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Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase
for references in articles please use BRENDA:EC1.8.4.12
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EC Tree 1 Oxidoreductases
1.8 Acting on a sulfur group of donors
1.8.4 With a disulfide as acceptor
1.8.4.12 peptide-methionine (R)-S-oxide reductase
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+.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.8.4.12
- thioredoxins
-
selenoproteins
- selenium
-
msrbs
- neisseria
-
metso
- trx
-
sulfenic
- methionine-s-sulfoxide
- meningitidis
-
thioredoxin-dependent
-
selenoenzyme
-
lincosamides
- synthesis
- biotechnology
Reaction Schemes
showSynonyms
methionine sulfoxide reductase, msrb3, msrb1, msrb2, peptide methionine sulfoxide reductase, msra/b, msrab, cbs-1, methionine-r-sulfoxide reductase, methionine sulfoxide reductase b1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CBS-1
cysteine-containing methionine-R-sulfoxide reductase
methionine sulfoxide reductase
methionine sulfoxide reductase B
methionine sulfoxide reductase B1
methionine sulfoxide reductase B2
methionine sulfoxide reductase B3
methionine sulfoxide reductases B
methionine-R-sulfoxide reductase
methionine-R-sulfoxide reductase B
MSR
MsrA
MsrA/B
msrAB
MsrB
MSRB1
MsrB2
MsrB3
MsrBA
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bifunctional methionine sulfoxide reductase (EC 1.8.4.11/EC 1.8.4.12)
peptide methionine sulfoxide reductase
peptide methionine sulfoxide reductase type B
PilB
PMSR
Sel-X
selenocysteine-containing methionine-R-sulfoxide reductase
selenoprotein R
SelR
TCDM_06423
YeaA
additional information
methionine sulfoxide reductase B
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-
MsrA
Yarrowia lipolytica YlCW001 v1.0
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-
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MsrB
-
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MsrB
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MsrB
Yarrowia lipolytica YlCW001 v1.0
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-
-
MsrB3
MsrB3 occurs in two forms, MsrB3A and MsrB3B, owing to alternative first exon splicing
additional information
-
the enzyme belongs to the Msr family of enzymes
additional information
-
the enzyme belongs to the Msr family of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
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-
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
selenomethionine is essential for MsrB activity
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
the active site selenocysteine SeC169 is essential for enzyme activity
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, modeling of substrate binding at the active site, Cys444 and Cys495 are involved
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, Cys494 and Cys439 are involved
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
three-step catalytic mechanism, influence of pH on reaction mechanism, overview
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L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
proposed catalytic mechanism of the reductase step of MsrB
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
formation of the MsrB substrate complex leads to an activation of the catalytic Cys-117 characterized by a decreased pKapp of about 2.7 pH units. The catalytic active MsrB form is the Cys117-/His103+ species with a pKapp of 6.6 and 8.3, respectively. His103 and to a lesser extent His100, Asn119, and Thr26 (via a water molecule) participate in the stabilization of the polarized form of the sulfoxide function and of the transition state. Trp65 is essential for the catalytic efficiency of the reductase step by optimizing the position of the substrate in the active site
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: the affinity of MsrB to acetyl-L-methionine (R)-sulfoxide methyl ester is higher than to L-methionine (R)-sulfoxide
Products: -
Products: -
?
acetyl-L-methionine (R)-sulfoxide N-methyl ester + thioredoxin
L-methionine methyl ester + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
r
acetyl-L-methionine-(R)-S-oxide-NHMe + thioredoxin
?
-
Substrates: -
Products: -
Products: -
?
calmodulin-L-methionine (R)-S-oxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + CDSP32
dabsyl-L-methionine + ?
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin C4
?
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin S12
?
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin S12
dabsyl-L-methionine + ?
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + thioredoxin h1
?
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
DL-methionine (R)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
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Substrates: enzyme MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
Products: -
Products: -
?
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
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Substrates: membrane-bound enzyme form Mem-R,S-Msr
Products: -
Products: -
?
L-methionine-(R)-S-oxide + dithioerythritol
L-methionine + dithioerythritol disulfide + H2O
-
Substrates: absolute stereospecific reduction, MsrB1 and MsrB2
Products: -
Products: -
?
L-methionine-(R)-S-oxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + DTT
L-methionine + thioredoxin disulfide + H2O
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Substrates: isozymes MsrB1, MsrB2, and MsrB3
Products: -
Products: -
?
N-acetyl-L-methionine (R)-sulfoxide + dithiothreitol
N-acetyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
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
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Substrates: enzyme MsrB
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
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Substrates: enzyme reduces L-methionine (R)-sulfoxide of the protein substrate
Products: -
Products: -
?
oxidized chloroplast signal particle protein 43 + ?
reduced chloroplast signal particle protein 43 + ?
-
Substrates: -
Products: -
Products: -
?
oxidized chloroplast signal particle protein 54 + ?
reduced chloroplast signal particle protein 54 + ?
-
Substrates: -
Products: -
Products: -
?
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
Substrates: 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
Products: -
Products: -
?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Substrates: 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
Products: -
Products: -
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
-
Substrates: type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
Products: -
Products: -
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Substrates: Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
Products: -
Products: -
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
Products: -
Products: -
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
racemic (ethanesulfinyl)benzene + dithiothreitol
(ethylsulfanyl)benzene + [(S)-ethanesulfinyl]benzene + dithiothreitol disulfide + H2O
K0HZZ3
Substrates: specifically reduces the (R)-enantiomer of methionine sulfoxide to methionine, 93.1% ee
Products: -
Products: -
?
racemic (methanesulfinyl)benzene + dithiothreitol
(methylsulfanyl)benzene + [(S)-methanesulfinyl]benzene + dithiothreitol disulfide + H2O
K0HZZ3
Substrates: specifically reduces the (R)-enantiomer of methionine sulfoxide to methionine, 96% ee
Products: -
Products: -
?
racemic 1-(methanesulfinyl)-4-methylbenzene + dithiothreitol
1-methyl-4-(methylsulfanyl)benzene + 1-[(S)-methanesulfinyl]-4-methylbenzene + dithiothreitol disulfide + H2O
K0HZZ3
Substrates: specifically reduces the (R)-enantiomer of methionine sulfoxide to methionine, 96.4% ee
Products: -
Products: -
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
Substrates: cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
Products: -
Products: -
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
Substrates: cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
Products: -
Products: -
?
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: thioredoxin f1, thioredoxin m1, thioredoxin m2, thioredoxin m3, thioredoxin m4, thioredoxin x, thioredoxin y1, thioredoxin y2
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
Substrates: -
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: FMsr is specific for the R-isomer
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
Substrates: rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond. Thioredoxin- and dithiothreitol-dependent activities are approximately equal
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
Substrates: rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
Substrates: -
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
Substrates: -
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
Substrates: activity with Escherichia coli thioredoxin, NtMsrB21
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
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dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
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dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
Substrates: -
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dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
Substrates: -
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Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Substrates: 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
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Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Substrates: 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
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: -
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L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
Substrates: -
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L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
Substrates: the MsrB-domain of MsrABTk is strictly specific for the reduction of L-methionine (R)-sulfoxide
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L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form of L-methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is absolute specific for the R-form, no activity with the S-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: substrates are peptides and proteins
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: enzyme is involved in repairing of oxidized methionine residues in proteins
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: membrane-bound enzyme form Mem-R,S-Msr
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is specific for the R-isomer, no activity with the S-isomer
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form of the substrate
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: Msr is specific for the R-isomer
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is specific for the R-isomer, no activity with the S-isomer
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: protein-bound methionine residues
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: protein-bound methionine residues
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form of the substrate
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is absolute specific for the R-form, no activity with the S-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is stereospecific for the R-epimer of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: specific substrate
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the (R)-form of the substrate
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: PilB shows absolute specificity for the R-form of free and protein-bound methionine sulfoxide
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: specific substrate
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
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L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
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L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
-
Substrates: -
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L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
-
Substrates: -
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L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
-
Substrates: stereospecific reduction
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L-methionine-(R)-S-oxide + glutaredoxin
L-methionine + glutaredoxin disulfide + H2O
Substrates: glutaredoxin from Homo sapiens
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L-methionine-(R)-S-oxide + glutaredoxin
L-methionine + glutaredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
Substrates: glutaredoxin from Homo sapiens
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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Substrates: substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: absolute stereospecific reduction
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: absolute stereospecific reduction, isozyme MsrB2, no activity with isozyme MsrB1
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
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L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
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Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction, MsrB accepts free and protein-bound substrates
Products: -
Products: -
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: isozymes MsrB1, MsrB2, and MsrB3
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: thioredoxin from Leptospira interrogans
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
Substrates: thioredoxin from Leptospira interrogans
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: isozymes MsrB1, MsrB2, and MsrB3
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
Substrates: -
Products: -
Products: -
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
Products: -
Products: -
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
Substrates: membrane-bound enzyme form Mem-R,S-Msr
Products: -
Products: -
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
Substrates: enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + glutaredoxin
N-acetyl-L-methionine + glutaredoxin disulfide + H2O
Substrates: glutaredoxin from Homo sapiens
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + glutaredoxin
N-acetyl-L-methionine + glutaredoxin disulfide + H2O
Leptospira interrogans Fiocruz L1-130
Substrates: glutaredoxin from Homo sapiens
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: protein-bound substrate, preferred substrate of isozyme MsrB2
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
Substrates: -
Products: -
Products: -
?
