EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | Escherichia coli | the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | Homo sapiens | the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview | L-methionine + thioredoxin disulfide + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.4.B3 | Homo sapiens | Q8IXL7 | - |
- |
1.8.4.B3 | Homo sapiens | Q9Y3D2 | - |
- |
1.8.4.12 | Escherichia coli | - |
- |
- |
1.8.4.12 | Homo sapiens | - |
isozyme MsrB2 | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.8.4.12 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin | catalytic mechanism and the role of cofactor recycling in vivo | Escherichia coli | |
1.8.4.12 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin | catalytic mechanism and the role of cofactor recycling in vivo | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.4.B3 | L-methionine (R)-S-sulfoxide + dithiothreitol | - |
Homo sapiens | L-methionine + dithiothreitol disulfide + H2O | - |
? | |
1.8.4.B3 | L-methionine (R)-S-sulfoxide + thionein | - |
Homo sapiens | L-methionine + thionein disulfide + H2O | - |
? | |
1.8.4.B3 | L-methionine (R)-S-sulfoxide + thioredoxin | reduced thioredoxin is not an efficient reducing agent for hMsrB3. Less than 5% of the activity with dithiothreitol | Homo sapiens | L-methionine + thioredoxin disulfide | - |
? | |
1.8.4.B3 | L-methionine (R)-S-sulfoxide + thioredoxin | reduced thioredoxin is not an efficient reducing agent for hMsrB2. Less than 5% of the activity with dithiothreitol | Homo sapiens | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.B3 | L-methionine (R)-sulfoxide + dithiothreitol | - |
Homo sapiens | L-methionine + dithiothreitol disulfide | - |
? | |
1.8.4.B3 | additional information | zinc-containing metallothionein in the presence of EDTA can serve as a reducing agent. Thioredoxin can reduce oxidized thionein | Homo sapiens | ? | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + DTT | - |
Escherichia coli | L-methionine + DTT disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + DTT | - |
Homo sapiens | L-methionine + DTT disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | - |
Escherichia coli | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | - |
Homo sapiens | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview | Escherichia coli | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview | Homo sapiens | L-methionine + thioredoxin disulfide + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.4.B3 | hMsrB2 | - |
Homo sapiens |
1.8.4.B3 | hMsrB3 | - |
Homo sapiens |
1.8.4.12 | MsrB | - |
Escherichia coli |
1.8.4.12 | MsrB | - |
Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.12 | dithiothreitol | can act as cofactor only in vitro showing a much higher activity than thioredoxin | Homo sapiens | |
1.8.4.12 | dithiothreitol | can substitute for thioredoxin in vitro | Escherichia coli | |
1.8.4.12 | thioredoxin | natural cofactor, the cofactor can be recycled in vivo by reduction via zinc-containing metallothionein, Zn-MT, after removal of the zinc ion due to its high content of cysteines, mechanism, overview | Homo sapiens | |
1.8.4.12 | thioredoxin | preferred and natural cofactor, the cofactor can be recycled in vivo by reduction via zinc-containing metallothionein, Zn-MT, after removal of the zinc ion due to its high content of cysteines, mechanism, overview | Escherichia coli |