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Literature summary extracted from

  • Kim, M.J.; Jeong, J.; Jeong, J.; Hwang, K.Y.; Lee, K.J.; Kim, H.Y.
    Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin (2015), Biochem. Biophys. Res. Commun., 457, 567-571 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.11
-
 Alkaliphilus oremlandii

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.11 C15S monothiol mutant Alkaliphilus oremlandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.4.11 0.25
-
 glutaredoxin 2 wild-type, pH 7.5, 37°C Alkaliphilus oremlandii
1.8.4.11 0.27
-
 glutaredoxin 2 mutant C15S, pH 7.5, 37°C Alkaliphilus oremlandii
1.8.4.11 0.84
-
 dithiothreitol wild-type, pH 7.5, 37°C Alkaliphilus oremlandii

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Alkaliphilus oremlandii A8MI53
-
-
1.8.4.11 Alkaliphilus oremlandii OhILAs A8MI53
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.11 L-methionine (S)-sulfoxide + 2 dithiothreitol
-
 Alkaliphilus oremlandii L-methionine + dithiothreitol disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + 2 dithiothreitol
-
 Alkaliphilus oremlandii OhILAs L-methionine + dithiothreitol disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + glutaredoxin 2
-
 Alkaliphilus oremlandii L-methionine + glutaredoxin 2 disulfide + H2O
-
 ?
1.8.4.11 L-methionine (S)-sulfoxide + glutaredoxin 2
-
 Alkaliphilus oremlandii OhILAs L-methionine + glutaredoxin 2 disulfide + H2O
-
 ?
1.8.4.11 additional information dunring the regeneration mechanism of MsrA by glutaredoxin, the catalytic Cys16 attacks the sulfoxide moiety of the substrate to form a sulfenic acid intermediate with the concomitant release of the product methionine. The catalytic Cys16 sulfenic acid is then attacked by glutaredoxin, leading to the formation of a complex through a mixed disulfide bond, which is reduced by glutathione, leading to MsrA regeneration Alkaliphilus oremlandii ?
-
 ?
1.8.4.11 additional information dunring the regeneration mechanism of MsrA by glutaredoxin, the catalytic Cys16 attacks the sulfoxide moiety of the substrate to form a sulfenic acid intermediate with the concomitant release of the product methionine. The catalytic Cys16 sulfenic acid is then attacked by glutaredoxin, leading to the formation of a complex through a mixed disulfide bond, which is reduced by glutathione, leading to MsrA regeneration Alkaliphilus oremlandii OhILAs ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.4.11 4.5
-
 glutaredoxin 2 wild-type, pH 7.5, 37°C Alkaliphilus oremlandii
1.8.4.11 4.6
-
 glutaredoxin 2 mutant C15S, pH 7.5, 37°C Alkaliphilus oremlandii
1.8.4.11 10
-
 dithiothreitol wild-type, pH 7.5, 37°C Alkaliphilus oremlandii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.4.11 12
-
 dithiothreitol wild-type, pH 7.5, 37°C Alkaliphilus oremlandii
1.8.4.11 17
-
 glutaredoxin 2 mutant C15S, pH 7.5, 37°C Alkaliphilus oremlandii
1.8.4.11 18
-
 glutaredoxin 2 wild-type, pH 7.5, 37°C Alkaliphilus oremlandii