EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.4.12 | C45D/C48S/C94S/C97S | site-directed mutagenesis, the mutant MsrB loses binding ability for Zn2+ and Fe2+, and shows no catalytic activity in presence of thioredoxin or DTT, substitution of the two cysteine residues of MsrB results in complete loss of the enzyme's metal binding and reductase activity | Escherichia coli |
1.8.4.12 | D45C/S48C/S94C/A97C | site-directed mutagenesis, the mutant MsrB shows increased binding of Zn2+ and Fe2+ compared to the wild-type enzyme, overview, introduction of two cysteine residues into Neisseria meningitidis MsrB analogously to the Escherichia coli enzyme results in increased tight binding of zinc to and strongly increased thermal stability with wild-type reductase activity but no thioredoxin recycling activity | Neisseria meningitidis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.12 | additional information | no inhibition by EDTA, 1,10-phenanthroline, and pyridine 2,6-dicarboxylic acid | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.8.4.12 | additional information | - |
additional information | thermodynamics and kinetics of wild-type and mutant MsrB | Escherichia coli | |
1.8.4.12 | additional information | - |
additional information | thermodynamics and kinetics of wild-type and mutant MsrB | Neisseria meningitidis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.12 | Fe2+ | with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding | Escherichia coli | |
1.8.4.12 | additional information | the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview | Escherichia coli | |
1.8.4.12 | additional information | wild-type MsrB of Neisseria meningitidis is no metal-binding enzyme, but contains a preformed metal binding site, metal binding to MsrB results in inhibition of binary complex formation between oxidized MsrB and reduced thioredoxin but not between reduced MsrB and substrate, metal content of wild-type and mutant enzymes, overview | Neisseria meningitidis | |
1.8.4.12 | Zn2+ | with Fe2+ in a ratio of 1 mol per mole of enzyme, tight metal binding, the metal binding site is composed of two CXXC motifs located at the opposite side of the active site, role in catalysis and structural stability, overview | Escherichia coli |
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 | stereospecific reduction | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | Neisseria meningitidis | stereospecific reduction | L-methionine + thioredoxin disulfide + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.4.12 | Escherichia coli | - |
- |
- |
1.8.4.12 | Neisseria meningitidis | - |
bifunctional enzyme MsrA/B | - |
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, overview | Escherichia coli | |
1.8.4.12 | peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin | catalytic mechanism, overview | Neisseria meningitidis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.4.12 | L-methionine-(R)-S-oxide + DTT | stereospecific reduction | Neisseria meningitidis | L-methionine + DTT disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | stereospecific reduction | Escherichia coli | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | L-methionine-(R)-S-oxide + thioredoxin | stereospecific reduction | Neisseria meningitidis | L-methionine + thioredoxin disulfide + H2O | - |
? | |
1.8.4.12 | additional information | the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separatly on the enzyme molecule, overview | Neisseria meningitidis | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.4.12 | methionine-R-sulfoxide reductase B | - |
Escherichia coli |
1.8.4.12 | methionine-R-sulfoxide reductase B | - |
Neisseria meningitidis |
1.8.4.12 | MsrB | - |
Escherichia coli |
1.8.4.12 | MsrB | - |
Neisseria meningitidis |
1.8.4.12 | PilB | - |
Neisseria meningitidis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.4.12 | 25 | - |
assay at | Escherichia coli |
1.8.4.12 | 25 | - |
assay at | Neisseria meningitidis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.4.12 | dithiothreitol | can substitute for thioredoxin | Neisseria meningitidis | |
1.8.4.12 | thioredoxin | - |
Escherichia coli | |
1.8.4.12 | thioredoxin | - |
Neisseria meningitidis |