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Literature summary for 1.8.4.14 extracted from

  • Lin, Z.; Johnson, L.C.; Weissbach, H.; Brot, N.; Lively, M.O.; Lowther, W.T.
    Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function (2007), Proc. Natl. Acad. Sci. USA, 104, 9597-9602.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.4.14

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0098
-
 thioredoxin
-
 Escherichia coli
3.9
-
 L-methionine (R)-S-oxide
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P76270
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine (R)-S-oxide + thioredoxin fRMsr exhibits the highest Met-(R)-O reductase activity when all components of the NADPHTrxR-Trx system are present in the reaction. The enzyme is not able to reduce L-methionine (S)-S-oxide, Met sulfone, dimethyl sulfoxide, or MetO when present in the synthetic peptide NH2-Pro-Thr-Ser-Met-(RS)-O-Glu-His-Val-NH2. Escherichia coli fRMsr is the first GAF domain family member to show enzymatic activity Escherichia coli L-methionine + thioredoxin disulfide + H2O
-
 ?

Synonyms

Synonyms Comment Organism
fRMsr
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.9
-
 L-methionine (R)-S-oxide
-
 Escherichia coli