N-acetyl-L-methionine-(R)-S-oxide + tryparedoxin I
N-acetyl-L-methionine + tryparedoxin I disulfide + H2O
Substrates: -
Products: -
Products: -
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
Substrates: activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
Substrates: activity with membrane-bound enzyme form Mem-R,S-Msr
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
Substrates: activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
Substrates: activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
Substrates: activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
trypanothione disulfide + NADPH + H+
trypanothione + NADP+
Substrates: -
Products: -
Products: -
?
trypanothione disulfide + NADPH + H+
trypanothione + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has regulatory function in the plant cell
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the reduction step is rate-determining
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related diseases
Products: -
Products: -
?
additional information
?
-
-
Substrates: MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme provides protection for the cell against oxidative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme contributes to resistance against cadmium, physiological role
Products: -
Products: -
?
additional information
?
-
-
Substrates: the reduction step is rate-determining
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: MsrB is specific for the R-form of the substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of enzyme forms with R-form of free and protein-bound methionine sulfoxide, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exhibits MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
Products: -
Products: -
?
additional information
?
-
-
Substrates: downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: MsrB3 physically interacts with the sulfenic acid intermediate of these oxidized enzymes to directly form an intermolecular disulfide bond
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: stereospecificity towards R-methionine sulfoxide
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protect cells against oxidative damage and plays a role in age-related diseases
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme provides protection for the cell against oxidative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
Products: -
Products: -
?
additional information
?
-
-
Substrates: The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificities of enzymes, the reduction step is rate-determining
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of MsrB activity, diverse substrates, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
Products: -
Products: -
?
additional information
?
-
Substrates: the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
Products: -
Products: -
?
additional information
?
-
Substrates: NtMsrB1 shows no activity with dithiothreitol
Products: -
Products: -
?
additional information
?
-
-
Substrates: NtMsrB1 shows no activity with dithiothreitol
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related diseases
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform MSRB1 exhibits no activity in thioredoxin dependent system
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with glutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with glutathione
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with glutathione
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the reduction step is rate-determining
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Substrates: 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
Products: -
Products: -
?
L-methionine (R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Substrates: 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
Products: -
Products: -
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
-
Substrates: type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
Products: -
Products: -
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Substrates: Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
Products: -
Products: -
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
-
Substrates: type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
Products: -
Products: -
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: substrates are peptides and proteins
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: enzyme is involved in repairing of oxidized methionine residues in proteins
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: Msr is specific for the R-isomer
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: protein-bound methionine residues
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: protein-bound methionine residues
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form of the substrate
Products: -
Products: -
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: -
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Substrates: MsrB is stereospecific for the R-epimer of methionine sulfoxide
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB specifically reduces the R-form of methionine sulfoxide
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the (R)-form of the substrate
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form
Products: -
Products: -
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
Products: -
Products: -
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: absolute stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: 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
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: stereospecific reduction
Products: -
Products: -
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
Substrates: activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
Substrates: activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
Products: activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
Products: -
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
Substrates: activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has regulatory function in the plant cell
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related diseases
Products: -
Products: -
?
additional information
?
-
-
Substrates: MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme provides protection for the cell against oxidative stress
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
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additional information
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-
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Substrates: enzyme contributes to resistance against cadmium, physiological role
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additional information
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-
-
Substrates: 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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Substrates: 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
?
-
-
Substrates: the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
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additional information
?
-
-
Substrates: downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
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additional information
?
-
-
Substrates: 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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additional information
?
-
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Substrates: 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
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additional information
?
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Substrates: 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
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additional information
?
-
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Substrates: 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
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additional information
?
-
-
Substrates: 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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additional information
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-
-
Substrates: 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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additional information
?
-
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Substrates: 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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additional information
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-
-
Substrates: the enzyme protect cells against oxidative damage and plays a role in age-related diseases
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additional information
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-
-
Substrates: enzyme provides protection for the cell against oxidative stress
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additional information
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-
-
Substrates: protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
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additional information
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-
-
Substrates: 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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additional information
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-
-
Substrates: 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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additional information
?
-
-
Substrates: 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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-
-
Substrates: enzyme acts on free and protein-bound methionine
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additional information
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-
-
Substrates: 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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additional information
?
-
-
Substrates: The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
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additional information
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-
-
Substrates: 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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additional information
?
-
-
Substrates: enzyme acts on free and protein-bound methionine
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additional information
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-
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Substrates: 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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additional information
?
-
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Substrates: 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
Products: -
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additional information
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-
-
Substrates: 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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-
-
Substrates: 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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-
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Substrates: 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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-
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Substrates: 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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-
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Substrates: 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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-
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Substrates: 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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-
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Substrates: 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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-
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Substrates: 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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-
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Substrates: 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
?
-
-
Substrates: 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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-
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Substrates: the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
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additional information
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-
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Substrates: 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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-
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Substrates: 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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
absolutely dependent on in vitro and in vivo with substrate Hsp21
dithiothreitol
-
MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity
dithiothreitol
-
can act as cofactor only in vitro showing a much higher activity than thioredoxin
thioredoxin
-
natural cofactor, the cofactor can be recycled in vivo by reduction via zinc-containing metallothionein, Zn-MT, after removal of the zinc ion due to its high content of cysteines, mechanism, overview
thioredoxin
-
preferred and natural cofactor, the cofactor can be recycled in vivo by reduction via zinc-containing metallothionein, Zn-MT, after removal of the zinc ion due to its high content of cysteines, mechanism, overview
thioredoxin
-
PilB contains an N-terminal thioredoxin-like domain, the NT domain, fused to the MsrA and MSrB domains, structure overview
additional information
-
DTT can substitute for thioredoxin in vitro
-
additional information
-
DTT can partially substitute for thioredoxin in vitro, low activity
-
additional information
-
DTT can substitute for thioredoxin in vitro
-
additional information
-
no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding
selenium
Zinc
Zn2+
additional information
selenium
-
the selenocysteine-containing Clostridium MsrB form exhibits 100fold higher activity than its Cys-containing form, revealing that selenocysteine provides the catalytic advantage of higher activity. A resolving Cys is required for the thioredoxin-dependent recycling process of the selenocysteine-containing form. Thus, thioredoxin can reduce the selenylsulfide bond, but its Trx-dependent recycling process is much less efficient compared to that for the disulfide bond in the Cys-containing form, demonstrating an obvious catalytic disadvantage
selenium
the presence of the selenium atom in its active site is critical for the catalytic function of this enzyme
selenium
-
selenoprotein. Se status affects Msr (most likely through effects on the selenoprotein MsrB)
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes
Zn2+
-
binding by residues at positions 45, 48, 94, and 97, 2 CXXC-motifs, role in catalysis
Zn2+
-
with Fe2+ in a ratio of 1 mol per mole of enzyme, tight metal binding, the metal binding site is composed of two CXXC motifs located at the opposite side of the active site, role in catalysis and structural stability, overview
Zn2+
-
about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
enzyme belongs to the metal-containing MsrB group I
additional information
-
the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
native isozyme MsrB1 contains selenocysteine, while native isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
isozyme MsrB1 contains selenocysteine, while isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
additional information
-
content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview
additional information
-
wild-type MsrB of Neisseria meningitidis is no metal-binding enzyme, but contains a preformed metal binding site, metal binding to MsrB results in inhibition of binary complex formation between oxidized MsrB and reduced thioredoxin but not between reduced MsrB and substrate, metal content of wild-type and mutant enzymes, overview
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
dimedone
-
binds specifically to the sulfenic acid reaction intermediate
additional information
-
no inhibition by EDTA, 1,10-phenanthroline, and pyridine 2,6-dicarboxylic acid
-
additional information
-
selenium-adequate diet retains MsrB mRNA and protein expression at basal levels
-
additional information
-
enzyme expression decreases during dehardening from 4°C to 22°C of cold-acclimated plants, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
selenium-adequate diet retains MsrB mRNA and protein expression at basal levels
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression of MsrB is induced by dehydration and H2O2
-
additional information
-
heat shock, dehydration, and reactive oxygen species like H2O2 induce the expression of MsrB
-
additional information
-
oxidative stress, e.g. caused by H2O2 up to 0.4 mM, induces enzyme expresssion
-
additional information
-
enzyme is induced under oxidative stress and heat shock
-
additional information
-
MsrB expression is induced by heat shock and alkylating methyl-methanesulfonate treatment
-
additional information
-
starvation induces MsrB expression, also heat treatment and methylmethanesulfonate induce the enzyme
-
additional information
-
48 h exposure to high light at 22°C induces enzyme expression, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
the msrA1-msrB operon is induced by antibiotics
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Anoxia, acidosis and intergenic interactions selectively regulate methionine sulfoxide reductase transcriptions in mouse embryonic stem cells.
Alzheimer Disease
Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain.
