Information on EC 1.8.4.14 - L-methionine (R)-S-oxide reductase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.8.4.14
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RECOMMENDED NAME
GeneOntology No.
L-methionine (R)-S-oxide reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-methionine + thioredoxin disulfide + H2O = L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
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SYSTEMATIC NAME
IUBMB Comments
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain MC1061
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Manually annotated by BRENDA team
serogroup C
C9X208
UniProt
Manually annotated by BRENDA team
serogroup C
C9X208
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
L-methionine + thioredoxin disulfide + H2O
L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 32
L-methionine (R)-S-oxide
0.0098 - 0.05
thioredoxin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 18
L-methionine (R)-S-oxide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.67
L-methionine (R)-S-oxide
3924
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15924
2 * 15924, calculated from sequence
18166
C9X208
2 * 18166, calculated
36330
C9X208
mass spectrometry under non-denaturing conditions
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with methionine sulfoxide, to 1.25 A resolution. Residue C118 is the catalytic Cys on which a sulfenic acid is formed
C9X208
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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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial; partially purified by (NH4)2SO4 precipitation (30-60% saturation) from MsrA/MsrB double mutants
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recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
C9X208
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C118A
C9X208
inactive
C136A
C9X208
about 60% of the catalytic efficiency of wild-type
C84A
C9X208
about 120% of the catalytic efficiency of wild-type
C84A/C136A
C9X208
catalytic efficiency similar to wild-type
C84A/C94A/C136A
C9X208
about 35% of the catalytic efficiency of wild-type
C94A
C9X208
about 40% of the catalytic efficiency of wild-type
C94A/C136A
C9X208
about 35% of the catalytic efficiency of wild-type
C118A
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inactive
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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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