1.8.4.11: peptide-methionine (S)-S-oxide reductase This is an abbreviated version! For detailed information about peptide-methionine (S)-S-oxide reductase, go to the full flat file .
Reaction
L-methionine (S)-sulfoxide +
thioredoxin =
L-methionine +
thioredoxin disulfide +
H2O
Synonyms EC 1.8.4.6, ecdysone-induced protein 28/29 kDa, FMsr, LIC_10545, LIC_12978, linmsra1, linmsra2, LMJF_07_1140, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase, methionine sulfoxide reductase A, methionine sulfoxide reductases A, methionine sulfoxide-S-reductase, methionine sulphoxide reductase, methionine sulphoxide reductase A, methionine-S-sulfoxide reductase, MetSO-L12 reductase, More, mrsA, MSR, MSR10, MSR180, MsrA, MSRA-1, MsrA/B, MsrA/MsrB, MsrA1, MSRA2, MSRA4, msrAB, MsrABTk, MsrBA, Peptide Met(O) reductase, peptide methionine S-sulfoxide reductase, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase A, peptide methionine sulfoxide reductase type A, peptide methionine sulphoxide reductase, peptide-methionine (S)-S-oxide reductase, peptide-methionine sulfoxide reductase, PilA, PilB, PilB protein, PMSR, PMSRA, protein-methionine-S-oxide-reductase, sulindac reductase, TbmsrA, TCDM_14270
ECTree
Metals Ions
Metals Ions on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase
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KCl
-
enzyme prefers high ionic strength, activation
Na2SO4
-
enzyme prefers high ionic strength, activation
NaCl
-
enzyme prefers high ionic strength, activation
NaF
-
enzyme prefers high ionic strength, activation
selenium
-
selenocysteine-containing
selenium
-
selenoprotein, has a single selenocysteine residue at the catalytic site, the selenocysteine-containing MsrA exhibits at least a 20fold higher activity than its cysteine mutant form U16C, indicating a critical role of selenocysteine in the catalytic activity of the enzyme
selenium
-
selenocysteine-containing
selenium
-
selenocysteine-containing
selenium
selenocysteine-containing
selenium
-
selenocysteine-containing
selenium
-
selenocysteine-containing
selenium
-
selenocysteine-containing
selenium
-
selenocysteine-containing
additional information
-
the enzyme does not require meal ions for activity, free sulfhydryl content and disulfide bond numbers in wild-type and mutant enzymes, overview
additional information
-
content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview