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Enzyme Nomenclature
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
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EC NUMBER 
COMMENTARY 
1.8.4.13
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RECOMMENDED NAME
GeneOntology No.
L-methionine (S)-S-oxide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-methionine (S)-S-oxide + reduced DTT
L-methionine + oxidized DTT + H2O
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highest activity at 10 mM
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-
?
L-methionine (S)-sulfoxide + NADPH + H+
L-methionine + NADP+ + H2O
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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
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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
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-
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?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
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membrane-bound enzyme form Mem-R,S-Msr
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-
?
L-(-)-methionine S-oxide + NADPH
L-methionine + NADP+ + H2O
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the enzyme is specific for the L-(-)-stereoisomer
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ir
L-(-)-methionine S-oxide + NADPH
L-methionine + NADP+ + H2O
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the enzyme is absolutely specific for the L-(-)-stereoisomer
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ir
L-methionine (S)-S-oxide + NADPH
L-methionine + NADP+ + H2O
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substrate is L-Met-DL-sulfoxide or L-Met-L-sulfoxide
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-
?
L-methionine (S)-S-oxide + NADPH
L-methionine + NADP+ + H2O
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substrate is L-Met-DL-sulfoxide or L-Met-L-sulfoxide
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-
?
sulindac + NADPH
sulindac sulfide + NADP+ + H2O
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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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?
sulindac + NADPH
sulindac sulfide + NADP+ + H2O
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activity with membrane-bound enzyme form Mem-R,S-Msr
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?
additional information
?
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the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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additional information
?
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substrate specificity, overview, Mem-R,S-Msr can also catalyze the reduction of L-methionine (R)-sulfoxide, EC 1.8.4.14, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation
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additional information
?
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no activity with peptide-L-methionine-(S)-S-oxide
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additional information
?
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methionine sulfoxide reduction pathway, overview
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additional information
?
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the enzyme might act in vivo on the free methionine sulfoxide substrate or on protein-bound methionine sulfoxide residues
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additional information
?
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the enzyme might act in vivo on the free methionine sulfoxide substrate or on protein-bound methionine sulfoxide residues
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additional information
?
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the purified enzyme may contain thioredoxin
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-(-)-methionine S-oxide + NADPH
L-methionine + NADP+ + H2O
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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
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
sulindac + NADPH
sulindac sulfide + NADP+ + H2O
-
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
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
methionine sulfoxide reduction pathway, overview
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-
-
additional information
?
-
-
the enzyme might act in vivo on the free methionine sulfoxide substrate or on protein-bound methionine sulfoxide residues
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additional information
?
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the enzyme might act in vivo on the free methionine sulfoxide substrate or on protein-bound methionine sulfoxide residues
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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NADPH
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required, can be substituted by DTT, but not by GSH or 2-mercaptoethanol
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydroxyethyl disulfide
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competitively inhibits the activity with L-(-)-methionine S-oxide about 2.5fold
L-(-)-methionine S-oxide
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competitively inhibits the activity with a disulfide about 2.5fold
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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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
LITERATURE
synthesis
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enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.4.13)
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