1.8.4.12: peptide-methionine (R)-S-oxide reductase
This is an abbreviated version!
For detailed information about peptide-methionine (R)-S-oxide reductase, go to the full flat file.
Word Map on EC 1.8.4.12
-
1.8.4.12
-
thioredoxins
-
selenoproteins
-
selenium
-
msrbs
-
neisseria
-
metso
-
trx
-
sulfenic
-
methionine-s-sulfoxide
-
meningitidis
-
thioredoxin-dependent
-
selenoenzyme
-
lincosamides
-
synthesis
-
biotechnology
- 1.8.4.12
- thioredoxins
-
selenoproteins
- selenium
-
msrbs
- neisseria
-
metso
- trx
-
sulfenic
- methionine-s-sulfoxide
- meningitidis
-
thioredoxin-dependent
-
selenoenzyme
-
lincosamides
- synthesis
- biotechnology
Reaction
Synonyms
1-Cys methionine sulfoxide reductase B, 1-Cys MSRB, CBS-1, CBS1, cysteine-containing methionine-R-sulfoxide reductase, LOC100305558, LOC100798757, methionine sulfoxide reductase, methionine sulfoxide reductase B, methionine sulfoxide reductase B1, methionine sulfoxide reductase B2, methionine sulfoxide reductase B3, methionine sulfoxide reductase B8, methionine sulfoxide reductase MsrB3, methionine sulfoxide reductases B, methionine sulfoxide reductases B2, methionine sulphoxide reductase, methionine-R-sulfoxide reductase, methionine-R-sulfoxide reductase B, methionine-R-sulfoxide reductase B2, MetO reductase, More, MSR, MsrA, MsrA/B, MsrA/MsrB, msrAB, MsrABTk, MsrB, MSRB1, MsrB2, MsrB3, MsrB3A, MSRB4, MsrB5, MsrB7, MsrB8, MsrBA, Mxr2, NtMsrB2, OsMSRB5, PaMsrB1, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase type B, PilB, PilB protein, PMSR, Sel-X, selenocysteine-containing methionine-R-sulfoxide reductase, selenoprotein R, SelR, sulindac reductase, TbmsrB, TCDM_06423, YeaA
ECTree
1.8.4.12 peptide-methionine (R)-S-oxide reductaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin
L-methionine methyl ester + thioredoxin disulfide + H2O
-
the affinity of MsrB to acetyl-L-methionine (R)-sulfoxide methyl ester is higher than to L-methionine (R)-sulfoxide
-
-
?
acetyl-L-methionine (R)-sulfoxide N-methyl ester + thioredoxin
L-methionine methyl ester + thioredoxin disulfide + H2O
-
-
-
-
r
calmodulin-L-methionine (R)-S-oxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
MsrBA is able to completely reduce (i.e., repair) MetSO in the calcium regulatory protein calmodulin. The efficient repair is the coordinate activity of the two catalytic domains in the MsrBA fusion protein, which results in a 1 order of magnitude rate enhancement in comparison to those of the individual MsrA or MsrB enzyme alone
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + 1,4-dithioerythritol
dabsyl-L-methionine + 1,4-dithioerythritol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin S12
dabsyl-L-methionine + ?
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
DL-methionine (R)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
-
enzyme MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine-(R)-S-oxide + dithioerythritol
L-methionine + dithioerythritol disulfide + H2O
-
absolute stereospecific reduction, MsrB1 and MsrB2
-
-
?
L-methionine-(R)-S-oxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + dithiothreitol
N-acetyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin
N-acetyl-L-methionine methyl ester + thioredoxin disulfide
-
enzyme MsrB
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
N-acetyl-L-methionine-(R)-S-oxide + glutaredoxin
N-acetyl-L-methionine + glutaredoxin disulfide + H2O
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine-(R)-S-oxide + tryparedoxin
N-acetyl-L-methionine + tryparedoxin disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
-
enzyme reduces L-methionine (R)-sulfoxide of the protein substrate
-
-
?
oxidized chloroplast signal particle protein 43 + ?
reduced chloroplast signal particle protein 43 + ?
-
-
-
-
?
oxidized chloroplast signal particle protein 54 + ?
reduced chloroplast signal particle protein 54 + ?
-
-
-
-
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
peptide-L-methionine + thioredoxin disulfide + H2O
peptide-L-methionine (R)-S-oxide + thioredoxin
the study reveals a mechanism to shuttle oxidizing equivalents from the primary MsrB3 active site toward the enzyme surface, where they would be available for further dithiol-disulfide exchange reactions
-
-
?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
-
-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
racemic (ethanesulfinyl)benzene + dithiothreitol
(ethylsulfanyl)benzene + [(S)-ethanesulfinyl]benzene + dithiothreitol disulfide + H2O
specifically reduces the (R)-enantiomer of methionine sulfoxide to methionine, 93.1% ee
-
-
?
racemic (methanesulfinyl)benzene + dithiothreitol
(methylsulfanyl)benzene + [(S)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
specifically reduces the (R)-enantiomer of methionine sulfoxide to methionine, 96% ee
-
-
?
racemic 1-(methanesulfinyl)-4-methylbenzene + dithiothreitol
1-methyl-4-(methylsulfanyl)benzene + 1-[(S)-methanesulfinyl]-4-methylbenzene + dithiothreitol disulfide + H2O
specifically reduces the (R)-enantiomer of methionine sulfoxide to methionine, 96.4% ee
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, recombinant human calmodulin, recombinant human enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview
-
-
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
isoforms MSRB2 and MSRB4 also show enzyme activity toward protein-based L-methionine (R)-sulfoxide with either dithiothreitol or thioredoxin as reductants, whereas isoform MSRB1 is active only with dithiothreitol
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
thioredoxin f1, thioredoxin m1, thioredoxin m2, thioredoxin m3, thioredoxin m4, thioredoxin x, thioredoxin y1, thioredoxin y2
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
FMsr is specific for the R-isomer
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond. Thioredoxin- and dithiothreitol-dependent activities are approximately equal
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
activity with Escherichia coli thioredoxin, NtMsrB21
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Hsp21 contains 6 methionine residues at positions 49, 52, 55, 59, 62, and 67, about half of the residues are reduced by the enzyme probably due to its stereospecificity
-
-
?
L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
the MsrB-domain of MsrABTk is strictly specific for the reduction of L-methionine (R)-sulfoxide
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of L-methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are peptides and proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Msr is specific for the R-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of the substrate
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
specific substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the (R)-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
PilB shows absolute specificity for the R-form of free and protein-bound methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
specific substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + glutaredoxin
L-methionine + glutaredoxin disulfide + H2O
glutaredoxin from Homo sapiens
-
-
?
L-methionine-(R)-S-oxide + glutaredoxin
L-methionine + glutaredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
glutaredoxin from Homo sapiens
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
absolute stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
absolute stereospecific reduction, isozyme MsrB2, no activity with isozyme MsrB1
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrB accepts free and protein-bound substrates
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
thioredoxin from Leptospira interrogans
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
thioredoxin from Leptospira interrogans
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
L-methionine-(R)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + glutaredoxin
N-acetyl-L-methionine + glutaredoxin disulfide + H2O
glutaredoxin from Homo sapiens
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + glutaredoxin
N-acetyl-L-methionine + glutaredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
glutaredoxin from Homo sapiens
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, preferred substrate of isozyme MsrB2
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
-
-
-
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
highest activity by a membrane bound enzyme form Mem-R,S-Msr, which preferentially reduces the R-substrate form, no activity by enzyme forms fRMsr, fSMsr, low activity by enzyme forms MsrB
-
-
?
trypanothione disulfide + NADPH + H+
trypanothione + NADP+
-
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
?
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, isozyme MsrB1 is not able to reduce free L-methionine-(R)-S-oxide or N-acetyl-L-methionine-(R)-S-oxide, while isozyme MsrB2 prefers protein-bound substrates such as N-acetyl-L-methionine (R)-S-oxide, overview
-
-
?
additional information
?
-
-
the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
-
-
?
additional information
?
-
-
MsrB3 plays an important role in cold tolerance by eliminating methionine sulfoxide and reactive oxygen species that accumulate at the endoplasmic reticulum during cold acclimation
-
-
?
additional information
?
-
-
the CDSP32 thioredoxin forms a heterodimeric complex with MSRB1 through its catalytic cysteine, Cys219, via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
?
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
enzyme provides protection for the cell against oxidative stress
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
?
additional information
?
-
-
MsrB is specific for the R-form of the substrate
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
additional information
?