Alzheimer Disease
Direct Interaction of Selenoprotein R with Clusterin and Its Possible Role in Alzheimer's Disease.
Alzheimer Disease
Methionine Sulfoxide Reductase-B3 (MsrB3) Protein Associates with Synaptic Vesicles and its Expression Changes in the Hippocampi of Alzheimer's Disease Patients.
Alzheimer Disease
Methionine Sulfoxide Reductase-B3 Risk Allele Implicated in Alzheimer's Disease Associates with Increased Odds for Brain Infarcts.
Alzheimer Disease
Mitochondrial methionine sulfoxide reductase B2 links oxidative stress to Alzheimer's disease-like pathology.
Alzheimer Disease
Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1-42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and function.
Brain Infarction
Methionine Sulfoxide Reductase-B3 Risk Allele Implicated in Alzheimer's Disease Associates with Increased Odds for Brain Infarcts.
Brain Injuries
Methionine Sulfoxide Reductase-B3 Risk Allele Implicated in Alzheimer's Disease Associates with Increased Odds for Brain Infarcts.
Breast Neoplasms
Important roles of multiple Sp1 binding sites and epigenetic modifications in the regulation of the methionine sulfoxide reductase B1 (MsrB1) promoter.
Carcinogenesis
Actin reduction by MsrB2 is a key component of the cytokinetic abscission checkpoint and prevents tetraploidy.
Carcinogenesis
[Expression of methionine sulfoxide reductase in colorectal cancer stem cells in vitro].
Carcinoma
MSRB3 promotes the progression of clear cell renal cell carcinoma via regulating endoplasmic reticulum stress.
Carcinoma, Hepatocellular
Methionine Sulfoxide Reductase B1 Regulates Hepatocellular Carcinoma Cell Proliferation and Invasion via the Mitogen-Activated Protein Kinase Pathway and Epithelial-Mesenchymal Transition.
Carcinoma, Renal Cell
MSRB3 promotes the progression of clear cell renal cell carcinoma via regulating endoplasmic reticulum stress.
Cataract
Effect of blood-retinal barrier development on formation of selenite nuclear cataract in rat.
Cataract
Effects of Sodium Selenite on Oxidative Damage in the Liver, Kidney and Brain in a Selenite Cataract Rat Model.
Cataract
Involvement of MsrB1 in the regulation of redox balance and inhibition of peroxynitrite-induced apoptosis in human lens epithelial cells.
Citrullinemia
Metabolic studies in older mentally retarded patients: significance of metabolic testing and correlation with the clinical phenotype.
Colonic Neoplasms
MsrB3 deficiency induces cancer cell apoptosis through p53-independent and ER stress-dependent pathways.
Colorectal Neoplasms
[Expression of methionine sulfoxide reductase in colorectal cancer stem cells in vitro].
Craniosynostoses
Genome-wide association analysis uncovers variants for reproductive variation across dog breeds and links to domestication.
Deafness
Down-regulation of msrb3 and destruction of normal auditory system development through hair cell apoptosis in zebrafish.
Deafness
Functional null mutations of MSRB3 encoding methionine sulfoxide reductase are associated with human deafness DFNB74.
Deafness
Methionine sulfoxide reductase B3 deficiency causes hearing loss due to stereocilia degeneration and apoptotic cell death in cochlear hair cells.
Dehydration
Peptide-Bound Methionine Sulfoxide (MetO) Levels and MsrB2 Abundance Are Differentially Regulated during the Desiccation Phase in Contrasted Acer Seeds.
Dementia
Methionine Sulfoxide Reductase-B3 (MsrB3) Protein Associates with Synaptic Vesicles and its Expression Changes in the Hippocampi of Alzheimer's Disease Patients.
Dementia
Methionine Sulfoxide Reductase-B3 Risk Allele Implicated in Alzheimer's Disease Associates with Increased Odds for Brain Infarcts.
Diabetes Mellitus
Metabolic studies in older mentally retarded patients: significance of metabolic testing and correlation with the clinical phenotype.
Eye Diseases
Mitochondrial function and redox control in the aging eye: Role of MsrA and other repair systems in cataract and macular degenerations.
Hearing Loss
Functional null mutations of MSRB3 encoding methionine sulfoxide reductase are associated with human deafness DFNB74.
Hearing Loss
Methionine Sulfoxide Reductase A, B1 and B2 Are Likely to Be Involved in the Protection against Oxidative Stress in the Inner Ear.
Hearing Loss
Methionine sulfoxide reductase B3 deficiency causes hearing loss due to stereocilia degeneration and apoptotic cell death in cochlear hair cells.
Hearing Loss
Methionine Sulfoxide Reductase B3-Targeted In Utero Gene Therapy Rescues Hearing Function in a Mouse Model of Congenital Sensorineural Hearing Loss.
Hearing Loss, Sensorineural
Methionine Sulfoxide Reductase B3-Targeted In Utero Gene Therapy Rescues Hearing Function in a Mouse Model of Congenital Sensorineural Hearing Loss.
Infections
A Novel, Molybdenum-Containing Methionine Sulfoxide Reductase Supports Survival of Haemophilus influenzae in an In vivo Model of Infection.
Infections
A strain-specific catalase mutation and mutation of the metal-binding transporter gene mntC attenuate Neisseria gonorrhoeae in vivo but not by increasing susceptibility to oxidative killing by phagocytes.
Infections
Contribution of methionine sulfoxide reductase B (MsrB) to Francisella tularensis infection in mice.
Infections
NIa-pro of Papaya ringspot virus interacts with papaya methionine sulfoxide reductase B1.
Infections
Peptide Methionine Sulfoxide Reductase from Haemophilus influenzae Is Required for Protection against HOCl and Affects the Host Response to Infection.
Influenza, Human
Effects of selenium supplementation on selenoprotein gene expression and response to influenza vaccine challenge: a randomised controlled trial.
Insulin Resistance
Methionine sulfoxide reductase B1 deficiency does not increase high-fat diet-induced insulin resistance in mice.
Insulin Resistance
Methionine sulfoxide reductase B3 deficiency inhibits the development of diet-induced insulin resistance in mice.
Leukemia
Overexpression of methionine sulfoxide reductases A and B2 protects MOLT-4 cells against zinc-induced oxidative stress.
Leukemia
Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage.
Lipoma
NFIB rearrangement in superficial, retroperitoneal, and colonic lipomas with aberrations involving chromosome band 9p22.
Lymphatic Metastasis
Increased expression of methionine sulfoxide reductases B3 is associated with poor prognosis in gastric cancer.
Myositis
The Protein Oxidation Repair Enzyme Methionine Sulfoxide Reductase A Modulates A? Aggregation and Toxicity In Vivo.
Myositis, Inclusion Body
The Protein Oxidation Repair Enzyme Methionine Sulfoxide Reductase A Modulates A? Aggregation and Toxicity In Vivo.
Neoplasm Metastasis
Identification of Key Gene and Pathways for the Prediction of Peritoneal Metastasis of Gastric Cancer by Co-expression Analysis.
Neoplasm Metastasis
Increased expression of methionine sulfoxide reductases B3 is associated with poor prognosis in gastric cancer.
Neoplasms
DNA methylation by dimethyl sulfoxide and methionine sulfoxide triggered by hydroxyl radical and implications for epigenetic modifications.
Neoplasms
Down-regulation of MsrB3 induces cancer cell apoptosis through reactive oxygen species production and intrinsic mitochondrial pathway activation.
Neoplasms
Genetic regulation of longevity and age-associated diseases through the methionine sulfoxide reductase system.
Neoplasms
Increased expression of methionine sulfoxide reductases B3 is associated with poor prognosis in gastric cancer.
Neoplasms
Methionine Sulfoxide Reductase B1 Regulates Hepatocellular Carcinoma Cell Proliferation and Invasion via the Mitogen-Activated Protein Kinase Pathway and Epithelial-Mesenchymal Transition.
Neoplasms
Methionine sulfoxide reductase B1 regulates proliferation and invasion by affecting mitogen-activated protein kinase pathway and epithelial-mesenchymal transition in u2os cells.
Neoplasms
MsrB3 deficiency induces cancer cell apoptosis through p53-independent and ER stress-dependent pathways.
Neoplasms
MSRB3 promotes the progression of clear cell renal cell carcinoma via regulating endoplasmic reticulum stress.
Nervous System Diseases
Dopamine D2 receptor function is compromised in the brain of the methionine sulfoxide reductase A knockout mouse.
Neurodegenerative Diseases
Age-associated neurodegeneration and oxidative damage to lipids, proteins and DNA.
Neurodegenerative Diseases
Genetic regulation of longevity and age-associated diseases through the methionine sulfoxide reductase system.
Obesity
12q14 microduplication: a new clinical entity reciprocal to the microdeletion syndrome?
