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Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase and Organism(s) Bacillus subtilis and UniProt Accession P54155

for references in articles please use BRENDA:EC1.8.4.12
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EC Tree
IUBMB Comments
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide . While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well . The enzyme from some species contains selenocysteine and Zn2+.
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Bacillus subtilis
UNIPROT: P54155
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
methionine sulfoxide reductase, msrb3, msrb1, msrb2, peptide methionine sulfoxide reductase, msra/b, msrab, cbs-1, methionine-r-sulfoxide reductase, methionine sulfoxide reductase b1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methionine sulfoxide reductase
-
-
methionine sulfoxide reductase B
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide [9]. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater [10]. The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well [11]. The enzyme from some species contains selenocysteine and Zn2+.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thioredoxin
additional information
-
DTT can substitute for thioredoxin in vitro
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
selenocysteine-containing
Zn2+
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about 50% of MsrBs binds a zinc atom in opposite direction of the active site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
kinetic mechanism
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging-drop vapor-diffusion method. The crystals belong to the trigonal space group P3, with unit-cell parameters a = b = 136.096, c = 61.918 , and diffracted to 2.5 A resolution
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes msrA, EC 1.8.4.11, and msrB form an operon
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ezraty, B.; Aussel, L.; Barras, F.
Methionine sulfoxide reductases in prokaryotes
Biochim. Biophys. Acta
1703
221-229
2005
Aggregatibacter actinomycetemcomitans, Bacillus subtilis, Dickeya chrysanthemi, Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, Neisseria gonorrhoeae, Neisseria meningitidis, no activity in Aquifex aeolicus, no activity in Thermotoga maritima, Sinorhizobium meliloti, Staphylococcus aureus, Vibrio cholerae serotype O1
Manually annotated by BRENDA team
Boschi-Muller, S.; Olry, A.; Antoine, M.; Branlant, G.
The enzymology and biochemistry of methionine sulfoxide reductases
Biochim. Biophys. Acta
1703
231-238
2005
Bacillus subtilis, Escherichia coli, Neisseria meningitidis, Xanthomonas campestris
Manually annotated by BRENDA team
Kim, H.Y.; Gladyshev, V.N.
Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals
Biochem. J.
407
321-329
2007
Drosophila melanogaster, Neisseria meningitidis, Bacillus subtilis (P54155), Mus musculus (Q8BU85), Homo sapiens (Q8IXL7)
Manually annotated by BRENDA team
You, C.; Sekowska, A.; Francetic, O.; Martin-Verstraete, I.; Wang, Y.; Danchin, A.
Spx mediates oxidative stress regulation of the methionine sulfoxide reductases operon in Bacillus subtilis
BMC Microbiol.
8
128
2008
Bacillus subtilis
Manually annotated by BRENDA team
Park, A.K.; Shin, Y.J.; Moon, J.H.; Kim, Y.K.; Hwang, K.Y.; Chi, Y.M.
Overexpression, purification, and preliminary X-ray crystallographic studies of methionine sulfoxide reductase B from Bacillus subtilis
J. Microbiol. Biotechnol.
18
59-62
2008
Bacillus subtilis
Manually annotated by BRENDA team