-
-
substrate specificity of enzyme forms with R-form of free and protein-bound methionine sulfoxide, overview
-
-
?
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates, the membrane-associated isozyme also shows MsrA activity utilizing L-methionine (S)-sulfoxide and N-acetyl-L-methionine (S)-sulfoxide as substrates
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
?
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
?
additional information
?
-
-
the enzyme also exhibits MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
?
additional information
?
-
-
downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
?
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
?
additional information
?
-
-
enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
?
additional information
?
-
-
the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
-
-
?
additional information
?
-
-
the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
-
-
?
additional information
?
-
Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
-
-
?
additional information
?
-
-
Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
-
-
?
additional information
?
-
MsrB3 physically interacts with the sulfenic acid intermediate of these oxidized enzymes to directly form an intermolecular disulfide bond
-
-
?
additional information
?
-
-
methionine-oxidized amyloid fibrils (methionine-oxidized monomer and fibrillar apoC-II) are poor substrates for human methionine sulfoxide reductase B2. At Msr concentrations of more than 0.0005 mM, approximately 90% of monomeric MetO-apoCII is reduced. In contrast, at 0.0005 mM Msr, only 35% of fibrillar MetO-apoC-II is reduced, which increased to only 37% after incubation with a 4fold higher enzyme concentration
-
-
?
additional information
?
-
stereospecificity towards R-methionine sulfoxide
-
-
-
additional information
?
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the enzyme contributes to the ecological performance of Lactobacillus reuteri in gastrointestinal ecosystems together with the high-molecular-mass surface protein Lsp, enzyme expression is induced in vivo
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the enzyme contributes to the ecological performance of Lactobacillus reuteri in gastrointestinal ecosystems together with the high-molecular-mass surface protein Lsp, enzyme expression is induced in vivo
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enzyme provides protection for the cell against oxidative stress
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protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
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recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview, oxidation of 2 essential methionine residues of HIV-2 particles can inactivate the virus and prevent infection of human cells
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the enzyme protect cells against oxidative damage and plays a role in age-related diseases
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roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
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the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
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the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
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enzyme acts on free and protein-bound methionine
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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enzyme acts on free and protein-bound methionine
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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enzyme acts on free and protein-bound methionine
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substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
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the tandem domains of PilB also possess MsrA activity utilizing L-methionine (S)-sulfoxide as substrate, the MsrA domain alone does very poorly utilize the R-isomer
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the tandem domains of PilB also possess MsrA activity utilizing L-methionine (S)-sulfoxide as substrate, the MsrA domain alone does very poorly utilize the R-isomer
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PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
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The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
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the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separately on the enzyme molecule, overview
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the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separatly on the enzyme molecule, overview
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PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
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the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separatly on the enzyme molecule, overview
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enzyme acts on free and protein-bound methionine
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substrate specificities of enzymes, the reduction step is rate-determining
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substrate specificity of MsrB activity, diverse substrates, overview
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the bifunctional enzyme catalyzes both reactions of MsrB or PilB, EC 1.8.4.12, and of MsrA or PilA, EC 1.8.4.11, the catalytic sites for the two different activities are localized separatly on the enzyme molecule, overview
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the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
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the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
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NtMsrB1 shows no activity with dithiothreitol
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NtMsrB1 shows no activity with dithiothreitol
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OsMSRB5 has the ability to reduce free methionine-R-sulfoxide (Met-R-SO) and protein-bound-like Met-SO (dabsyl-Met-SO) to Met and dabsyl-Met, respectively
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
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cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, enzyme activity is not age-related
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additional information
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recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
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additional information
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the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
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additional information
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the enzyme protects cells against oxidative damage and plays a role in age-related diseases
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additional information
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roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, regulation of MsrB expression, overview
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additional information
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the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
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additional information
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the enzyme is essential in protection of the cells against oxidative damage by reactive oxygen species, yeast cell life span analysis of wild-type and mutant cells, the latter either overexpress or lack enzyme activity, overview
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additional information
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potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
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additional information
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enzyme acts on free and protein-bound methionine
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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isoform MSRB1 exhibits no activity in thioredoxin dependent system
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additional information
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enzyme acts on free and protein-bound methionine
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
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additional information
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the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
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additional information
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recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
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additional information
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enzyme acts on free and protein-bound methionine
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additional information
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enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
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additional information
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the reduction step is rate-determining
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