Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kauffmann, B.; Aubry, A.; Favier, F.
    The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions (2005), Biochim. Biophys. Acta, 1703, 249-260.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.12 additional information enzyme belongs to the metal-containing MsrB group I Escherichia coli
1.8.4.12 Zn2+ binding by residues at positions 45, 48, 94, and 97, 2 CXXC-motifs, role in catalysis Escherichia coli
1.8.4.12 Zn2+ enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis Pseudomonas aeruginosa
1.8.4.12 Zn2+ enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis Caulobacter vibrioides
1.8.4.12 Zn2+ enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis Synechococcus elongatus

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Bacillus subtilis
-
-
-
1.8.4.11 Bos taurus P54149
-
-
1.8.4.11 Deinococcus radiodurans
-
-
-
1.8.4.11 Escherichia coli P0A744
-
-
1.8.4.11 Mycobacterium tuberculosis P9WJM5
-
-
1.8.4.11 Mycobacterium tuberculosis H37Rv P9WJM5
-
-
1.8.4.11 Neisseria gonorrhoeae P14930
-
-
1.8.4.11 Neisseria meningitidis
-
-
-
1.8.4.11 Solanum lycopersicum
-
-
-
1.8.4.12 Caulobacter vibrioides
-
 enzyme belongs to the metal-containing MsrB group I
-
1.8.4.12 Drosophila melanogaster
-
-
-
1.8.4.12 Escherichia coli
-
 enzyme belongs to the metal-containing MsrB group I
-
1.8.4.12 Neisseria gonorrhoeae P14930 enzyme belongs to the MsrB group IIS
-
1.8.4.12 Neisseria meningitidis
-
 enzyme belongs to the MsrB group IIS
-
1.8.4.12 Pseudomonas aeruginosa
-
 enzyme belongs to the metal-containing MsrB group I
-
1.8.4.12 Synechococcus elongatus
-
 enzyme belongs to the metal-containing MsrB group I
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Bacillus subtilis
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Neisseria meningitidis
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Solanum lycopersicum
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Deinococcus radiodurans
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Neisseria gonorrhoeae
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Bos taurus
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Escherichia coli
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism and structural features, roles of cysteine residues, active site structure Mycobacterium tuberculosis
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview Drosophila melanogaster
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview Escherichia coli
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview Neisseria meningitidis
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview Neisseria gonorrhoeae
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview Pseudomonas aeruginosa
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview Caulobacter vibrioides
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview Synechococcus elongatus
a

Subunits

EC Number Subunits Comment Organism
1.8.4.11 monomer
-
 Escherichia coli
1.8.4.11 More amino acid sequence comparison Neisseria meningitidis
1.8.4.11 More amino acid sequence comparison Solanum lycopersicum
1.8.4.11 More amino acid sequence comparison Deinococcus radiodurans
1.8.4.11 More amino acid sequence comparison, analysis of three-dimensional structures, N-terminal coil, structure comparison to enzymes from other species Escherichia coli
1.8.4.11 More amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species Neisseria gonorrhoeae
1.8.4.11 More amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species Bos taurus
1.8.4.11 More amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species Mycobacterium tuberculosis
1.8.4.11 More amino acid sequence comparison, structure analysis, active enzyme possesses no N-terminal coil before the core Bacillus subtilis
1.8.4.12 More analysis of three-dimensional structure and active site structure Drosophila melanogaster
1.8.4.12 More analysis of three-dimensional structure and active site structure Escherichia coli
1.8.4.12 More analysis of three-dimensional structure and active site structure Neisseria meningitidis
1.8.4.12 More analysis of three-dimensional structure and active site structure Neisseria gonorrhoeae

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 MsrA
-
 Bacillus subtilis
1.8.4.11 MsrA
-
 Neisseria meningitidis
1.8.4.11 MsrA
-
 Solanum lycopersicum
1.8.4.11 MsrA
-
 Deinococcus radiodurans
1.8.4.11 MsrA
-
 Neisseria gonorrhoeae
1.8.4.11 MsrA
-
 Bos taurus
1.8.4.11 MsrA
-
 Escherichia coli
1.8.4.11 MsrA
-
 Mycobacterium tuberculosis
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Bacillus subtilis
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Neisseria meningitidis
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Solanum lycopersicum
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Deinococcus radiodurans
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Neisseria gonorrhoeae
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Bos taurus
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Escherichia coli
1.8.4.11 peptide methionine sulfoxide reductase type A
-
 Mycobacterium tuberculosis
1.8.4.12 MsrB
-
 Drosophila melanogaster
1.8.4.12 MsrB
-
 Escherichia coli
1.8.4.12 MsrB
-
 Pseudomonas aeruginosa
1.8.4.12 MsrB
-
 Neisseria meningitidis
1.8.4.12 MsrB
-
 Caulobacter vibrioides
1.8.4.12 MsrB
-
 Neisseria gonorrhoeae
1.8.4.12 MsrB
-
 Synechococcus elongatus
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Drosophila melanogaster
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Escherichia coli
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Pseudomonas aeruginosa
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Neisseria meningitidis
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Caulobacter vibrioides
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Neisseria gonorrhoeae
1.8.4.12 peptide methionine sulfoxide reductase type B
-
 Synechococcus elongatus