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Literature summary extracted from

  • Boschi-Muller, S.; Olry, A.; Antoine, M.; Branlant, G.
    The enzymology and biochemistry of methionine sulfoxide reductases (2005), Biochim. Biophys. Acta, 1703, 231-238.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 C198S MsrA mutant, mutation of one recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, probably due to formation of a nonproductive complex between sulfenic intermediate and thioredoxin Escherichia coli
1.8.4.11 additional information mutation of the 2 recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, while exchange of the catalytic Cys for Ser causes complete loss of activity Escherichia coli
1.8.4.11 additional information mutation of the recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, while exchange of the catalytic Cys for Ser causes complete loss of activity Neisseria meningitidis
1.8.4.12 additional information mutation of the recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, while exchange of the catalytic Cys for Ser causes complete loss of activity Neisseria meningitidis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.4.11 3-carboxy 4-nitrobenzenethiol binds specifically to the sulfenic acid reaction intermediate Escherichia coli
1.8.4.11 3-carboxy 4-nitrobenzenethiol binds specifically to the sulfenic acid reaction intermediate Neisseria meningitidis
1.8.4.11 dimedone binds specifically to the sulfenic acid reaction intermediate Escherichia coli
1.8.4.11 dimedone binds specifically to the sulfenic acid reaction intermediate Neisseria meningitidis
1.8.4.12 3-carboxy 4-nitrobenzenethiol binds specifically to the sulfenic acid reaction intermediate Escherichia coli
1.8.4.12 3-carboxy 4-nitrobenzenethiol binds specifically to the sulfenic acid reaction intermediate Neisseria meningitidis
1.8.4.12 dimedone binds specifically to the sulfenic acid reaction intermediate Escherichia coli
1.8.4.12 dimedone binds specifically to the sulfenic acid reaction intermediate Neisseria meningitidis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.11 additional information
-
 additional information kinetic mechanism Bacillus subtilis
1.8.4.11 additional information
-
 additional information kinetic mechanism Escherichia coli
1.8.4.11 additional information
-
 additional information kinetic mechanism Xanthomonas campestris
1.8.4.11 0.01
-
 thioredoxin pH 8.0, 25°C, substrate L-methionine (S)-sulfoxide Escherichia coli
1.8.4.11 1.9
-
 L-methionine (S)-sulfoxide pH 8.0, 25°C, cofactor thioredoxin Escherichia coli
1.8.4.12 additional information
-
 additional information kinetic mechanism Bacillus subtilis
1.8.4.12 additional information
-
 additional information kinetic mechanism Neisseria meningitidis
1.8.4.12 additional information
-
 additional information kinetic mechanism Xanthomonas campestris
1.8.4.12 0.058
-
 thioredoxin MsrB, pH 8.0, 25°C, substrate acetyl-L-methionine (R)-sulfoxide N-methyl ester Neisseria meningitidis
1.8.4.12 1.2
-
 (S)-1-nonen-4-ol MsrB, pH 8.0, 25°C, cofactor thioredoxin Neisseria meningitidis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.12 Zn2+ about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes Escherichia coli
1.8.4.12 Zn2+ about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes Neisseria meningitidis
1.8.4.12 Zn2+ about 50% of MsrBs binds a zinc atom in opposite direction of the active site Bacillus subtilis
1.8.4.12 Zn2+ about 50% of MsrBs binds a zinc atom in opposite direction of the active site Xanthomonas campestris

