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

BRENDA support

Literature summary for 1.8.4.11 extracted from

  • Lowther, W.T.; Weissbach, H.; Etienne, F.; Brot, N.; Matthews, B.W.
    The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB (2002), Nat. Struct. Biol., 9, 348-352.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli Neisseria gonorrhoeae

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae P14930 posesses MsrA and MsrB domains; PilB enzyme has 2 catalytic domains showing MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity, respectively
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion Neisseria gonorrhoeae

Reaction

Reaction Comment Organism Reaction ID
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O reaction mechanism, modeling of substrate binding at the active site, Cys72 is involved Neisseria gonorrhoeae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.083
-
purified recombinant MsrA/MsrB tandem domain, substrate L-methionine (S)-sulfoxide Neisseria gonorrhoeae
0.15
-
purified recombinant MsrA domain alone, substrate L-methionine (S)-sulfoxide Neisseria gonorrhoeae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine (S)-sulfoxide + thioredoxin MsrA activity of the tandem domains of PilB, the MsrA domain alone does very poorly utilize the R-isomer Neisseria gonorrhoeae L-methionine + thioredoxin disulfide + H2O
-
?
additional information the tandem domains of PilB also posesses MsrB activity utilizing L-methionine (R)-sulfoxide as substrate, the MsrB domain alone does not utilize the S-isomer Neisseria gonorrhoeae ?
-
?

Subunits

Subunits Comment Organism
More enzyme domain and active site structure, MsrA domain comprises residues 181-362, overview Neisseria gonorrhoeae

Synonyms

Synonyms Comment Organism
methionine sulfoxide reductase
-
Neisseria gonorrhoeae
MsrA
-
Neisseria gonorrhoeae
PilB
-
Neisseria gonorrhoeae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Neisseria gonorrhoeae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.9
-
assay at Neisseria gonorrhoeae

Cofactor

Cofactor Comment Organism Structure
thioredoxin
-
Neisseria gonorrhoeae