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Literature summary extracted from

  • Olry, A.; Boschi-Muller, S.; Yu, H.; Burnel, D.; Branlant, G.
    Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B (2005), Protein Sci., 14, 2828-2837.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.12 Escherichia coli
-
-
-
1.8.4.12 Neisseria meningitidis
-
bifunctional enzyme MsrA/B
-

Reaction

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

Substrates and Products (Substrate)

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 ?
-
?

Synonyms

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

Temperature Optimum [°C]

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

Cofactor

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