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

BRENDA support

Literature summary for 1.8.5.B1 extracted from

  • Gennaris, A.; Ezraty, B.; Henry, C.; Agrebi, R.; Vergnes, A.; Oheix, E.; Bos, J.; Leverrier, P.; Espinosa, L.; Szewczyk, J.; Vertommen, D.; Iranzo, O.; Collet, J.F.; Barras, F.
    Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons (2015), Nature, 528, 409-412 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.8
-
N-acetyl-L-methionine (S)-sulfoxide pH 7.0, 30┬░C Escherichia coli
8
-
L-methionine (S)-S-oxide pH 7.0, 30┬░C Escherichia coli
25.7
-
L-methionine (S)-S-oxide pH 7.0, 30┬░C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P76342 and P76343 P76342 i.e. catalytic subunit MsrP, P76343 i.e. heme-binding subunit MsrQ
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-methionine (R)-S-oxide + reduced benzyl viologen
-
Escherichia coli L-methionine + oxidized benzyl viologen + H2O
-
?
L-methionine (S)-S-oxide + reduced benzyl viologen
-
Escherichia coli L-methionine + oxidized benzyl viologen + H2O
-
?
L-methionine S-oxide in chaperone SurA + reduced benzyl viologen
-
Escherichia coli L-methionine in chaperone SurA + oxidized benzyl viologen + H2O
-
?
L-methionine S-oxide in lipoprotein Pal + reduced benzyl viologen
-
Escherichia coli L-methionine in lipoprotein Pal + oxidized benzyl viologen + H2O
-
?
additional information MsrPQ is able to reduce both R- and S-diastereoisomers of methionine sulfoxide Escherichia coli ?
-
?
N-acetyl-L-methionine (S)-sulfoxide + reduced benzyl viologen
-
Escherichia coli N-acetyl-L-methionine + oxidized benzyl viologen + H2O
-
?
oxidized calmodulin + reduced benzyl viologen
-
Escherichia coli reduced calmodulin + oxidized benzyl viologen + H2O
-
?

Expression

Organism Comment Expression
Escherichia coli MsrPQ synthesis is induced by hypochlorous acid up

General Information

General Information Comment Organism
physiological function system MsrPQ repairs proteins containing methionine sulfoxide in the bacterial cell envelope rescuing a series of structurally unrelated periplasmic proteins from methionine oxidation. MsrPQ uses electrons from the respiratory chain. MsrPQ is essential for the maintenance of envelope integrity under bleach stress Escherichia coli