Obesity
Obesity reduces methionine sulphoxide reductase activity in visceral adipose tissue.
peptide-methionine (r)-s-oxide reductase deficiency
Down-regulation of MsrB3 induces cancer cell apoptosis through reactive oxygen species production and intrinsic mitochondrial pathway activation.
peptide-methionine (r)-s-oxide reductase deficiency
In Vivo Effects of Methionine Sulfoxide Reductase Deficiency in Drosophila melanogaster.
peptide-methionine (r)-s-oxide reductase deficiency
Metabolic studies in older mentally retarded patients: significance of metabolic testing and correlation with the clinical phenotype.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine Sulfoxide Reductase A, B1 and B2 Are Likely to Be Involved in the Protection against Oxidative Stress in the Inner Ear.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine sulfoxide reductase B1 deficiency does not increase high-fat diet-induced insulin resistance in mice.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine sulfoxide reductase B3 deficiency causes hearing loss due to stereocilia degeneration and apoptotic cell death in cochlear hair cells.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine sulfoxide reductase B3 deficiency inhibits cell growth through the activation of p53-p21 and p27 pathways.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine sulfoxide reductase B3 deficiency inhibits the development of diet-induced insulin resistance in mice.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine sulfoxide reductase B3 deficiency stimulates heme oxygenase-1 expression via ROS-dependent and Nrf2 activation pathways.
peptide-methionine (r)-s-oxide reductase deficiency
Methionine Sulfoxide Reductase B3-Targeted In Utero Gene Therapy Rescues Hearing Function in a Mouse Model of Congenital Sensorineural Hearing Loss.
peptide-methionine (r)-s-oxide reductase deficiency
MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form.
peptide-methionine (r)-s-oxide reductase deficiency
MsrB3 deficiency induces cancer cell apoptosis through p53-independent and ER stress-dependent pathways.
peptide-methionine (r)-s-oxide reductase deficiency
Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase.
peptide-methionine (r)-s-oxide reductase deficiency
Selenoprotein MsrB1 deficiency exacerbates acetaminophen-induced hepatotoxicity via increased oxidative damage.
Starvation
Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase b1, reveal a role of selenoproteins in stress resistance.
Stillbirth
Genome-wide association analysis uncovers variants for reproductive variation across dog breeds and links to domestication.
Stomach Neoplasms
Identification of Key Gene and Pathways for the Prediction of Peritoneal Metastasis of Gastric Cancer by Co-expression Analysis.
Stroke
Methionine Sulfoxide Reductase-B3 Risk Allele Implicated in Alzheimer's Disease Associates with Increased Odds for Brain Infarcts.
Tuberculosis
Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates.
Tularemia
Contribution of methionine sulfoxide reductase B (MsrB) to Francisella tularensis infection in mice.
Uterine Cervical Neoplasms
A three-gene novel predictor for improving the prognosis of cervical cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00021
CDSP32
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.0028
glutaredoxin
30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
0.00053
glutaredoxin S12
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.204
trypanothione disulfide
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S/C74S
0.14
acetyl-L-methionine (R)-sulfoxide N-methyl ester
-
pH 5.5, 25°C
-
0.06
dabsyl-L-methionine (R)-S-oxide
mutant Y163A//E165A, pH 7.5, 37°C
0.085
dabsyl-L-methionine (R)-S-oxide
isolated MrsB domain, pH 7.5, 37°C
0.02
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E339A
0.03
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme Y343F
0.05
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, wild-type enzyme
0.05
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E193A/D197A
0.06
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E193A
0.06
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme D197A
0.0091
dithiothreitol
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C
0.03
dithiothreitol
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
0.05
dithiothreitol
mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
2
dithiothreitol
-
MsrB domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide
1.451
L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
2.093
L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
67
L-methionine (R)-sulfoxide
-
MsrB domain of MsrABTk, in the presence of 20 mM dithiothreiol
0.054
L-methionine-(R)-S-oxide
-
recombinant isozyme MsrB2, with dithioerythritol
0.079
L-methionine-(R)-S-oxide
-
recombinant isozyme MsrB1, with dithioerythritol
0.31
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB2 expressed in Escherichia coli
0.5
L-methionine-(R)-S-oxide
-
recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.8
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
1
L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I
1
L-methionine-(R)-S-oxide
30°C, pH 7.0, cosubstrate: glutaredoxin
1.3
L-methionine-(R)-S-oxide
-
recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.049
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
0.049
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
0.043
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: trypanothione, mutant enzyme C72S/C74S
0.045
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C72S
0.047
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C74S
0.2
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I
0.21
N-acetyl-L-methionine-(R)-S-oxide
30°C, pH 7.0, cosubstrate: glutaredoxin
0.0055
thioredoxin
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
0.026
thioredoxin
30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
0.058
thioredoxin
-
MsrB, pH 8.0, 25°C, substrate acetyl-L-methionine (R)-sulfoxide N-methyl ester
0.66
thioredoxin
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
7
thioredoxin
mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
0.0016
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S
-
0.0019
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C74S
-
0.0021
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
-
additional information
additional information
-
stopped flow kinetics, steady-state kinetics
-
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant MsrB
-
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant MsrB
-
additional information
additional information
-
thioredoxin- and DTT-dependent kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
thioredoxin- and DTT-dependent kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
reductase step kinetic parameters of the wild-type and mutated MsrB
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
CDSP32
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.09
dithiothreitol
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0145
glutaredoxin
30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
2.8
L-methionine (R,S)-sulfoxide
-
MsrB activity of PILB, pH 8.0, 25°C
0.0048
trypanothione disulfide
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S/C74S
0.004
dabsyl-L-methionine (R)-S-oxide
isolated MrsB domain, pH 7.5, 37°C
0.025
dabsyl-L-methionine (R)-S-oxide
mutant Y163A//E165A, pH 7.5, 37°C
0.002
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 wild type enzyme, in the presence of 20 mMTris(2-carboxyethyl) phosphine hydrochloride
0.005
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 mutant T132C, in the presence of 20 mM dithioerythritol
0.012
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 mutant T132A, in the presence of 20 mM dithioerythritol
0.014
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB2 wild type enzyme, in the presence of 20 mMTris(2-carboxyethyl) phosphine hydrochloride
0.028
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB2 wild type enzyme, in the presence of 20 mM dithioerythritol
0.045
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E339A
0.047
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 mutant C116S, in the presence of 20 mM dithioerythritol
0.05
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E193A/D197A
0.064
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB2 mutant C134T, in the presence of 20 mM dithioerythritol
0.073
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme D197A
0.075
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 wild type enzyme, in the presence of 20 mM dithioerythritol
0.078
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E193A
0.087
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme Y343F
0.157
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, wild-type enzyme
0.17
glutaredoxin S12
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.01
L-methionine (R)-sulfoxide
-
in vitro, substrate free L-methionine (R)-sulfoxide
0.13
L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
2.86
L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
0.002
L-methionine-(R)-S-oxide
-
recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.002
L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, wild-type enzyme
0.0076
L-methionine-(R)-S-oxide
30°C, pH 7.0, cosubstrate: glutaredoxin
0.02
L-methionine-(R)-S-oxide
-
recombinant isozyme MsrB2, with dithioerythritol
0.07
L-methionine-(R)-S-oxide
-
recombinant isozyme MsrB1, with dithioerythritol
0.22
L-methionine-(R)-S-oxide
-
recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.46
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB2 expressed in Escherichia coli
0.83
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
0.24
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
2.04
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
0.00052
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C72S
0.0016
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C74S
0.0023
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: trypanothione, mutant enzyme C72S/C74S
0.0048
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, wild-type enzyme
0.014
N-acetyl-L-methionine-(R)-S-oxide
30°C, pH 7.0, cosubstrate: glutaredoxin
0.0043
thioredoxin
30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
0.0056
thioredoxin
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, wild-type enzyme
0.00067
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S
-
0.0025
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C74S
-
0.00583
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, wild-type enzyme
-
additional information
additional information
-
reductase step kinetic parameters of the wild-type and mutated MsrB
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
dithiothreitol
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C
5.2
glutaredoxin
30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
0.024
trypanothione disulfide
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S/C74S
0.005
dabsyl-L-methionine (R)-S-oxide
isolated MrsB domain, pH 7.5, 37°C
0.42
dabsyl-L-methionine (R)-S-oxide
mutant Y163A//E165A, pH 7.5, 37°C
1
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E193A/D197A
1.22
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme D197A
1.3
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E193A
2.25
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme E339A
2.88
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, mutant enzyme Y343F
3.1
dabsyl-L-methionine (R)-sulfoxide
pH 7.5, 37°C, wild-type enzyme
0.09
L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
1.4
L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
0.002
L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I
0.0076
L-methionine-(R)-S-oxide
30°C, pH 7.0, cosubstrate: glutaredoxin
5
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
42
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
0.011
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C72S
0.024
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I
0.034
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C74S
0.054
N-acetyl-L-methionine-(R)-S-oxide
pH 7.5, 30°C, cosubstrate: trypanothione, mutant enzyme C72S/C74S
0.067
N-acetyl-L-methionine-(R)-S-oxide
30°C, pH 7.0, cosubstrate: glutaredoxin
0.17
thioredoxin
30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
1.03
thioredoxin
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
0.417
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S
-
1.307
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C74S
-
2.778
tryparedoxin I
pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000029
-
wild-type strain RN450, substrate L-methionine (R)-sulfoxide
0.00003
-
msrA2 knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.000046
-
purified recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.0012
-
msrA1 knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.0015
-
msrA1/msrA2 double knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.002
-
purified recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and DTT
