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Literature summary extracted from

  • Weissbach, H.; Resnick, L.; Brot, N.
    Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage (2005), Biochim. Biophys. Acta, 1703, 203-212.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.8.4.11 synthesis enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs Escherichia coli
1.8.4.11 synthesis enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs Bos taurus
1.8.4.12 synthesis enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs Escherichia coli
1.8.4.13 synthesis enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.11
-
 Bos taurus
1.8.4.11
-
 Escherichia coli
1.8.4.11 gene msr or pilB, DNA sequence determination and analysis Neisseria gonorrhoeae
1.8.4.11 gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, functional overexpression of MsrB from gene msrB or yeaA Escherichia coli
1.8.4.11 gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, overexpression of MsrA leads to increased resistance to reactive oxygen species Bos taurus
1.8.4.11 overexpression of MsrA in T-lymphocytes and PC12 cells leads to increased resistance of the cells to reactive oxygen species and apoptotic death Homo sapiens
1.8.4.11 overexpression of MsrA leads to increased resistance to reactive oxygen species Mus musculus
1.8.4.12 gene msr or pilB, DNA sequence determination and analysis Neisseria gonorrhoeae

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 C52S site-directed mutagenesis, inactive mutant, no protection of the cell against reactive oxygen species Escherichia coli
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells, construction of a msrA/msrB double mutant for detection of additional enzyme form activities Escherichia coli
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells Neisseria gonorrhoeae
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows defective interaction with plant host cells Dickeya chrysanthemi
1.8.4.11 additional information knockout mutants show shortened life span and have neurological lesions Mus musculus
1.8.4.11 additional information transgenic flies overexpressing MsrA show increased extended life span, with extended time of physical and sexual activity, and increased resistance to paraquat Drosophila melanogaster
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells Neisseria meningitidis
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells Helicobacter pylori
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells Haemophilus influenzae
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and is 60% reduced binding to host lung cells Streptococcus pneumoniae
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells Streptococcus gordonii
1.8.4.11 additional information a knockout MsrA mutant strain is sensitive to reactive oxygen species Saccharomyces cerevisiae
1.8.4.12 additional information construction of a msrA/msrB double mutant for detection of additional enzyme form activities Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.11 membrane enzyme form Mem-R,S-Msr Escherichia coli 16020
-
1.8.4.11 microsome calf, sulindac reducing activity Bos taurus
-
-
1.8.4.11 additional information subcellular sulindac reducing activity distribution in calf liver Bos taurus
-
-
1.8.4.12 cytosol Sel-X, a MsrB enzyme variant Mus musculus 5829
-
1.8.4.12 cytosol Sel-X, a MsrB enzyme form variant Saccharomyces cerevisiae 5829
-
1.8.4.12 cytosol Sel-X, a MsrB enzyme form variant Homo sapiens 5829
-
1.8.4.12 cytosol Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf Bos taurus 5829
-
1.8.4.12 membrane enzyme form Mem-R,S-Msr Escherichia coli 16020
-
1.8.4.12 microsome calf, sulindac reducing activity Bos taurus
-
-
1.8.4.12 mitochondrion Sel-X, a MsrB enzyme variant Mus musculus 5739
-
1.8.4.12 mitochondrion Sel-X, a MsrB enzyme form variant Saccharomyces cerevisiae 5739
-
1.8.4.12 mitochondrion Sel-X, a MsrB enzyme form variant Homo sapiens 5739
-
1.8.4.12 mitochondrion Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf Bos taurus 5739
-
1.8.4.12 additional information subcellular sulindac reducing activity distribution in calf liver Bos taurus
-
-
1.8.4.13 membrane enzyme form Mem-R,S-Msr Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.12 selenium selenoprotein Bos taurus
1.8.4.12 selenium selenoprotein Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.4.11 25000
-
 x * 25000, MsrA Drosophila melanogaster
1.8.4.11 25000
-
 x * 25000, MsrA Haemophilus influenzae
1.8.4.11 25000
-
 x * 25000, MsrA Mus musculus
1.8.4.11 25000
-
 x * 25000, MsrA Escherichia coli
1.8.4.11 25000
-
 x * 25000, MsrA Homo sapiens
1.8.4.11 25000
-
 x * 25000, MsrA Saccharomyces cerevisiae
1.8.4.11 25000
-
 x * 25000, MsrA Bos taurus
1.8.4.11 25000
-
 x * 25000, MsrA Neisseria meningitidis
1.8.4.11 25000
-
