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Literature summary for 1.8.4.12 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
Search for more literature for 1.8.4.12

Protein Variants

Protein Variants Comment Organism
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
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

Inhibitors Comment Organism Structure
additional information no inhibition by EDTA, 1,10-phenanthroline, and pyridine 2,6-dicarboxylic acid Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamics and kinetics of wild-type and mutant MsrB Escherichia coli
additional information
-
 additional information thermodynamics and kinetics of wild-type and mutant MsrB Neisseria meningitidis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding Escherichia coli
additional information the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview Escherichia coli
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-methionine-(R)-S-oxide + thioredoxin Escherichia coli stereospecific reduction L-methionine + thioredoxin disulfide + H2O
-
 ?
L-methionine-(R)-S-oxide + thioredoxin Neisseria meningitidis stereospecific reduction L-methionine + thioredoxin disulfide + H2O
-
 ?

Organism

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

Reaction

Reaction Comment Organism Reaction ID
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin catalytic mechanism, overview Escherichia coli
a
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin catalytic mechanism, overview Neisseria meningitidis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine-(R)-S-oxide + DTT stereospecific reduction Neisseria meningitidis L-methionine + DTT disulfide + H2O
-
 ?
L-methionine-(R)-S-oxide + thioredoxin stereospecific reduction Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
L-methionine-(R)-S-oxide + thioredoxin stereospecific reduction Neisseria meningitidis L-methionine + thioredoxin disulfide + H2O
-
 ?
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

Synonyms Comment Organism
methionine-R-sulfoxide reductase B
-
 Escherichia coli
methionine-R-sulfoxide reductase B
-
 Neisseria meningitidis
MsrB
-
 Escherichia coli
MsrB
-
 Neisseria meningitidis
PilB
-
 Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli
25
-
 assay at Neisseria meningitidis

Cofactor

Cofactor Comment Organism Structure
dithiothreitol can substitute for thioredoxin Neisseria meningitidis
thioredoxin
-
 Escherichia coli
thioredoxin
-
 Neisseria meningitidis