0.01
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.023
0.045
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.075
purified recombinant MsrA/MsrB tandem domain, substrate L-methionine (R)-sulfoxide
0.085
purified recombinant CBS-1, substrate L-methionine (R)-sulfoxide
0.11
0.128
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.17
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and DTT
0.173
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.386
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
0.452
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
additional information
0.023
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.11
purified recombinant MsrB domain alone, substrate L-methionine (R)-sulfoxide
additional information
-
thioredoxin- and DTT-dependent activities of mutant enzymes, overview
additional information
-
tissue specific activity, activity in tissues of MsrA-deficient mutant mice
additional information
-
thioredoxin- and DTT-dependent activities of mutant enzymes, overview
additional information
-
recombinant activity in overexpressing yeast cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
7.4
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional methionine sulfoxide reductase AB, cf. EC 1.8.1.11
UniProt
brenda
bifunctional methionine sulfoxide reductase AB, cf. EC 1.8.1.11
UniProt
brenda
enzyme forms MsrB, and other enzyme forms, e.g. Mem-R,S-Msr, overview
-
-
brenda
gene msrB, enzyme SelR which is a selenoprotein, enzyme is organized in a fusion protein together with MsrA, EC 1.8.4.B2
-
-
brenda
wild-type strain MC1061, isozyme MsrB and a membrane-associated isozyme
-
-
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
brenda
enzyme forms MsrA and MsrB are fused together forming a single protein termed Msr
-
-
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
brenda
MsrB variants one of which is also called Sel-X, encoded by distinct genes, MsrB is a selenoprotein
-
-
brenda
enzyme contains MsrA and MsrB domains; PilB enzyme has 2 catalytic domains showing MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity, respectively, the MsrB domain contains a selenomethionine at position 39
SwissProt
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
brenda
2 structurally unrelated enzymes with different stereospecificity, MsrA, EC 1.8.4.B2, and MsrB, which occur in different variants, but are located on one protein
-
-
brenda
enzyme PILB, a peptide methionine sulfoxide reductase with 2 subdomains MsrA and MsrB with opposite stereospecificity, MsrA activity belongs to EC 1.8.4.B2
-
-
brenda
gene msr encodes an enzyme showing both MsrA, EC 1.8.4.B2, and MsrB activity
-
-
brenda
PilB enzyme has 2 catalytic domains showing MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity, respectively
-
-
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
brenda
2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MsrB1 is highly expressed in HCC tissues and its expression correlates with the prognoses of patients with HCC after hepatectomy
brenda
-
epithelia and fibers, isozymes MsrB1 or selenoprotein R, MsrB2 or CBS-1, and MsrB3, differential expression patterns of isozymes, overview
brenda
additional information
-
enzyme form MsrB2 is detectable in the embryonic axes and in cotyledons
brenda
highly expressed in the epidermis of adult workers
brenda
expression/activities of MSRA and MSRB are significantly decreased in the epidermis of patients with vitiligo compared to healthy controls
brenda
-
cell line WI-38, young and old cells, enzyme expression pattern during cell development, senescent cells show decreased enzyme expression and activity
brenda
-
marginal Zn deficiency has little effect on Msr in liver and kidney. Msr activity is significantly reduced by Se deficiency
brenda
-
MsrB1 is present in the renal Mg2+-transporting distal convoluted tubules
brenda
expression levels are the highest in leaves, followed by roots, and lowest in seeds and seed pods. Among the MsrB isoforms, transcripts of MSRB1 in the leaves are the highest
brenda
expression levels are the highest in leaves, followed by roots, and lowest in seeds and seed pods. Among the MsrB isoforms, transcripts of MSRB5 in the leaves are the lowest
brenda
-
marginal Zn deficiency has little effect on Msr in liver and kidney. Msr activity is significantly reduced by Se deficiency
brenda
control and stably overexpressing MsrA (from rat) and MsrB2 (from human). Zinc treatment has a pro-antioxidant effect in MOLT-4 cells by positively modulating the activity of the Msr enzymes. Overexpression of the Msr enzymes, due to their antioxidant properties, counteracts the pro-oxidant effects of zinc treatment, which lead to a cellular protection against protein oxidative damage and cell death, by reducing the production of reactive oxygen species
brenda
overexpression of human methionine sulfoxide reductase B2 in mitochondria of acute T-lymphoblastic leukemia MOLT-4 cell line, in which methionine sulfoxide reductase A is missing
brenda
-
ethionine sulfoxide reductase B2 is highly expressed in the retina, in the monkey retina MSRB2 localizes to the ganglion cell layer, the outer plexiform layer and the retinal pigment epithelium
brenda
expression levels are the highest in leaves, followed by roots, and lowest in seeds and seed pods
brenda
-
enzyme form MsrB2 is detectable in the embryonic axes and in cotyledons. A greater amount of MsrB2 is revealed in embryonic axes at the 14th weeks after flowering (WAF). The two redox MsrB2 forms (two different redox forms with molecular masses of 12000 Da and 13000 Da) are revealed in cotyledons at the 12th-16th WAF. During later stages, the 12000 Da form is hardly detectable in the cotyledons, and the protein abundance decreases. Higher abundance of reduced MsrB2 during the first stages of seed formation
brenda
-
in embryonic axes, detectable amounts of the enzyme form MsrB1 are revealed at the 13th weeks after flowering (WAF). In cotyledons, MsrB1 is detectable one week earlier, and the protein is present in larger amounts throughout the whole development and during the maturation phase. Linear increase in the amount of the enzyme form MsrB1 at the 12th-17th WAF in cotyledons. Increased abundance of enzyme form MsrB1 at the 15th-17th WAF in embryonic axes. MsrB2 is detectable in the embryonic axes
brenda
the enzyme is detected in cortical cells and the outer area of the vascular cylinder of the embryonic axes as well as in the epidermis and parenchyma cells of cotyledons. The abundances of MsrB1 and MsrB2 decreased during long-term storage
brenda
expression levels are the highest in leaves, followed by roots, and lowest in seeds and seed pods
brenda
chronic sun-exposure would result in a decreased expression of two main components of the methionine sulfoxide reductase system, MsrA and MsrB2
brenda
-
embryonic fibroblast, activity during development: downregulation during replicative senescence
brenda
-
fibroblast, young and old cells, enzyme expression pattern during cell development
brenda
MsrB2 is downregulated during replicative senescence of WI-38 human fibroblasts
brenda
additional information
-
high expression level of the plastidic isozyme pPMSR in photosynthetic active tissue
brenda
additional information
-
tissue distribution, main expression of CBS1 in muscle tissues, overview
brenda
additional information
-
enzyme expression level and methionine sulfoxide content in fibroblasts during development, overview
brenda
additional information
-
tissue-specific expression of MsrB isozymes, overview
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additional information
OsMSRB5 is mainly expressed in leaves, with low transcriptional levels of OsMSRB5 observed in seeds, stems, and roots
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additional information
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presence of MsrABTk is greater in Thermococcus kodakaraensis cells grown at suboptimal temperatures (60 to 70°C) and could not be detected at 80 to 90°C. The amount of intracellular MsrABTk protein increases with exposure to higher dissolved oxygen levels, but only at suboptimal growth temperatures
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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secretion of MsrA, EC 1.8.4.11, and MsrB fused together
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brenda
additional information
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plastidic isozymes MsrB1 and MsrB2, analysis of subcellular localization
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sequence lacks any signal-peptide motif necessary for the protein transport across membranes
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sequence lacks any signal-peptide motif necessary for the protein transport across membranes
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dual localization, both in cytoplasm and periplasm
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Leptospira interrogans Fiocruz L1-130
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dual localization, both in cytoplasm and periplasm
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Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf
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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
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sequence contains a a putative transmembrane domain and an ER-specific retention signal
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sequence contains a a putative transmembrane domain and an ER-specific retention signal
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MsrB3A contains an endoplasmic reticulum signal peptide at the N-terminus and an endoplasmic reticulum retention signal at the C-terminus, and is targeted to the endoplasmic reticulum
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two splice variants of the enzyme (Msr B3) that differ in their N-terminal signal sequence, which directs the protein to either the endoplasmic reticulum (ER) or mitochondria
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MsrB3 has consecutive endoplasmic reticulum and mitochondrial targeting signals at the N-terminus. This protein is targeted to the endoplasmic reticulum, and the function of the mitochondrial signal appears to be masked by the endoplasmic reticulum signal peptide
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Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf
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sequence contains a mitochondrial signal sequence
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sequence contains a mitochondrial signal sequence
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MsrB3B contains a different signal peptide at the N-terminus and is targeted to mitochondria
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two splice variants of the enzyme (Msr B3) that differ in their N-terminal signal sequence, which directs the protein to either the endoplasmic reticulum (ER) or mitochondria
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sequence forms a monopartite nuclear localization signal
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sequence forms a monopartite nuclear localization signal
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dual localization, both in cytoplasm and periplasm
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Leptospira interrogans Fiocruz L1-130
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dual localization, both in cytoplasm and periplasm
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brenda
additional information
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subcellular sulindac reducing activity distribution in calf liver
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brenda
additional information
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subcellular targeting is determined by alternative splicing
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brenda
additional information
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subcellular targeting is determined by alternative splicing
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brenda
additional information
subcellular localization analysis, no localization of MsrB3 in the mitochondria
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additional information
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subcellular localization analysis, no localization of MsrB3 in the mitochondria
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Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
phylogenetic analysis suggested that OsMSRB5 is a B-type MSR with similar structure to MSRBs of other species, and belongs to 2-Cys MSRB
malfunction
metabolism
physiological function
additional information
drug target
the enzyme (MsrB1) may be a therapeutic target with respect to the treatment of hepatocellular carcinoma
drug target
