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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Escherichia coli | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P76342 and P76343 | P76342 i.e. catalytic subunit MsrP, P76343 i.e. heme-binding subunit MsrQ | - |
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 | - |
? |
Organism | Comment | Expression |
---|---|---|
Escherichia coli | MsrPQ synthesis is induced by hypochlorous acid | up |
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 |