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Bacillus subtilis MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Escherichia coli MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Xanthomonas campestris MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Bacillus subtilis MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Escherichia coli MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Xanthomonas campestris MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently L-methionine + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Bacillus subtilis
-
-
-
1.8.4.11 Escherichia coli
-
-
-
1.8.4.11 Neisseria meningitidis
-
 2 structurally unrelated enzymes with different stereospecificity, MsrA and MsrB, EC 1.8.4.B1, which occur in different variants, but are located on one protein
-
1.8.4.11 Xanthomonas campestris
-
 2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
-
1.8.4.12 Bacillus subtilis
-
-
-
1.8.4.12 Escherichia coli
-
-
-
1.8.4.12 Neisseria meningitidis
-
 2 structurally unrelated enzymes with different stereospecificity, MsrA, EC 1.8.4.B2, and MsrB, which occur in different variants, but are located on one protein
-
1.8.4.12 Xanthomonas campestris
-
 2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Escherichia coli
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Neisseria meningitidis
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Bacillus subtilis
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Xanthomonas campestris
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Escherichia coli
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Neisseria meningitidis
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Bacillus subtilis
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O 3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview Xanthomonas campestris
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 DL-methionine (S)-sulfoxide + thioredoxin enzyme MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently Neisseria meningitidis DL-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently Bacillus subtilis L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently Xanthomonas campestris L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 additional information substrate specificities of enzymes, the reduction step is rate-determining Neisseria meningitidis ?
-
 ?
1.8.4.11 additional information the reduction step is rate-determining Bacillus subtilis ?
-
 ?
1.8.4.11 additional information the reduction step is rate-determining Escherichia coli ?
-
 ?
1.8.4.11 additional information the reduction step is rate-determining Xanthomonas campestris ?
-
 ?
1.8.4.11 N-acetyl-L-methionine (S)-sulfoxide methyl ester + thioredoxin enzyme MsrA Neisseria meningitidis N-acetyl-L-methionine methyl ester + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 (S)-1-nonen-4-ol + thioredoxin
-
 Neisseria meningitidis ?
-
 r
1.8.4.12 DL-methionine (R)-sulfoxide + thioredoxin enzyme MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently Neisseria meningitidis DL-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently Bacillus subtilis L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently Xanthomonas campestris L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 additional information substrate specificities of enzymes, the reduction step is rate-determining Neisseria meningitidis ?
-
 ?
1.8.4.12 additional information the reduction step is rate-determining Bacillus subtilis ?
-
 ?
1.8.4.12 additional information the reduction step is rate-determining Escherichia coli ?
-
 ?
1.8.4.12 additional information the reduction step is rate-determining Xanthomonas campestris ?
-
 ?
1.8.4.12 N-acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin enzyme MsrB Neisseria meningitidis N-acetyl-L-methionine methyl ester + thioredoxin disulfide
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.4.11 monomer
-
 Bacillus subtilis
1.8.4.11 monomer
-
 Escherichia coli
1.8.4.11 monomer
-
 Neisseria meningitidis
1.8.4.11 monomer
-
 Xanthomonas campestris
1.8.4.11 More the enzyme forms are produced as individual folded entities, but in vivo the enzyme is part of a three-domain protein named PILB, with the central domain exhibiting MsrA activity, and the C-terminal domain showing MsrB activity Neisseria meningitidis
1.8.4.12 monomer
-
 Bacillus subtilis
1.8.4.12 monomer
-
 Neisseria meningitidis
1.8.4.12 monomer
-
 Xanthomonas campestris
1.8.4.12 More the enzyme forms are produced as individual folded entities, but in vivo the enzyme is part of a three-domain protein named PILB, with the central domain exhibiting MsrA activity, and the C-terminal domain showing MsrB activity Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 methionine sulfoxide reductase
-
 Bacillus subtilis
1.8.4.11 methionine sulfoxide reductase
-
 Escherichia coli
1.8.4.11 methionine sulfoxide reductase
-
 Neisseria meningitidis
1.8.4.11 methionine sulfoxide reductase
-
 Xanthomonas campestris
1.8.4.11 MsrA
-
 Bacillus subtilis
1.8.4.11 MsrA
-
 Escherichia coli
1.8.4.11 MsrA
-
 Neisseria meningitidis
1.8.4.11 MsrA
-
 Xanthomonas campestris
1.8.4.12 methionine sulfoxide reductase
-
 Bacillus subtilis
1.8.4.12 methionine sulfoxide reductase
-
 Escherichia coli
1.8.4.12 methionine sulfoxide reductase
-
 Neisseria meningitidis
1.8.4.12 methionine sulfoxide reductase
-
 Xanthomonas campestris
1.8.4.12 MsrB
-
 Bacillus subtilis
1.8.4.12 MsrB
-
 Escherichia coli
1.8.4.12 MsrB
-
 Neisseria meningitidis
1.8.4.12 MsrB
-
 Xanthomonas campestris
1.8.4.12 PilB
-
 Neisseria meningitidis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.4.11 25
-
 assay at Escherichia coli
1.8.4.11 25
-
 assay at Neisseria meningitidis
1.8.4.12 25
-
 assay at Escherichia coli
1.8.4.12 25
-
 assay at Neisseria meningitidis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.4.11 3.7
-
 L-methionine (S)-sulfoxide pH 8.0, 25°C, cofactor thioredoxin Escherichia coli
1.8.4.12 1.1
-
 (S)-1-nonen-4-ol MsrB, pH 8.0, 25°C, cofactor thioredoxin Neisseria meningitidis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.11 8
-
 assay at Escherichia coli
1.8.4.11 8
-
 assay at Neisseria meningitidis
1.8.4.12 8
-
 assay at Escherichia coli
1.8.4.12 8
-
 assay at Neisseria meningitidis

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 additional information DTT can partially substitute for thioredoxin in vitro, low activity Escherichia coli
1.8.4.11 additional information DTT can substitute for thioredoxin in vitro Bacillus subtilis
1.8.4.11 additional information DTT can substitute for thioredoxin in vitro Neisseria meningitidis
1.8.4.11 additional information DTT can substitute for thioredoxin in vitro Xanthomonas campestris
1.8.4.11 thioredoxin physiological cofactor Bacillus subtilis
1.8.4.11 thioredoxin physiological cofactor Escherichia coli
1.8.4.11 thioredoxin physiological cofactor Neisseria meningitidis
1.8.4.11 thioredoxin physiological cofactor Xanthomonas campestris
1.8.4.12 additional information DTT can partially substitute for thioredoxin in vitro, low activity Escherichia coli
1.8.4.12 additional information DTT can substitute for thioredoxin in vitro Bacillus subtilis
1.8.4.12 additional information DTT can substitute for thioredoxin in vitro Neisseria meningitidis
1.8.4.12 additional information DTT can substitute for thioredoxin in vitro Xanthomonas campestris
1.8.4.12 thioredoxin physiological cofactor Bacillus subtilis
1.8.4.12 thioredoxin physiological cofactor Escherichia coli
1.8.4.12 thioredoxin physiological cofactor Neisseria meningitidis
1.8.4.12 thioredoxin physiological cofactor Xanthomonas campestris