MsrB1-dependent reduction of oxidized methionine in proteins may be a regulatory event underlying immunity and inflammatory disease, and a novel target for clinical applications
malfunction
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the concomitant absence of both protein isoforms MSRB1 and MSRB2 results in a reduced growth for plants cultivated under high light or low temperature, double mutant lines restored for MSRB2 expression display no phenotype, the absence of plastidial MSRBs is associated with an increased chlorophyll a/b ratio, a reduced content of Lhca1 and Lhcb1 proteins, and an impaired photosynthetic performance
malfunction
-
deficiency in MsrB enzyme reduces the level of Enterococcus faecalis virulence in a systemic and urinary tract infection model
malfunction
loss-of-function studies of MsrB2 using virus-induced gene silencing in pepper plants (cultivar Early Calwonder-30R) result in accelerated cell death from an incompatible bacterial pathogen, Xanthomonas axonopodis pv vesicatoria race 1, and enhanced susceptibility to a compatible bacterial pathogen, virulent Xanthomonas axonopodis pv vesicatoria race 3. Suppression of CaMsrB2 increased the production of reactive oxygen species, which in turn results in the acceleration of cell death via accumulation of reactive oxygen species
malfunction
-
the msrB mutant MSDELTAmsrB exhibits significantly lower intracellular survival than its wild type counterpart and shows no sensitivity to oxidants in vitro. The msrA/B double mutant (MSDELTAmsrA/B) exhibits a phenotype similar to that of msrA mutant in terms of both intracellular survival and sensitivity to oxidants
malfunction
-
knockdown of MsrB3A in mammalian cells leads to a significant decrease in the resistance to thapsigargin-induced endoplasmic reticulum (ER) stress, but had no effects on the resistance to either dithiothreitol- or tunicamycin-induced ER stress
malfunction
-
cytosolic MsrB7 and MsrB8 knockdown lines are sensitive to oxidative stress
malfunction
MsrB1 knockdown effectively inhibits tumor growth. MsrB1 knockdown reduces hepatocellular carcinoma cell migration and invasion in a transwell assay through inhibition of cytoskeletal rearrangement and spread
malfunction
genetic ablation of MsrB1 doesd not preclude LPS-induced intracellular signaling in macrophages, but results in attenuated induction of antiinflammatory cytokines, such as interleukin (IL)-10 and the IL-1 receptor antagonist
malfunction
-
deficiency in MsrB enzyme reduces the level of Enterococcus faecalis virulence in a systemic and urinary tract infection model
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metabolism
epimastigotes overexpressing the enzyme (MSRB) exhibit inhibition of the metacyclogenesis process
metabolism
reactive oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate proteins. Methionine sulfoxide reductase (MSR) enzyme converts MetSO back to the reduced form and thereby detoxifies the effect of ROS
metabolism
-
epimastigotes overexpressing the enzyme (MSRB) exhibit inhibition of the metacyclogenesis process
-
physiological function
-
both single and double inactivation mutants are viable, but more sensitive to oxidative stress agents as hydrogen peroxide, paraquat, and ultraviolet light. These strains also accumulate more carbonylated proteins when exposed to hydrogen peroxide indicating that MsrB is an active player in the protection of the cellular proteins from oxidative stress damage
physiological function
-
MsrB is important for the oxidative stress response, macrophage survival, and persistent infection with Enterococcus faecalis
physiological function
-
MsrB1 recovers transient receptor potential melastatin type 6 channel activity by reducing the oxidation of Met1755 and can thereby function as a modulator of transient receptor potential melastatin type 6 during oxidative stress
physiological function
-
oxidative stress can lead to oxidation of methionine residues, which are repaired by MsrB1
physiological function
MsrB2 is a defense regulator against oxidative stress and pathogen attack, MsrB2 causes enhanced resistance to Phytophthora capsici and Phytophthora infestans
physiological function
-
MsrB of plays only a limited role in resisting intracellular and in vitro reactive oxygen intermediates
physiological function
-
MSRB2 plays an important function in protecting cones from multiple type of oxidative stress and is critical in preserving central vision
physiological function
-
MSRB2 plays an important function in protecting cones from multiple type of oxidative stress and is critical in preserving central vision
physiological function
-
neuronal expression of isoform MsrB3A renders Drosophilaflies resistant to oxidative stress. These flies also show significantly enhanced cold (4°C) and heat (37°C) tolerance. Expression of isoform MsrB3A in the whole body and nervous system extends the lifespan of fruit flies at 29°C by 43-50% and 12-37%, respectively. Additionally, isoform MsrB3A overexpression significantly delays the age-related decline in locomotor activity and fecundity
physiological function
-
methionine sulfoxide reductase B3 protects from endoplasmic reticulum (ER) stress. Drosophila flies overexpressing human MsrB3A exhibit significantly increased resistance to ER stress induced by dithiothreitol (cell viability is enhanced by 40% and 30% in the treatment of 0.5 and 1 mM dithiothreitol, respectively). These flies also show slightly enhanced resistance to tunicamycin-induced ER stress. The enzyme may be involved in the regulation of ER homeostasis. Overexpression of MsrB3A in mammalian cells increases resistance to dithiothreitol- and thapsigargin-induced endoplasmic reticulum (ER) stresses. However, MsrB3A overexpression has no effect on the resistance to tunicamycin-induced ER stress
physiological function
-
isoforms MsrB7 and MsrB8 play an important role in defense against oxidative stress. Transgenic plants overexpressing MsrB7 or MsrB8 are viable and survive after methyl viologen and H2O2 treatment. Arabidopsis plants overexpressing isoforms MsrB7/B8 have shorter roots
physiological function
-
the MSRB1 gene plays a critical role in protecting against oxidative stress
physiological function
in the presence of 0.1 mM L-methionine-(R,S)-sulfoxide, Mxr2 overexpressing cells grow normally while the growth of control cells is almost arrested. Overexpressing cells exhibit enhanced growth in presence of hydrogen peroxide, superoxide radical-generating menadione, sodium nitroprusside, and cadmium, when compared with the control cells. They show better growth at 37°C and contain less reactive oxygen species and higher total glutathione levels than the control cells
physiological function
MsrB-overexpressing cell exhibit better growth in presence of cadmium chloride than controls. Both groups contain enhanced reactive oxygen and nitric oxide levels in the presence of Cd, levels are significantly lower in the overexpressing cells. Overexpressing cells possess higher total glutathione levels and a greater reduced/oxidized glutathione ratio than controls
physiological function
methionine sulfoxide reductase A (MsrA, EC 1.8.1.11) and B (MsrB, EC 1.8.1.12) are present as a fusion form. The catalytic efficiency of both MsrA and MsrB increases after fusion of the domains and the linker region (iloop) that connects MsrA and MsrB is required for the higher catalytic efficiency of the fusion protein. The iloop mainly interacts with MsrB via hydrogen bonds. The iloop-MsrB interactions are critical to MsrB and MsrA activities
physiological function
an mMrB mutant exhibits decreased in vitro growth, exogenous oxidative stress resistance and intracellular growth in macrophages. A double mutant lacking both MsrA, EC 1.8.1.11, and MsrB exhibits the same characteristics as the MsrB mutant. The bacterial count of the MsrB mutant is significantly lower than that of the wild-type strain in the liver and spleen of mice
physiological function
-
Escherichia coli cells harboring MSRB3 display increased viability under H2O2 stress
physiological function
-
methionine sulfoxide reductase B can regulate the redox state and activity of ascorbate peroxidase, a key antioxidant enzyme that is involved in diverse developmental and physiological process and stress responses by scavenging H2O2 in plants
physiological function
-
MsrB2 is associated with the acquisition of desiccation tolerance
physiological function
methionine sulfoxide reductase B1 regulates hepatocellular carcinoma cell proliferation and invasion via the mitogen-activated protein kinase pathway and epithelial-mesenchymal transition
physiological function
the enzyme (MsrB3) is able to function in vivo to complement a bacterial strain deficient in endogenous Msr
physiological function
-
to combat the deleterious effects that oxidation of the sulfur atom in methionine to sulfoxide may bring, aerobic cells express repair pathways involving methionine sulfoxide reductases (MSRs) to reverse the deleterious reaction
physiological function
methionine sulfoxide reductase B1 (MsrB1) protects the photosynthetic apparatus from oxidative damage by scavenging reactive oxygen species to repair Met-oxidized proteins in response to abiotic stresses and biotic attack
physiological function
the enzyme is involved in the regulation of many developmental processes and stress responses
physiological function
methionine sulfoxide reductase B8 influences stress-induced cell death and effector-triggered immunity
physiological function
the enzyme (MsrB1) controls immune responses by promoting anti-inflammatory cytokine expression in macrophages
physiological function
methionine-R-sulfoxide reductase OsMSRB5 is required for rice defense against copper toxicity
physiological function
MsrB is implicated in human lens epithelial cell viability
physiological function
-
MsrB is important for the oxidative stress response, macrophage survival, and persistent infection with Enterococcus faecalis
-
physiological function
-
methionine sulfoxide reductase A (MsrA, EC 1.8.1.11) and B (MsrB, EC 1.8.1.12) are present as a fusion form. The catalytic efficiency of both MsrA and MsrB increases after fusion of the domains and the linker region (iloop) that connects MsrA and MsrB is required for the higher catalytic efficiency of the fusion protein. The iloop mainly interacts with MsrB via hydrogen bonds. The iloop-MsrB interactions are critical to MsrB and MsrA activities
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additional information
the enzyme harbors two CXXC motifs (M1 and M3) including four non-redox-active cysteines, as well as XCGWP (M2) and RXCXNS (M4) conserved domains
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Pichia kudriavzevii CBS573
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Yarrowia lipolytica CLIB 89 (W29)
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Absidia repens NRRL 1336
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Crucibulum laeve CBS 166.37 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Dendrothele bispora CBS 962.96 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Tulasnella calospora AL13/4D v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Ramaria rubella UT-36052-T v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Coprinellus micaceus FP101781 v2.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Hortaea werneckii EXF-2000 M0 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Yarrowia lipolytica FKP355 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Yarrowia lipolytica YB419 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Yarrowia lipolytica YB420 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Yarrowia lipolytica YB566 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Yarrowia lipolytica YB567 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Yarrowia lipolytica YlCW001 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
-
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Smittium mucronatum ALG-7-W6
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Smittium culicis GSMNP
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Coniochaeta sp. 2T2.1 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
-
survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Yarrowia lipolytica YB392 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
-
additional information
Gonapodya prolifera v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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Show AA Sequence and Transmembrane Helices (28160 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
15000
16374
-
x * 16374, about, recombinant wild-type MsrB domain, mass spectrometry
16860
17000
21000
5000
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MsrB1 occurs in two protein forms that migrate as 14000 and 5000 Da proteins, SDS-PAGE
14000
-
MsrB1 occurs in two protein forms that migrate as 14000 and 5000 Da proteins, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
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x * 16372.0, recombinant MsrB, mass spectrometry, x * 16467.2, recombinant selenomethionine-MsrB, mass spectrometry
?
