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 |
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 |
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 |
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 |
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 | - |
? |
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 | - |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
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 |
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 | - |
? |
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 |
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 |
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 |
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 |
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 |
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 |