Information on EC 1.8.5.B1 - peptide-methionine (S)-S-oxide reductase (quinone)

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
1.8.5.B1
-
RECOMMENDED NAME
GeneOntology No.
peptide-methionine (S)-S-oxide reductase (quinone)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[protein]-L-methionine + a quinone + H2O = [protein]-L-methionine (R,S)-S-oxide + a quinol
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
peptide-L-methionine:quinone S-oxidoreductase [L-methionine (S)-S-oxide-forming]
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethyl sulfoxide + reduced benzyl viologen
dimethyl sulfide + oxidized benzyl viologen + H2O
show the reaction diagram
P76342 and P76343
-
-
-
?
L-methionine (R)-S-oxide + reduced benzyl viologen
L-methionine + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-S-oxide + reduced benzyl viologen
L-methionine + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
L-methionine S-oxide in chaperone SurA + reduced benzyl viologen
L-methionine in chaperone SurA + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
L-methionine S-oxide in lipoprotein Pal + reduced benzyl viologen
L-methionine in lipoprotein Pal + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
L-methionine sulfoxide + reduced benzyl viologen
L-methionine + oxidized benzyl viologen + H2O
show the reaction diagram
P76342 and P76343
-
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + reduced benzyl viologen
N-acetyl-L-methionine + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
oxidized calmodulin + reduced benzyl viologen
reduced calmodulin + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
tetrahydrothiophene oxide + reduced benzyl viologen
tetrahydrothiophene + oxidized benzyl viologen + H2O
show the reaction diagram
P76342 and P76343
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen
trimethylamine + oxidized benzyl viologen + H2O
show the reaction diagram
P76342 and P76343
-
-
-
?
[protein]-L-methionine + a quinone + H2O
[protein]-L-methionine (R)-S-oxide + a quinol
show the reaction diagram
P76342 and P76343
-
-
-
r
[protein]-L-methionine + a quinone + H2O
[protein]-L-methionine (S)-S-oxide + a quinol
show the reaction diagram
P76342 and P76343
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
-
heme/protein ratio is 2.5. The extinction coefficient value for the oxidized subunit MsrQ form at 412 nm is 51950 per M and cm. For the reduced MsrQ form at 426 and 558 nm, the extinction coefficient values are 69015 per M and cm and 11075 per M and cm, respectively
molybdopterin
P76342 and P76343
presence of one molybdenum molybdopterin not conjugated by an additional nucleotide.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
P76342 and P76343
the molybdenum ion is coordinated by three sulfur ligands, two contributed from the dithiolene sulfurs of the molybdopterin with a Mo-S distance of 2.4 A. The third sulfur ligand is Sgamma of residue C102 at a distance of 2.4 A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
dimethyl sulfoxide
P76342 and P76343
25C, pH not specified in the publication
8 - 25.7
L-methionine (S)-S-oxide
119
L-methionine sulfoxide
P76342 and P76343
25C, pH not specified in the publication
3.8
N-acetyl-L-methionine (S)-sulfoxide
-
pH 7.0, 30C
27.9
tetrahydrothiophene oxide
P76342 and P76343
25C, pH not specified in the publication
-
22 - 46.4
Trimethylamine N-oxide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.83
dimethyl sulfoxide
P76342 and P76343
25C, pH not specified in the publication
25.6
L-methionine sulfoxide
P76342 and P76343
25C, pH not specified in the publication
18.1
tetrahydrothiophene oxide
P76342 and P76343
25C, pH not specified in the publication
-
14.8 - 19
Trimethylamine N-oxide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.403
dimethyl sulfoxide
P76342 and P76343
25C, pH not specified in the publication
0.215
L-methionine sulfoxide
P76342 and P76343
25C, pH not specified in the publication
0.649
tetrahydrothiophene oxide
P76342 and P76343
25C, pH not specified in the publication
-
0.319 - 0.864
Trimethylamine N-oxide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
subunit MsrQ
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
P76342 and P76343
monomer in solution, light scattering analysis
additional information
-
protein physically interacts with flavin reductase Fre
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structures of catalytic subunit YedY in both the molybdenum- and tungsten-substituted forms, five monomers per asymmetric unit
P76342 and P76343
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MsrPQ synthesis is induced by hypochlorous acid
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H151A
-
mutant has aout 57% of the heme content of wild-type
H164A
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mutant has aout 63% of the heme content of wild-type
H91A
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almost complete loss of heme binding