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x * 16374, about, recombinant wild-type MsrB domain, mass spectrometry
additional information
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analysis of three-dimensional structure and active site structure
additional information
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MsrB has a highly conserved sequence among organisms
additional information
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analysis of three-dimensional structure and active site structure
additional information
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the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
enzyme domain and active site structure, MsrB domain comprises residues 375-522, overview
additional information
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enzyme domain and active site structure, MsrB domain comprises residues 375-522, overview
additional information
analysis of three-dimensional structure and active site structure
additional information
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the enzyme forms are produced as individual folded entities, but in vivo the enzyme is part of a three-domain protein named PILB, with the central domain exhibiting MsrA activity, and the C-terminal domain showing MsrB activity
additional information
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MsrB and enzyme MsrA, EC 1.8.4.11, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
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MsrB activity is located on the C-terminal domain of PILB, the fused domains are folded entities
additional information
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analysis of three-dimensional structure and active site structure
additional information
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solution structure and dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms
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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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sitting drop vapor diffusion method, crystal structure of HpMsrAB C44S/C318S at 2.2 A, which shows that a linker region (Hpiloop, 193-205) between two domains interacts with each HpMsrA or HpMsrB domain via three salt bridges (E193-K107, D197-R103, and K200-D339)
hanging drop vapor diffusion method, crystals diffracting to 1.87 A resolution, the MsrB3 structure is determined by using X-ray crystallography
purified recombinant detagged MsrB domain containing SeMet39, hanging drop vapour-diffusion method, 15 mg/ml protein in 20 mM Tris, pH 8.5, 10% v/v glycerol, against a well solution containing 0.1 M sodium cacodylate, pH 6.5, 30% w/v PEG 4000, room temperature, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
purified recombinant PilB mutant L38M/L41M, vapour diffusion method, 30 mg/ml protein in 20 mM HEPES, pH 7.5, and 100 mM NaCl, is mixed with well solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 26% PEG 2000 monomethylester, and 25% glycerol, X-ray diffraction structure determination and analysis at 1.6 A resolution, multiwavelength anomalous dispersion at -170°C
-
batch method, using 30% PEG 400, 0.1 M Tris-HCl (pH 8.5), and 0.2 M Na-citrate
selenomethionine-substituted peptide methionine sulfoxide reductase B domain, hanging drop vapour diffusion method in multiwell tissue-culture plates, 0.004 ml protein solution containing 75 mg/ml protein in 50 mM Tris-HCl, pH 8.0, mixed with 0.004 ml precipitant solution at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
batch method, crystals of the oxidized form are obtained by 32% PEG 4000, 0.8 M LiCl, and 0.1 M Tris HCl (pH 8.5), no crystal is obtained for wild type Xanthomonas campestris MsrB in its reduced form
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C116S
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C134T
-
MSRB2 mutant with increased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
T132A
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
T132C
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C45D/C48S/C94S/C97S
-
site-directed mutagenesis, the mutant MsrB loses binding ability for Zn2+ and Fe2+, and shows no catalytic activity in presence of thioredoxin or DTT, substitution of the two cysteine residues of MsrB results in complete loss of the enzyme's metal binding and reductase activity
D197A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 2.6fold lower than wild-type value
E193A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 2.4fold lower than wild-type value
E193A/D197A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 3.1fold lower than wild-type value
E339A
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 1.39fold lower than wild-type value
Y343F
kcat/Km for dabsyl-L-methionine (R)-sulfoxide is 1.1fold lower than wild-type value
C105S
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
C169S
-
site-directed mutagenesis, active site mutant, completely inactive mutant
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to highly reduced activity with cofactor thioredoxin or DTT compared to wild-type MsrB3
H77G/I81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
I81E
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to slightly increased activity with cofactor thioredoxin and reduced activcity with DTT compared to wild-type MsrB3
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB3
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant shows highly reduced activity with cofactor DTT or thioredoxin compared to wild-type MsrB3
W110A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C98S
the mutant show increased Km values with dithiothreitol (1.7fold) and thioredoxin (6fold) compared to the wild type enzyme
E81V
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB1s
F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, the selenocysteine-containing mutant shows reduced activity with either cofactor thioredoxin and DTT compared to wild-type selenocysteine MsrB1, while the cysteine-containing mutant shows activity and kinetics similar to the wild-type cysteine MsrB1
G77H/E81V/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to highly reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
H77G/V81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
V81E
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
L38M/L41M
-
site-directed mutagenesis, mutation of the NT domain of PilB, thioredoxin binding structure, crystal structure analysis, overview
C439S
-
site-directed mutagenesis, MsrA domain of PILB, mutant is inactive with thioredoxin, but about 10fold more active than the wild-type enzyme MsrA domain
C494S
-
site-directed mutagenesis, MsrA domain of PILB, inactive mutant
C63S
-
site-directed mutagenesis, the mutant accumulates the sulfenic acid intermediate, while the wild-type accumulates the disulfide intermediate
D45C/S48C/S94C/A97C
-
site-directed mutagenesis, the mutant MsrB shows increased binding of Zn2+ and Fe2+ compared to the wild-type enzyme, overview, introduction of two cysteine residues into Neisseria meningitidis MsrB analogously to the Escherichia coli enzyme results in increased tight binding of zinc to and strongly increased thermal stability with wild-type reductase activity but no thioredoxin recycling activity
W65F
-
site-directed mutagenesis, structural change of substrate binding and active site structure compared to the wild-type enzyme
C72S
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 7fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
C72S/C74S
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. The mutant enzyme is unable to use Trypanosoma cruzi tryparedoxin or Trypanosoma cruzi thioredoxin as reducing substrates, being able to use trypanothione disulfide as a direct reducing substrate. The double mutation allows the protein to use glutathione as a reductant
C74S
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 2fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
C72S
-
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 7fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
-
C72S/C74S
-
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. The mutant enzyme is unable to use Trypanosoma cruzi tryparedoxin or Trypanosoma cruzi thioredoxin as reducing substrates, being able to use trypanothione disulfide as a direct reducing substrate. The double mutation allows the protein to use glutathione as a reductant
-
C74S
-
similar catalytic efficiency (regarding wild-type protein) for the reduction of N-acetyl-L-methionine-(R)-S-oxide. About 2fold less efficient for tryparedoxin I oxidation than the wild-type enzyme. The mutant enzyme does not exhibit changes in electrophoretic motility respect to wild-type enzyme
-
additional information
additional information
-
cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation
additional information
-
H2O2 shortens the life span of cells in constructed null mutants
additional information
-
construction of a msrA/msrB double mutant for detection of additional enzyme form activities
additional information
-
construction of an enzyme-deficient mutant strain which shows diminished growth in presence of chemical oxidants with rapid loss of viability compared to the wild-type strain, activity can be recovered by complementation with the wild-type gene, study of oxidative stress resistance and colonization activity
additional information
-
substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
additional information
-
enzyme inactivation by insertional mutagenesis in strain 100-23, reduction of ecological performance of the mutant strain in the gut in vivo, mutant phenotype analysis
additional information
-
