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Literature summary for 1.8.4.11 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
Search for more literature for 1.8.4.11

Cloned(Commentary)

Cloned (Comment) Organism
-
 Alkaliphilus oremlandii

Protein Variants

Protein Variants Comment Organism
C15S monothiol mutant Alkaliphilus oremlandii

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Alkaliphilus oremlandii A8MI53
-
-
Alkaliphilus oremlandii OhILAs A8MI53
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine (S)-sulfoxide + 2 dithiothreitol
-
 Alkaliphilus oremlandii L-methionine + dithiothreitol disulfide + H2O
-
 ?
L-methionine (S)-sulfoxide + 2 dithiothreitol
-
 Alkaliphilus oremlandii OhILAs L-methionine + dithiothreitol disulfide + H2O
-
 ?
L-methionine (S)-sulfoxide + glutaredoxin 2
-
 Alkaliphilus oremlandii L-methionine + glutaredoxin 2 disulfide + H2O
-
 ?
L-methionine (S)-sulfoxide + glutaredoxin 2
-
 Alkaliphilus oremlandii OhILAs L-methionine + glutaredoxin 2 disulfide + H2O
-
 ?
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 ?
-
 ?
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]

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

kcat/KM [mM/s]

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