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Literature summary for 1.8.4.12 extracted from
- New membrane-associated and soluble peptide methionine sulfoxide reductases in Escherichia coli (2003), Biochem. Biophys. Res. Commun., 302, 284-289.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a MsrA/MsrB double mutant | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Escherichia coli | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protein-L-methionine-(R)-sulfoxide + thioredoxin | Escherichia coli | MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin | protein-L-methionine + thioredoxin disulfide + H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
wild-type strain MC1061, isozyme MsrB and a membrane-associated isozyme | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.00022 | - |
MsrB, substrate N-acetyl-L-methionine-(R)-sulfoxide | Escherichia coli |
| 0.0004 | - |
membrane vesicles, substrate N-acetyl-L-methionine-(R)-sulfoxide | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-methionine (R)-sulfoxide + thioredoxin | MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins | Escherichia coli | L-methionine + thioredoxin disulfide + H2O | - |
? | |
| additional information | the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates, the membrane-associated isozyme also shows MsrA activity utilizing L-methionine (S)-sulfoxide and N-acetyl-L-methionine (S)-sulfoxide as substrates | Escherichia coli | ? | - |
? | |
| N-acetyl-L-methionine (R)-sulfoxide + thioredoxin | MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers | Escherichia coli | N-acetyl-L-methionine + thioredoxin disulfide + H2O | - |
? | |
| protein-L-methionine-(R)-sulfoxide + thioredoxin | MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin | Escherichia coli | protein-L-methionine + thioredoxin disulfide + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MsrB | - |
Escherichia coli |
| peptide methionine sulfoxide reductase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity | Escherichia coli | |
| thioredoxin | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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