 x * 25000, MsrA Streptococcus pneumoniae
1.8.4.11 25000
-
 x * 25000, MsrA Helicobacter pylori
1.8.4.11 25000
-
 x * 25000, MsrA Dickeya chrysanthemi
1.8.4.11 25000
-
 x * 25000, MsrA Streptococcus gordonii
1.8.4.11 57000
-
 x * 57000, MsrA/B Neisseria gonorrhoeae
1.8.4.12 57000
-
 x * 57000, MsrA/B Neisseria gonorrhoeae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin Neisseria gonorrhoeae the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin Neisseria meningitidis the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin Helicobacter pylori the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin Haemophilus influenzae the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin Streptococcus pneumoniae the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin Streptococcus gordonii the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Escherichia coli membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Dickeya chrysanthemi MsrA is specific for the S-form, free and protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Mus musculus MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Drosophila melanogaster MsrA is specific for the S-form, free and protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Saccharomyces cerevisiae MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Homo sapiens MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin Bos taurus MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 additional information Escherichia coli the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate ?
-
 ?
1.8.4.11 additional information Dickeya chrysanthemi the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions ?
-
 ?
1.8.4.11 additional information Mus musculus the enzyme protect cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.11 additional information Drosophila melanogaster the enzyme protects cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.11 additional information Saccharomyces cerevisiae the enzyme protects cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.11 additional information Homo sapiens the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease ?
-
 ?
1.8.4.11 additional information Bos taurus the enzyme protects cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.11 additional information Escherichia coli MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant ?
-
 ?
1.8.4.11 additional information Streptococcus pneumoniae MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60% ?
-
 ?
1.8.4.11 additional information Dickeya chrysanthemi MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells ?
-
 ?
1.8.4.11 additional information Mus musculus MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking ?
-
 ?
1.8.4.11 sulindac + thioredoxin Escherichia coli activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.11 sulindac + thioredoxin Bos taurus activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Escherichia coli membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Mus musculus MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Saccharomyces cerevisiae MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Homo sapiens MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin Bos taurus enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin Neisseria gonorrhoeae the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin Neisseria meningitidis the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin Helicobacter pylori the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin Haemophilus influenzae the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin Streptococcus pneumoniae the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin Streptococcus gordonii the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 additional information Escherichia coli the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions ?
-
 ?
1.8.4.12 additional information Mus musculus the enzyme protect cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.12 additional information Saccharomyces cerevisiae the enzyme protects cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.12 additional information Homo sapiens the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease ?
-
 ?
1.8.4.12 additional information Bos taurus the enzyme protects cells against oxidative damage and plays a role in age-related diseases ?
-
 ?
1.8.4.12 sulindac + thioredoxin Escherichia coli activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.12 sulindac + thioredoxin Bos taurus activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.13 L-methionine (S)-sulfoxide + NADPH + H+ Escherichia coli membrane-bound enzyme form Mem-R,S-Msr L-methionine + NADP+ + H2O
-
 ?
1.8.4.13 additional information Escherichia coli the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions ?
-
 ?
