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Literature summary for 1.8.4.12 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
Search for more literature for 1.8.4.12

Protein Variants

Protein Variants Comment Organism
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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
Zn2+ about 50% of MsrBs binds a zinc atom in opposite direction of the active site Bacillus subtilis
Zn2+ about 50% of MsrBs binds a zinc atom in opposite direction of the active site Xanthomonas campestris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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
-
 ?
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

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-
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
-
Xanthomonas campestris
-
 2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
-

Reaction

Reaction Comment Organism Reaction ID
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
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
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
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-1-nonen-4-ol + thioredoxin
-
 Neisseria meningitidis ?
-
 r
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
-
 ?
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
-
 ?
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
-
 ?
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
-
 ?
additional information substrate specificities of enzymes, the reduction step is rate-determining Neisseria meningitidis ?
-
 ?
additional information the reduction step is rate-determining Bacillus subtilis ?
-
 ?
additional information the reduction step is rate-determining Escherichia coli ?
-
 ?
additional information the reduction step is rate-determining Xanthomonas campestris ?
-
 ?
N-acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin enzyme MsrB Neisseria meningitidis N-acetyl-L-methionine methyl ester + thioredoxin disulfide
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Bacillus subtilis
monomer
-
 Neisseria meningitidis
monomer
-
 Xanthomonas campestris
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

Synonyms Comment Organism
methionine sulfoxide reductase
-
 Bacillus subtilis
methionine sulfoxide reductase
-
 Escherichia coli
methionine sulfoxide reductase
-
 Neisseria meningitidis
methionine sulfoxide reductase
-
 Xanthomonas campestris
MsrB
-
 Bacillus subtilis
MsrB
-
 Escherichia coli
MsrB
-
 Neisseria meningitidis
MsrB
-
 Xanthomonas campestris
PilB
-
 Neisseria meningitidis

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1
-
 (S)-1-nonen-4-ol MsrB, pH 8.0, 25°C, cofactor thioredoxin Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli
8
-
 assay at Neisseria meningitidis

Cofactor

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