enzyme inactivation by insertional mutagenesis in strain 100-23, reduction of ecological performance of the mutant strain in the gut in vivo, mutant phenotype analysis
-
additional information
-
construction of a non-selenomethionine mutant of MsrB by site-directed mutagenesis, exchange of the selenomethionine by Cys, Ala, or Ser, the Cys-enzyme shows reduced activity, the Ser- and Ala-enzymes are inactive, substrate specificity, overview
additional information
-
construction of MsrB null mutant and of overexpressing strains, phenotypes, overview
additional information
-
substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
additional information
-
mutant strains produce a truncated version of fused MsrA/MsrB with increased sensitivity to H2O2 and superoxide anions
additional information
-
construction of truncated PilB domain forms, which show decreased survival of the organism to reactive oxygen species, the mutations do not affect piliation, pilin production, or adherence, overview
additional information
-
construction of truncated PilB domain forms, which show decreased survival of the organism to reactive oxygen species, the mutations do not affect piliation, pilin production, or adherence, overview
-
additional information
-
mutation of the recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, while exchange of the catalytic Cys for Ser causes complete loss of activity
additional information
generation of a mutant with osmsrb5 (PFG_3D-00669.R) with T-DNA insertion in the promoter region of the OsMSRB5 gene
additional information
-
H2O2 shortens the life span of cells in constructed null mutants, the mutants show decreased MsrB activity with age compared to the wild-type enzyme
additional information
-
yeast cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation
additional information
-
H2O2 shortens the life span of cells in constructed null mutants
additional information
-
mutation of the msr genes impair virulence, overview, mutation of the msrA1 operon leads to increased susceptibility to H2O2
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
half-life of MsrABTk is 30 min, half-life of MsrB domain is 31 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification of native MsrB from liver, recombinant modified MsrB from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration, to homogeneity
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion
recombinant His-tagged PilB forms in Escherichia coli strain Xl-1 blue by nickel affinity chromatography
-
recombinant His-tagged PilB from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant N-terminally His-tagged full-length PilB and MsrB domain variants from Escherichia coli by nickel affinity chromatography followed by cleavage of the His-Tag through thrombin, followed by gel filtration and ion exchange chomatography
-
recombinant plastidic isozyme pPMSR from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heparin affinity chromatography
-
recombinant wild-type and mutant isozyme MsrB3 from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant isozymes MsrB1 and MsrB2 from Escherichia coli strain BL21(DE3) and NIH-3T3 cells
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
3 genes msrA and 1 gene msrB form an operon, one of the 3 msrA genes is fused to the msrB gene, genetic organization and regulation, overview
-
chromosome 1 contains 2 genes msrB, chromosome 2 contains 1 gene msrB
-
co-expressed with transient receptor potential melastatin type 6 in HEK-293 cells
-
DNA and amino acid sequence determination and analysis of plastidic isozymes MsrB1 and MsrB2, functional expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
endoplasmic reticulum isozyme MsrB3, DNA and amino acid sequence determination and analysis, expression of different constructs of GFP-tagged MsrB3 in monkey kidney CV-1 cells or in mouse fibroblast NIH 3T3 cells
expressed in Drosophila melanogaster, in A-549 cells and human dermal fibroblasts
-
expressed in Escherichia coli BL21 (DE3)cells and in Saccharomyces cerevisiae strain BY4741
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli as a fusion protein with GST which is subsequently cleaved after purification
expression in Escherichia coli BL21 (DE3) fused to an C-terminal 6Histag
expression in in Escherichia coli as a fusion with maltose binding protein
expression inm Escherichia coli, recombinant proteins corresponding to MsrABTk and the individual domains (MsrATk and MsrBTk) are produced
-
expression of the plastidic isozyme pPMSR in Escherichia coli strain BL21(DE3) without the chloroplast signal sequence
-
expression of wild-type and mutant isozyme MsrB3 in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant isozymes MsrB1 and MsrB2 in Escherichia coli strain BL21(DE3) and in NIH-3T3 cells
-
gene msrB with the codon for selenomehinonine is exchanged for methionine, overexpression in Escherichia coli
-
gene msrB, located in the chromosome at 40.09 min, respectively, regulation mechanism of gene expression, overview
-
gene msrB, overexpression of wild-type enzyme and mutant enzymes in Escherichia coli strain DH5alpha
-
gene OsMSRB5, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, recombinant ectopic expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of N- or C-terminally sGFP-tagged enzyme in onion epidermal cells
gene pilB, expression of N-terminally His-tagged full-length wild-type and mutant PilB and MsrB domain variants in Escherichia coli
-
gene pilB, transposon insertion, truncated PilB enzyme forms of the enzyme lacking the MsrA domain from strain MS11, variant VD300, overexpression of the His-tagged PilB forms in Escherichia coli strain Xl-1 blue
-
gene selR, DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli strain BL21(DE3)
human MOLT-4 cell line are stably transfected with the pLXSN retroviral expression vector based on the Moloney murine leukemia virus and Moloney murine sarcoma virus to generate a replication-deficient recombinant retrovirus containing the rat MsrA and the human MsrB2 cDNA. The oxidized protein repair enzymes MsrA and MsrB2, when overexpressed in the cells, are able to counteract the zinc-mediated damaging effects
mitochondrial and cytosolic isozymes are encoded on a single gene with 2 initiations sites, delivering an N-terminal signal peptide to the mitochondrial enzyme form
-
msr gene, DNA sequence determination and analysis, subcloning in Escherichia coli strain DH5-alpha, functional complementation of the enzyme-deficient mutant with the wild-type gene
-
MsrB2DELTAS containing one extra amino acid in N-terminal (Met) and a C-terminal His-tag is expressed in Escherichia coli
overexpression of MsrB in a yeast strain, expression of MsrB as N-terminally 6His-tagged protein in Escherichia coli strain BL-21
-
overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli
overexpression of the MsrB domain in Escherichia coli, strain B834(DE3) produces a selenomethionine-substituted MsrB
-
overexpression of truncated wild-type and mutant enzymes as His-tagged proteins in Escherichia coli, functional coexpression of CBS1 in oocytes with Drosophila melanogaster ShC/B potassium channel
-
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpression of wild-type and mutants in Escherichia coli, expression as N- or C-terminally 6His-tagged protein lowers the recombinant expression level to 3% of total enzyme expressed, labeling of expressed wild-type with 75SeMet
-
PaMsrB1 as a fusion protein containing an N-terminal maltose-binding protein (MBP) is expressed in Escherichia coli Rosetta (DE3) cells. Production of soluble fusion protein is greater when the cells are cultured at 16 °C than at 37°C
pilB is transcribed as polycistronic transcript, overexpression of PilB as His-tagged protein in Escherichia coliBL21(DE3)
-
the chromosome contains 2 copies of gene msrB, a plasmid harbors 1 copy of gene msrB
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme is constitutively expressed
expression is upregulated by abscisic acid, salt, cold, and methyl viologen stress within 24 h of treatment
-
expression is upregulated by oxidative stresses, including 4°C, 16°C, 25°C, and 42°C, ultraviolet light, H2O2, CdCl2, HgCl2, paraquat, imidacloprid, and cyhalothrin
in seedling shoots, isoform MSRB5 is expressed in response to drought conditions. Under salt stress, MSRB5 is upregulated in seedling roots
MsrB2 is down-regulated upon inoculation with either incompatible or compatible pathogens. The expression of MsrB2 is suppressed by treatment with 0.1 mM methyl jasmonate, 5 mM salicylic acid, and 5 mM ethephone
sRNA RyhB is a direct regulator of the MsrB. RyhB down-regulates MsrB transcripts along with Hfq and RNaseE proteins. Mutations in the ryhB, fur, hfq, or RNaseE-encoded genes result in iron-insensitive expression of MsrB. RyhB pairing to msrB mRNA prevents efficient ribosome binding and thereby inhibits translation initiation. Both RyhB-pairing sites are required to decrease msrB expression
enzyme is constitutively expressed
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
enzyme is a target for modification of redox-dependent regulation
synthesis
synthesis
-
enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs
synthesis
K0HZZ3
application of methionine sulfoxide reductase B for preparation of (S)-sulfoxides through kinetic resolution of racemic sulfoxides. The kinetic resolution of rac-sulfoxides is successfully accomplished at substrate concentrations up to 50 mM (7.8 g/l) when catalyzed by akMsrB whole-cell catalyst. The study supports that asymmetric reductive resolution of rac-sulfoxides catalysed by MsrB can become an effective strategy for green synthesis of optically pure sulfoxides
EXTERNAL LINKS (specific for EC-Number 1.8.4.12)
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Release 2026.1 (March 2026)
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