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Literature summary extracted from

  • Vougier, S.; Mary, J.; Dautin, N.; Vinh, J.; Friguet, B.; Ladant, D.
    Essential role of methionine residues in calmodulin binding to Bordetelle pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases (2004), J. Biol. Chem., 279, 30210-30218.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.11 expression of MsrA in Escherichia coli strain BL21(DE3) Rattus norvegicus
1.8.4.12 expression of MsrB in Escherichia coli strain BL21(DE3) Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.11 calmodulin L-methionine-(S)-sulfoxide + thioredoxin Rattus norvegicus MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview calmodulin L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 calmodulin-L-methionine (R)-sulfoxide + thioredoxin Homo sapiens MsrB is specific for the R-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview calmodulin-L-methionine + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Rattus norvegicus
-
-
-
1.8.4.12 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.11 recombinant MsrA from Escherichia coli strain BL21(DE3) Rattus norvegicus
1.8.4.12 recombinant MsrB from Escherichia coli strain BL21(DE3) Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 calmodulin L-methionine-(S)-sulfoxide + thioredoxin MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview Rattus norvegicus calmodulin L-methionine + thioredoxin disulfide
-
 ?
1.8.4.11 calmodulin L-methionine-(S)-sulfoxide + thioredoxin MsrA is specific for the S-form, recombinant human calmodulin, recombinant rat enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview Rattus norvegicus calmodulin L-methionine + thioredoxin disulfide
-
 ?
1.8.4.12 calmodulin-L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview Homo sapiens calmodulin-L-methionine + thioredoxin disulfide + H2O
-
 ?
1.8.4.12 calmodulin-L-methionine (R)-sulfoxide + thioredoxin MsrB is specific for the R-form, recombinant human calmodulin, recombinant human enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview Homo sapiens calmodulin-L-methionine + thioredoxin disulfide + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 MsrA
-
 Rattus norvegicus
1.8.4.11 peptide methionine sulfoxide reductase
-
 Rattus norvegicus
1.8.4.12 MsrB
-
 Homo sapiens
1.8.4.12 peptide methionine sulfoxide reductase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.11 thioredoxin
-
 Rattus norvegicus
1.8.4.12 thioredoxin
-
 Homo sapiens