A/C136A
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catalytic efficiency similar to wild-type
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C94A
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about 40% of the catalytic efficiency of wild-type
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C15S
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mutant exhibits apparent activity. The kcat and Km values of the mutant enzyme are similar to those of wild type, showing that Cys15 is dispensable for catalysis
C15S
kcat and Km values of C15S are similar to those of wild type. Cells expressing the C15S mutant enzyme show similar growth to wild type-expressing cells
C60S
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mutant exhibits apparent activity. The kcat value is dramatically reduced in the C60S mutant (80fold lower), while the Km value does not significantly change compared to wild type
C60S
the kcat value is reduced in the C60S mutant (80fold lower), while the Km value does not significantly change compared to wild type. In cells expressing C60S, growth is not observed during a 3-day incubation but observed at a 7-day incubation
C84S
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no detectable activity. Cells expressing C84S do not grow in the Met-O medium at all
C84S
activity is not detectable. Cells expressing C84S do not grow in the methionione sulfoxide medium at all
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cells expressing the wild-type enzyme and C15S mutant enzyme exhibit increased resistance to H2O2-mediated oxidative stress. The resistance is similar to that of the wild type-expressing cells. In contrast, cells expressing both the C84S and C60S mutants show no resistance to the peroxide treatment
729109
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partially purified by (NH4)2SO4 precipitation (30-60% saturation) from MsrA/MsrB double mutants
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expression in Escherichia coli
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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
Escherichia coli
brenda
Etienne, F.; Spector, D.; Brot, N.; Weissbach, H.
A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide
Biochem. Biophys. Res. Commun.
300
378-382
2003
Escherichia coli, Escherichia coli MC1061
brenda
Lin, Z.; Johnson, L.C.; Weissbach, H.; Brot, N.; Lively, M.O.; Lowther, W.T.
Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function
Proc. Natl. Acad. Sci. USA
104
9597-9602
2007
Escherichia coli (P76270)
brenda
Gruez, A.; Libiad, M.; Boschi-Muller, S.; Branlant, G.
Structural and biochemical characterization of free methionine-R-sulfoxide reductase from Neisseria meningitidis
J. Biol. Chem.
285
25033-25043
2010
Neisseria meningitidis (A0A0Y6TLH6), Neisseria meningitidis 8013 (A0A0Y6TLH6)
brenda
Kim, H.S.; Kwak, G.H.; Lee, K.; Jo, C.H.; Hwang, K.Y.; Kim, H.Y.
Structural and biochemical analysis of a type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum
Arch. Biochem. Biophys.
560
10-9
2014
Thermoplasma acidophilum
brenda
Kim, H.S.; Kwak, G.H.; Lee, K.; Jo, C.H.; Hwang, K.Y.; Kim, H.Y.
Structural and biochemical analysis of a type II free methionine-R-sulfoxide reductase from Thermoplasma acidophilum
Arch. Biochem. Biophys.
560
10-19
2014
Thermoplasma acidophilum (Q9HJW5), Thermoplasma acidophilum
brenda
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