1.8.4.13 sulindac + NADPH Escherichia coli activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr sulindac sulfide + NADP+ + H2O activated drug which inhibits cyclooxygenase 1 and 2 and exhibits anti-inflammatory activity ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Bos taurus
-
-
-
1.8.4.11 Dickeya chrysanthemi
-
-
-
1.8.4.11 Drosophila melanogaster
-
-
-
1.8.4.11 Escherichia coli
-
 enzyme forms MsrA and Mem-R,S-Msr
-
1.8.4.11 Escherichia coli
-
-
-
1.8.4.11 Haemophilus influenzae
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.11 Haemophilus influenzae
-
-
-
1.8.4.11 Helicobacter pylori
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.11 Helicobacter pylori
-
-
-
1.8.4.11 Homo sapiens
-
-
-
1.8.4.11 Mus musculus
-
-
-
1.8.4.11 Neisseria gonorrhoeae
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.11 Neisseria gonorrhoeae
-
-
-
1.8.4.11 Neisseria meningitidis
-
 gene msr encodes an enzyme showing both MsrA and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.11 Neisseria meningitidis
-
-
-
1.8.4.11 Saccharomyces cerevisiae
-
-
-
1.8.4.11 Streptococcus gordonii
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.11 Streptococcus gordonii
-
-
-
1.8.4.11 Streptococcus pneumoniae
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.11 Streptococcus pneumoniae
-
-
-
1.8.4.12 Bos taurus
-
 MsrB variants one of which is also called Sel-X
-
1.8.4.12 Escherichia coli
-
 enzyme forms MsrB and Mem-R,S-Msr
-
1.8.4.12 Haemophilus influenzae
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.12 Haemophilus influenzae
-
-
-
1.8.4.12 Helicobacter pylori
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.12 Helicobacter pylori
-
-
-
1.8.4.12 Homo sapiens
-
 MsrB variants one of which is also called Sel-X, encoded by distinct genes, MsrB is a selenoprotein
-
1.8.4.12 Mus musculus
-
 MsrB is a selenoprotein
-
1.8.4.12 Neisseria gonorrhoeae
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.12 Neisseria gonorrhoeae
-
-
-
1.8.4.12 Neisseria meningitidis
-
 gene msr encodes an enzyme showing both MsrA, EC 1.8.4.B2, and MsrB activity
-
1.8.4.12 Neisseria meningitidis
-
-
-
1.8.4.12 Saccharomyces cerevisiae
-
 MsrB variants one of which is also called Sel-X
-
1.8.4.12 Streptococcus gordonii
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.12 Streptococcus gordonii Q9LAM9
-
-
1.8.4.12 Streptococcus pneumoniae
-
 gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
1.8.4.12 Streptococcus pneumoniae
-
-
-
1.8.4.13 Escherichia coli
-
 isozyme Mem-R,S-Msr, bifunctional enzyme
-
1.8.4.13 Escherichia coli
-
-
-
1.8.4.14 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys52 is involved Escherichia coli
a
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys72, Cys218 and Cys228 are involved Bos taurus
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism involving the formation of a sulfenic acid intermediate Escherichia coli
a
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O catalytic mechanism involving the formation of a sulfenic acid intermediate Bos taurus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.4.11 brain calf, sulindac reducing activity Bos taurus
-
1.8.4.11 kidney calf, sulindac reducing activity Bos taurus
-
1.8.4.11 liver calf, sulindac reducing activity Bos taurus
-
1.8.4.11 T-lymphocyte overexpression of MsrA in human T-lymphocyte cells protects them against oxidative stress Homo sapiens
-
1.8.4.12 brain calf, sulindac reducing activity Bos taurus
-
1.8.4.12 kidney calf, sulindac reducing activity Bos taurus
-
1.8.4.12 liver calf, sulindac reducing activity Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.4.11 additional information
-
 activity in mutant strains Escherichia coli
1.8.4.11 additional information
-
 subcellular sulindac reducing activity in calf liver Bos taurus
1.8.4.11 0.00009
-
 enzyme form Mem-R,S-Msr, substrate sulindac Escherichia coli
1.8.4.11 0.00019
-
 enzyme form MsrA, substrate sulindac Escherichia coli
1.8.4.11 0.0018
-
 wild-type strain, substrate L-methionine (S)-sulfoxide Escherichia coli
1.8.4.12 additional information
-
 subcellular sulindac reducing activity in calf liver Bos taurus
1.8.4.12 0.00009
-
 enzyme form Mem-R,S-Msr, substrate sulindac Escherichia coli
1.8.4.12 0.0048
-
 wild-type strain, substrate L-methionine (R)-sulfoxide Escherichia coli
1.8.4.13 0.00009
-
 enzyme form Mem-R,S-Msr, substrate sulindac Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Neisseria gonorrhoeae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Neisseria meningitidis L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Helicobacter pylori L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Haemophilus influenzae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Streptococcus pneumoniae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Streptococcus gordonii L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Neisseria gonorrhoeae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Neisseria meningitidis L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Helicobacter pylori L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Haemophilus influenzae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Streptococcus pneumoniae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Streptococcus gordonii L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, free and protein-bound methionine Dickeya chrysanthemi L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, free and protein-bound methionine Drosophila melanogaster L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine Bos taurus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, there exist MsrA enzyme form variants with specificities for either free or protein-bound methionine Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 L-methionine sulfoxide enkephalin + thioredoxin membrane-bound enzyme form Mem-R,S-Msr Escherichia coli L-methionine enkephalin
-
 ?
1.8.4.11 L-methionine-(S)-S-oxide + thioredoxin
-
 Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 additional information the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate Escherichia coli ?
-
 ?
1.8.4.11 additional information the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Dickeya chrysanthemi ?
-
 ?
1.8.4.11 additional information the enzyme protect cells against oxidative damage and plays a role in age-related diseases Mus musculus ?
-
 ?
1.8.4.11 additional information the enzyme protects cells against oxidative damage and plays a role in age-related diseases Drosophila melanogaster ?
-
 ?
1.8.4.11 additional information the enzyme protects cells against oxidative damage and plays a role in age-related diseases Saccharomyces cerevisiae ?
-
 ?
1.8.4.11 additional information the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease Homo sapiens ?
-
 ?
1.8.4.11 additional information the enzyme protects cells against oxidative damage and plays a role in age-related diseases Bos taurus ?
-
 ?
1.8.4.11 additional information substrate specificity of the different enzyme forms, overview, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation Escherichia coli ?
-
 ?
1.8.4.11 additional information substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview Neisseria gonorrhoeae ?
-
 ?
1.8.4.11 additional information enzyme reduces oxidized methionine residues of the shaker potassium channel, which becomes reversibly inactivated upon oxidation Drosophila melanogaster ?
-
 ?
1.8.4.11 additional information enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation Homo sapiens ?
-
 ?
1.8.4.11 additional information MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant Escherichia coli ?
-
 ?
1.8.4.11 additional information MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60% Streptococcus pneumoniae ?
-
 ?
1.8.4.11 additional information MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells Dickeya chrysanthemi ?
-
 ?
1.8.4.11 additional information MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking Mus musculus ?
-
 ?
1.8.4.11 N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr Escherichia coli N-acetyl-L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Neisseria gonorrhoeae N-acetyl-L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 peptide-L-methionine-(S)-S-oxide + thioredoxin
-
 Escherichia coli peptide-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 sulindac + thioredoxin
-
 Escherichia coli sulindac sulfide + thioredoxin disulfide + H2O
-
 ?
1.8.4.11 sulindac + thioredoxin activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA Escherichia coli sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.11 sulindac + thioredoxin activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr Bos taurus sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.11 sulindac + thioredoxin activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA Escherichia coli sulindac sulfide + thioredoxin disulfide
-
 ?
1.8.4.11 sulindac + thioredoxin activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA Bos taurus sulindac sulfide + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine Mus musculus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine Saccharomyces cerevisiae L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine Homo sapiens L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine Bos taurus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine Bos taurus L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Neisseria gonorrhoeae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Neisseria meningitidis L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Helicobacter pylori L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Haemophilus influenzae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Streptococcus pneumoniae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Streptococcus gordonii L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Neisseria gonorrhoeae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Neisseria meningitidis L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Helicobacter pylori L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Haemophilus influenzae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Streptococcus pneumoniae L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Streptococcus gordonii L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 L-methionine sulfoxide enkephalin + thioredoxin membrane-bound enzyme form Mem-R,S-Msr Escherichia coli L-methionine enkephalin
-
 ?
1.8.4.12 additional information the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Escherichia coli ?
-
 ?
1.8.4.12 additional information the enzyme protect cells against oxidative damage and plays a role in age-related diseases Mus musculus ?
-
 ?
1.8.4.12 additional information the enzyme protects cells against oxidative damage and plays a role in age-related diseases Saccharomyces cerevisiae ?
-
 ?
1.8.4.12 additional information the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease Homo sapiens ?
-
 ?
1.8.4.12 additional information the enzyme protects cells against oxidative damage and plays a role in age-related diseases Bos taurus ?
-
 ?
1.8.4.12 additional information substrate specificity of the different enzyme forms, overview, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate Escherichia coli ?
-
 ?
1.8.4.12 additional information substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview Neisseria gonorrhoeae ?
-
 ?
1.8.4.12 additional information enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation Homo sapiens ?
-
 ?
1.8.4.12 N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr Escherichia coli N-acetyl-L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine Neisseria gonorrhoeae N-acetyl-L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 sulindac + thioredoxin activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA Escherichia coli sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.12 sulindac + thioredoxin activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr Bos taurus sulindac sulfide + thioredoxin disulfide activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity ?
1.8.4.12 sulindac + thioredoxin activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA Escherichia coli sulindac sulfide + thioredoxin disulfide
-
 ?
1.8.4.12 sulindac + thioredoxin activity with membrane-bound enzyme form Mem-R,S-Msr Bos taurus sulindac sulfide + thioredoxin disulfide
-
 ?
1.8.4.13 L-methionine (S)-sulfoxide + NADPH + H+ membrane-bound enzyme form Mem-R,S-Msr Escherichia coli L-methionine + NADP+ + H2O
-
 ?
1.8.4.13 L-methionine sulfoxide enkephalin + NADPH membrane-bound enzyme form Mem-R,S-Msr Escherichia coli L-methionine enkephalin + NADP+ + H2O
-
 ?
1.8.4.13 L-methionine-(S)-S-oxide + thioredoxin
-
 Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.13 additional information the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions Escherichia coli ?
-
 ?
1.8.4.13 additional information substrate specificity, overview, Mem-R,S-Msr can also catalyze the reduction of L-methionine (R)-sulfoxide, EC 1.8.4.14, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation Escherichia coli ?
-
 ?
1.8.4.13 additional information no activity with peptide-L-methionine-(S)-S-oxide Escherichia coli ?
-
 ?
1.8.4.13 N-acetyl-L-methionine (S)-sulfoxide + thioredoxin membrane-bound enzyme form Mem-R,S-Msr Escherichia coli N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.13 sulindac + NADPH activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr Escherichia coli sulindac sulfide + NADP+ + H2O activated drug which inhibits cyclooxygenase 1 and 2 and exhibits anti-inflammatory activity ?
1.8.4.13 sulindac + NADPH activity with membrane-bound enzyme form Mem-R,S-Msr Escherichia coli sulindac sulfide + NADP+ + H2O
-
 ?
1.8.4.14 L-methionine-(R)-S-oxide + thioredoxin
-
 Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.14 additional information no activity with peptide-L-methionine-(R)-S-oxide Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.4.11 ? x * 25000, MsrA Escherichia coli
1.8.4.11 ? x * 57000, MsrA/B Neisseria gonorrhoeae
1.8.4.11 ? x * 25000, MsrA Dickeya chrysanthemi
1.8.4.11 ? x * 25000, MsrA Mus musculus
1.8.4.11 ? x * 25000, MsrA Drosophila melanogaster
1.8.4.11 ? x * 25000, MsrA Neisseria meningitidis
1.8.4.11 ? x * 25000, MsrA Helicobacter pylori
1.8.4.11 ? x * 25000, MsrA Haemophilus influenzae
1.8.4.11 ? x * 25000, MsrA Streptococcus pneumoniae
1.8.4.11 ? x * 25000, MsrA Streptococcus gordonii
1.8.4.11 ? x * 25000, MsrA Saccharomyces cerevisiae
1.8.4.11 ? x * 25000, MsrA Homo sapiens
1.8.4.11 ? x * 25000, MsrA Bos taurus
1.8.4.11 additional information the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity Escherichia coli
1.8.4.11 additional information the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity Bos taurus
1.8.4.12 ? x * 57000, MsrA/B Neisseria gonorrhoeae

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 methionine sulfoxide reductase
-
 Escherichia coli
1.8.4.11 methionine sulfoxide reductase
-
 Neisseria gonorrhoeae
1.8.4.11 methionine sulfoxide reductase
-
 Dickeya chrysanthemi
1.8.4.11 methionine sulfoxide reductase
-
 Mus musculus
1.8.4.11 methionine sulfoxide reductase
-
 Drosophila melanogaster
1.8.4.11 methionine sulfoxide reductase
-
 Neisseria meningitidis
1.8.4.11 methionine sulfoxide reductase
-
 Helicobacter pylori
1.8.4.11 methionine sulfoxide reductase
-
 Haemophilus influenzae
1.8.4.11 methionine sulfoxide reductase
-
 Streptococcus pneumoniae
1.8.4.11 methionine sulfoxide reductase
-
 Streptococcus gordonii
1.8.4.11 methionine sulfoxide reductase
-
 Saccharomyces cerevisiae
1.8.4.11 methionine sulfoxide reductase
-
 Homo sapiens
1.8.4.11 methionine sulfoxide reductase
-
 Bos taurus
1.8.4.11 MSR
-
 Escherichia coli
1.8.4.11 MSR
-
 Neisseria meningitidis
1.8.4.11 MSR
-
 Helicobacter pylori
1.8.4.11 MSR
-
 Haemophilus influenzae
1.8.4.11 MSR
-
 Streptococcus pneumoniae
1.8.4.11 MSR
-
 Streptococcus gordonii
1.8.4.11 MsrA
-
 Escherichia coli
1.8.4.11 MsrA
-
 Dickeya chrysanthemi
1.8.4.11 MsrA
-
 Mus musculus
1.8.4.11 MsrA
-
 Drosophila melanogaster
1.8.4.11 MsrA
-
 Saccharomyces cerevisiae
1.8.4.11 MsrA
-
 Homo sapiens
1.8.4.11 MsrA
-
 Bos taurus
1.8.4.11 MsrA
-
 Streptococcus pneumoniae
1.8.4.11 MsrA/B
-
 Neisseria gonorrhoeae
1.8.4.11 MsrA/B enzyme contains activity of EC 1.8.4.11 and EC 1.8.4.12 Neisseria gonorrhoeae
1.8.4.11 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Neisseria meningitidis
1.8.4.11 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Helicobacter pylori
1.8.4.11 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Haemophilus influenzae
1.8.4.11 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Streptococcus pneumoniae
1.8.4.11 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Streptococcus gordonii
1.8.4.11 PilB
-
 Neisseria gonorrhoeae
1.8.4.12 methionine sulfoxide reductase
-
 Escherichia coli
1.8.4.12 methionine sulfoxide reductase
-
 Neisseria gonorrhoeae
1.8.4.12 methionine sulfoxide reductase
-
 Mus musculus
1.8.4.12 methionine sulfoxide reductase
-
 Neisseria meningitidis
1.8.4.12 methionine sulfoxide reductase
-
 Helicobacter pylori
1.8.4.12 methionine sulfoxide reductase
-
 Haemophilus influenzae
1.8.4.12 methionine sulfoxide reductase
-
 Streptococcus pneumoniae
1.8.4.12 methionine sulfoxide reductase
-
 Streptococcus gordonii
1.8.4.12 methionine sulfoxide reductase
-
 Saccharomyces cerevisiae
1.8.4.12 methionine sulfoxide reductase
-
 Homo sapiens
1.8.4.12 methionine sulfoxide reductase
-
 Bos taurus
1.8.4.12 MSR
-
 Escherichia coli
1.8.4.12 MSR
-
 Neisseria meningitidis
1.8.4.12 MSR
-
 Helicobacter pylori
1.8.4.12 MSR
-
 Haemophilus influenzae
1.8.4.12 MSR
-
 Streptococcus pneumoniae
1.8.4.12 MSR
-
 Streptococcus gordonii
1.8.4.12 MsrA/B
-
 Neisseria gonorrhoeae
1.8.4.12 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Neisseria gonorrhoeae
1.8.4.12 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Neisseria meningitidis
1.8.4.12 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Helicobacter pylori
1.8.4.12 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Haemophilus influenzae
1.8.4.12 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Streptococcus pneumoniae
1.8.4.12 MsrA/B bifunctional enzyme: EC 1.8.4.11/EC 1.8.4.12 Streptococcus gordonii
1.8.4.12 MsrB
-
 Escherichia coli
1.8.4.12 MsrB
-
 Mus musculus
1.8.4.12 MsrB
-
 Saccharomyces cerevisiae
1.8.4.12 MsrB
-
 Homo sapiens
1.8.4.12 MsrB
-
 Bos taurus
1.8.4.12 PilB
-
 Neisseria gonorrhoeae
1.8.4.12 Sel-X
-
 Mus musculus
1.8.4.12 Sel-X
-
 Saccharomyces cerevisiae
1.8.4.12 Sel-X
-
 Homo sapiens
1.8.4.12 Sel-X
-
 Bos taurus
1.8.4.13 fSMsr
-
 Escherichia coli
1.8.4.14 fRMsr
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 additional information no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr Escherichia coli
1.8.4.11 NADPH membrane-bound enzyme form Mem-R,S-Msr Escherichia coli
1.8.4.11 thioredoxin preferred cofactor Escherichia coli
1.8.4.11 thioredoxin
-
 Neisseria gonorrhoeae
1.8.4.11 thioredoxin
-
 Dickeya chrysanthemi
1.8.4.11 thioredoxin
-
 Mus musculus
1.8.4.11 thioredoxin
-
 Drosophila melanogaster
1.8.4.11 thioredoxin
-
 Neisseria meningitidis
1.8.4.11 thioredoxin
-
 Helicobacter pylori
1.8.4.11 thioredoxin
-
 Haemophilus influenzae
1.8.4.11 thioredoxin
-
 Streptococcus pneumoniae
1.8.4.11 thioredoxin
-
 Streptococcus gordonii
1.8.4.11 thioredoxin
-
 Saccharomyces cerevisiae
1.8.4.11 thioredoxin
-
 Homo sapiens
1.8.4.11 thioredoxin
-
 Bos taurus
1.8.4.12 additional information no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr Escherichia coli
1.8.4.12 NADPH membrane-bound enzyme form Mem-R,S-Msr Escherichia coli
1.8.4.12 thioredoxin preferred cofactor Escherichia coli
1.8.4.12 thioredoxin
-
 Neisseria gonorrhoeae
1.8.4.12 thioredoxin
-
 Mus musculus
1.8.4.12 thioredoxin
-
 Neisseria meningitidis
1.8.4.12 thioredoxin
-
 Helicobacter pylori
1.8.4.12 thioredoxin
-
 Haemophilus influenzae
1.8.4.12 thioredoxin
-
 Streptococcus pneumoniae
1.8.4.12 thioredoxin
-
 Streptococcus gordonii
1.8.4.12 thioredoxin
-
 Saccharomyces cerevisiae
1.8.4.12 thioredoxin
-
 Homo sapiens
1.8.4.12 thioredoxin
-
 Bos taurus
1.8.4.13 additional information no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr Escherichia coli
1.8.4.13 NADPH membrane-bound enzyme form Mem-R,S-Msr Escherichia coli