Information on EC 1.8.4.13 - L-methionine (S)-S-oxide reductase

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

EC NUMBER
COMMENTARY hide
1.8.4.13
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RECOMMENDED NAME
GeneOntology No.
L-methionine (S)-S-oxide reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-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
Requires NADPH [2]. The reaction occurs in the opposite direction to that given above. Dithiothreitol can replace reduced thioredoxin. L-Methionine (R)-S-oxide is not a substrate [see EC 1.8.4.14, L-methionine (R)-S-oxide reductase].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain 2276
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Manually annotated by BRENDA team
strain 2276
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Manually annotated by BRENDA team
two enzyme forms
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-
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 S-oxide + NADPH
L-methionine + NADP+ + H2O
show the reaction diagram
L-methionine (S)-S-oxide + NADPH
L-methionine + NADP+ + H2O
show the reaction diagram
L-methionine (S)-S-oxide + reduced DTT
L-methionine + oxidized DTT + H2O
show the reaction diagram
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highest activity at 10 mM
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-
?
L-methionine (S)-sulfoxide + NADPH + H+
L-methionine + NADP+ + H2O
show the reaction diagram
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membrane-bound enzyme form Mem-R,S-Msr
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-
?
L-methionine sulfoxide enkephalin + NADPH
L-methionine enkephalin + NADP+ + H2O
show the reaction diagram
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membrane-bound enzyme form Mem-R,S-Msr
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-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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-
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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membrane-bound enzyme form Mem-R,S-Msr
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-
?
sulindac + NADPH
sulindac sulfide + NADP+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-(-)-methionine S-oxide + NADPH
L-methionine + NADP+ + H2O
show the reaction diagram
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the enzyme is specific for the L-(-)-stereoisomer
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ir
L-methionine (S)-sulfoxide + NADPH + H+
L-methionine + NADP+ + H2O
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
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-
?
sulindac + NADPH
sulindac sulfide + NADP+ + H2O
show the reaction diagram
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activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibits anti-inflammatory activity
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
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complete inhibition at 1 mM
arsenite
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strong inhibition
bovine serum albumin
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DL-methionine sulfoximine
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50% inhibition at 1 mM
hydroxyethyl disulfide
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competitively inhibits the activity with L-(-)-methionine S-oxide about 2.5fold
iodoacetic acid
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complete inhibition at 10 mM
L-(-)-methionine S-oxide
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competitively inhibits the activity with a disulfide about 2.5fold
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
L-(-)-methionine S-oxide
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pH 7.0, 22°C
0.0003
L-methionine (S)-S-oxide
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pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00009
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enzyme form Mem-R,S-Msr, substrate sulindac
0.00452
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
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assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme form Mem-R,S-Msr
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 21000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme about 1100fold by ammonium sulfate fractionation, anion exchange chromatography, gel filtration, again anion exchange chromatography, heat treatment, and hydroxyapatite chromatography to near homogeneity
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native enzyme partially by subcellular fractionation
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two native enzyme forms by ammonium sulfate fractionation, anion exchange chromatography, and a calcium phosphate resin chromatography
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs