Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.8.4.12
-
RECOMMENDED NAME
GeneOntology No.
peptide-methionine (R)-S-oxide reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism involves the formation of a sulfenic acid intermediate
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism involving the formation of a sulfenic acid intermediate
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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
show the reaction diagram
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
P14930
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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
show the reaction diagram
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
reaction mechanism, Cys494 and Cys439 are involved
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
reaction mechanism, modeling of substrate binding at the active site, Cys444 and Cys495 are involved
P14930
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
selenomethionine is essential for MsrB activity
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
the active site selenocysteine SeC169 is essential for enzyme activity
-
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
three-step catalytic mechanism, influence of pH on reaction mechanism, overview
-
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
show the reaction diagram
proposed catalytic mechanism of the reductase step of MsrB
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
-
-
-
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
catalytic mechanism and the role of cofactor recycling in vivo
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
catalytic mechanism and the role of cofactor recycling in vivo
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
catalytic mechanism, overview
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
show the reaction diagram
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
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methionine metabolism
-
-
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+.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
5 genes, including 1 plastidic isozyme
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
isozymes MsrB1-3
-
-
Manually annotated by BRENDA team
plastidic isozymes MsrB1 and MsrB2
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
MsrB variants one of which is also called Sel-X
-
-
Manually annotated by BRENDA team
strain NCTC 11168
-
-
Manually annotated by BRENDA team
Campylobacter jejuni NCTC 11168
strain NCTC 11168
-
-
Manually annotated by BRENDA team
ECW-30R
UniProt
Manually annotated by BRENDA team
enzyme belongs to the metal-containing MsrB group I
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
-
-
-
Manually annotated by BRENDA team
1 copy gene msrB
-
-
Manually annotated by BRENDA team
enzyme belongs to the metal-containing MsrB group I
-
-
Manually annotated by BRENDA team
enzyme forms MsrB and Mem-R,S-Msr
-
-
Manually annotated by BRENDA team
enzyme forms MsrB, and other enzyme forms, e.g. Mem-R,S-Msr, overview
-
-
Manually annotated by BRENDA team
gene msrB, enzyme SelR which is a selenoprotein, enzyme is organized in a fusion protein together with MsrA, EC 1.8.4.B2
-
-
Manually annotated by BRENDA team
wild-type strain MC1061, isozyme MsrB and a membrane-associated isozyme
-
-
Manually annotated by BRENDA team
; 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
-
-
Manually annotated by BRENDA team
strain NRC-1
-
-
Manually annotated by BRENDA team
Halobacterium salinarum NRC-1
strain NRC-1
-
-
Manually annotated by BRENDA team
; 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
-
-
Manually annotated by BRENDA team
strain 26695, enzyme forms MsrA and MsrB are fused together forming a single protein termed Msr
-
-
Manually annotated by BRENDA team
strain 26695, enzyme forms MsrA and MsrB are fused together forming a single protein termed Msr
-
-
Manually annotated by BRENDA team
; overexpressed in Escherichia coli BL21
SwissProt
Manually annotated by BRENDA team
isozyme MsrB2
-
-
Manually annotated by BRENDA team
isozymes MsrB1 or selenoprotein R, MsrB2 or CBS-1, and MsrB3
-
-
Manually annotated by BRENDA team
isozymes MsrB1, MsrB2, and MsrB3
-
-
Manually annotated by BRENDA team
isozymes MsrB1-3
-
-
Manually annotated by BRENDA team
MsrB variants one of which is also called Sel-X, encoded by distinct genes, MsrB is a selenoprotein
-
-
Manually annotated by BRENDA team
MsrB, one isozyme of which is termed CBS-1
-
-
Manually annotated by BRENDA team
several splicing variants resulting in three isozymes MsrB1-3
-
-
Manually annotated by BRENDA team
strain 100-23 in murine gut
-
-
Manually annotated by BRENDA team
strain 100-23 in murine gut
-
-
Manually annotated by BRENDA team
strain Fusaro
-
-
Manually annotated by BRENDA team
Methanosarcina barkeri Fusaro
strain Fusaro
-
-
Manually annotated by BRENDA team
strain Go1
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
; overexpressed in Escherichia coli BL21
SwissProt
Manually annotated by BRENDA team
isozyme MsrB3
SwissProt
Manually annotated by BRENDA team
isozymes MsrB1, MsrB2, and MsrB3
-
-
Manually annotated by BRENDA team
isozymes MsrB1-3
-
-
Manually annotated by BRENDA team
MsrB is a selenoprotein
-
-
Manually annotated by BRENDA team
selenomethionine-containing enzyme MsrB
-
-
Manually annotated by BRENDA team
; 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
-
-
Manually annotated by BRENDA team
bifunctional enzyme MsrA/B, gene pilB
-
-
Manually annotated by BRENDA team
enzyme belongs to the MsrB group IIS
SwissProt
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
strain MS11, variant VD300, bifunctional enzyme MsrA/B, gene pilB
-
-
Manually annotated by BRENDA team
strain MS11, variant VD300, bifunctional enzyme MsrA/B, gene pilB
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-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA, EC 1.8.4.B2, and MsrB activity
-
-
Manually annotated by BRENDA team
bifunctional enzyme MsrA/B
-
-
Manually annotated by BRENDA team
enzyme belongs to the MsrB group IIS
-
-
Manually annotated by BRENDA team
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
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-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
no activity in Aeropyrum pernix K1
-
-
-
Manually annotated by BRENDA team
no activity in Aquifex aeolicus
-
-
-
Manually annotated by BRENDA team
no activity in Archaeoglobus fulgidus DSM 4304
-
-
-
Manually annotated by BRENDA team
no activity in Bifidobacterium longum
NCC2705
-
-
Manually annotated by BRENDA team
no activity in Bifidobacterium longum NCC2705
NCC2705
-
-
Manually annotated by BRENDA team
no activity in Clostridium tetani
strain E88
-
-
Manually annotated by BRENDA team
no activity in Clostridium tetani E88
strain E88
-
-
Manually annotated by BRENDA team
no activity in Ferroplasma acidarmanus
-
-
-
Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
DSM 2661
-
-
Manually annotated by BRENDA team
no activity in Methanococcus maripaludis
strain S2
-
-
Manually annotated by BRENDA team
no activity in Methanococcus maripaludis S2
strain S2
-
-
Manually annotated by BRENDA team
no activity in Methanopyrus kandleri
strain AV19
-
-
Manually annotated by BRENDA team
no activity in Methanopyrus kandleri AV19
strain AV19
-
-
Manually annotated by BRENDA team
no activity in Nanoarchaeum equitans
Kin4-M
-
-
Manually annotated by BRENDA team
no activity in Nanoarchaeum equitans Kin4-M
Kin4-M
-
-
Manually annotated by BRENDA team
no activity in Picrophilus torridus
strain DSM 9790
-
-
Manually annotated by BRENDA team
no activity in Pyrobaculum aerophilum
strain IM2
-
-
Manually annotated by BRENDA team
no activity in Pyrobaculum aerophilum IM2
strain IM2
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus abyssi
strain GE5
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus abyssi GE5
strain GE5
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus furiosus
strain DSM 3638
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus horikoshii
strain OT3
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus horikoshii OT3
strain OT3
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus acidocaldarius
DSM 639
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus solfataricus
strain P2
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus solfataricus P2
strain P2
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus tokodaii
strain 7
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus tokodaii 7
strain 7
-
-
Manually annotated by BRENDA team
no activity in Thermococcus kodakarensis
strain KOD1
-
-
Manually annotated by BRENDA team
no activity in Thermococcus kodakarensis KOD1
strain KOD1
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma acidophilum
DSM 1728
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma volcanium
strain GSS1
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma volcanium GSS1
strain GSS1
-
-
Manually annotated by BRENDA team
no activity in Thermotoga maritima
-
-
-
Manually annotated by BRENDA team
enzyme belongs to the metal-containing MsrB group I
-
-
Manually annotated by BRENDA team
isozymes MsrB1-3
-
-
Manually annotated by BRENDA team
MsrB variants one of which is also called Sel-X
-
-
Manually annotated by BRENDA team
strain BY4741, enzyme MsrB
-
-
Manually annotated by BRENDA team
strain BY4741, enzyme MsrB
-
-
Manually annotated by BRENDA team
winter rye, cv. Halo
-
-
Manually annotated by BRENDA team
3 copies of gene msrB
-
-
Manually annotated by BRENDA team
1 copy of gene msrB
-
-
Manually annotated by BRENDA team
strains RN450 and BB270, and derivatives, 1 gene msrB
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
; 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
-
-
Manually annotated by BRENDA team
enzyme belongs to the metal-containing MsrB group I
-
-
Manually annotated by BRENDA team
3 isozymes of MsrB
-
-
Manually annotated by BRENDA team
2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
B7S5L1
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
-
cytosolic MsrB7 and MsrB8 knockdown lines are sensitive to oxidative stress
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
-
deficiency in MsrB enzyme reduces the level of Enterococcus faecalis virulence in a systemic and urinary tract infection model
-
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
-
MsrB of plays only a limited role in resisting intracellular and in vitro reactive oxygen intermediates
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
B7S5L1
MsrB2 is a defense regulator against oxidative stress and pathogen attack, MsrB2 causes enhanced resistance to Phytophthora capsici and Phytophthora infestans
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
-
oxidative stress can lead to oxidation of methionine residues, which are repaired by MsrB1
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
-
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
-
neuronal expression of isoform MsrB3A renders Drosophilaflies resistant to oxidative stress. These flies also show significantly enhanced cold (4C) and heat (37C) tolerance. Expression of isoform MsrB3A in the whole body and nervous system extends the lifespan of fruit flies at 29C by 43-50% and 12-37%, respectively. Additionally, isoform MsrB3A overexpression significantly delays the age-related decline in locomotor activity and fecundity
physiological function
Q9C8M2
the MSRB1 gene plays a critical role in protecting against oxidative stress
physiological function
-
MsrB is important for the oxidative stress response, macrophage survival, and persistent infection with Enterococcus faecalis
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-methyl 4-tolyl sulfoxide + thioredoxin
?
show the reaction diagram
-
-
-
-
?
acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin
L-methionine methyl ester + thioredoxin disulfide + H2O
show the reaction diagram
-
the affinity of MsrB to acetyl-L-methionine (R)-sulfoxide methyl ester is higher than to L-methionine (R)-sulfoxide
-
-
?
acetyl-L-methionine-(R)-S-oxide-NHMe + thioredoxin
?
show the reaction diagram
-
-
-
-
?
calmodulin-L-methionine (R)-S-oxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrBA is able to completely reduce (i.e., repair) MetSO in the calcium regulatory protein calmodulin. The efficient repair is the coordinate activity of the two catalytic domains in the MsrBA fusion protein, which results in a 1 order of magnitude rate enhancement in comparison to those of the individual MsrA or MsrB enzyme alone
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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, MsrB is specific for the R-form, recombinant human calmodulin, recombinant human enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview
-
-
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q78J03
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8IXL7
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl-L-methionine (R)-sulfoxide + 1,4-dithioerythritol
dabsyl-L-methionine + 1,4-dithioerythritol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + CDSP32
dabsyl-L-methionine + ?
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q9JLC3
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q78J03
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q8IXL7
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q9C8M2
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
isoforms MSRB2 and MSRB4 also show enzyme activity toward protein-based L-methionine (R)-sulfoxide with either dithiothreitol or thioredoxin as reductants, whereas isoform MSRB1 is active only with dithiothreitol
-
-
?
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin C4
?
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin S12
dabsyl-L-methionine + ?
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin S12
?
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
B7S5L1
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
FMsr is specific for the R-isomer
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
A7U629
activity with Escherichia coli thioredoxin, NtMsrB21
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q78J03
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8IXL7
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond. Thioredoxin- and dithiothreitol-dependent activities are approximately equal
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
thioredoxin f1, thioredoxin m1, thioredoxin m2, thioredoxin m3, thioredoxin m4, thioredoxin x, thioredoxin y1, thioredoxin y2
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin h1
?
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
Q78J03
-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
Q8IXL7
-
-
-
?
DL-methionine (R)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
show the reaction diagram
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21, Hsp21 contains 6 methionine residues at positions 49, 52, 55, 59, 62, and 67, about half of the residues are reduced by the enzyme probably due to its stereospecificity
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
show the reaction diagram
-
the MsrB-domain of MsrABTk is strictly specific for the reduction of L-methionine (R)-sulfoxide
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q9C8M2
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9JLC3
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8P4Q6
specific substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
specific substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
Msr is specific for the R-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q81NK9
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the (R)-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form of the substrate
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrates are peptides and proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
P14930
MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q81NK9
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9Y3D2
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
P0A746
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
PilB shows absolute specificity for the R-form of free and protein-bound methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form of L-methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
Q9LAM9
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
Q9LAM9
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine-(R)-S-oxide + dithioerythritol
L-methionine + dithioerythritol disulfide + H2O
show the reaction diagram
-
absolute stereospecific reduction, MsrB1 and MsrB2
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8BU85
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
absolute stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
absolute stereospecific reduction, isozyme MsrB2, no activity with isozyme MsrB1
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + dithiothreitol
N-acetyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin
N-acetyl-L-methionine methyl ester + thioredoxin disulfide
show the reaction diagram
-
enzyme MsrB
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
show the reaction diagram
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
protein-bound substrate, preferred substrate of isozyme MsrB2
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
show the reaction diagram
-
enzyme reduces L-methionine (R)-sulfoxide of the protein substrate
-
-
?
oxidized chloroplast signal particle protein 43 + ?
reduced chloroplast signal particle protein 43 + ?
show the reaction diagram
-
-
-
-
?
oxidized chloroplast signal particle protein 54 + ?
reduced chloroplast signal particle protein 54 + ?
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
-
-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q78J03
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2, 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
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activity with membrane-bound enzyme form Mem-R,S-Msr
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction, MsrB accepts free and protein-bound substrates
-
-
r
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
-
downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
-
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
-
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
-
additional information
?
-
-
enzyme provides protection for the cell against oxidative stress
-
-
-
additional information
?
-
Q81NK9
enzyme provides protection for the cell against oxidative stress
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
-
additional information
?
-
-
MsrB is specific for the R-form of the substrate
-
-
-
additional information
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
-
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
-
additional information
?
-
-
enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation
-
-
-
additional information
?
-
-
substrate specificities of enzymes, the reduction step is rate-determining
-
-
-
additional information
?
-
-
substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
-
-
-
additional information
?
-
-
substrate specificity of enzyme forms with R-form of free and protein-bound methionine sulfoxide, overview
-
-
-
additional information
?
-
-
substrate specificity of MsrB activity, diverse substrates, overview
-
-
-
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzyme also exhibits MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates, the membrane-associated isozyme also shows MsrA activity utilizing L-methionine (S)-sulfoxide and N-acetyl-L-methionine (S)-sulfoxide as substrates
-
-
-
additional information
?
-
-
the reduction step is rate-determining
-
-
-
additional information
?
-
P14930
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
-
-
-
additional information
?
-
-
PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, regulation of MsrB expression, overview
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
-
additional information
?
-
-
The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
-
-
-
additional information
?
-
-
substrate specificity, overview, isozyme MsrB1 is not able to reduce free L-methionine-(R)-S-oxide or N-acetyl-L-methionine-(R)-S-oxide, while isozyme MsrB2 prefers protein-bound substrates such as N-acetyl-L-methionine (R)-S-oxide, overview
-
-
-
additional information
?
-
-
the 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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
-
-
-
additional information
?
-
-
the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
-
-
-
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
MsrB3 plays an important role in cold tolerance by eliminating methionine sulfoxide and reactive oxygen species that accumulate at the endoplasmic reticulum during cold acclimation
-
-
-
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
-
additional information
?
-
Q9NZV6
Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
-
-
-
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
-
additional information
?
-
Q8IXL7
MsrB3 physically interacts with the sulfenic acid intermediate of these oxidized enzymes to directly form an intermolecular disulfide bond
-
-
-
additional information
?
-
A7U629
NtMsrB1 shows no activity with dithiothreitol
-
-
-
additional information
?
-
Q9JWM8
the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
-
-
-
additional information
?
-
-
methionine-oxidized amyloid fibrils (methionine-oxidized monomer and fibrillar apoC-II) are poor substrates for human methionine sulfoxide reductase B2. At Msr concentrations of more than 0.0005 mM, approximately 90% of monomeric MetO-apoCII is reduced. In contrast, at 0.0005 mM Msr, only 35% of fibrillar MetO-apoC-II is reduced, which increased to only 37% after incubation with a 4fold higher enzyme concentration
-
-
-
additional information
?
-
-
the CDSP32 thioredoxin forms a heterodimeric complex with MSRB1 through its catalytic cysteine, Cys219, via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction
-
-
-
additional information
?
-
Q9C8M2
isoform MSRB1 exhibits no activity in thioredoxin dependent system
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Campylobacter jejuni NCTC 11168
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
the enzyme also exhibits MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
-
additional information
?
-
-
PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
show the reaction diagram
-
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
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9JLC3
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
Msr is specific for the R-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q81NK9
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the (R)-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form of the substrate
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrates are peptides and proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
Q9LAM9
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
absolute stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
-
-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
Q78J03
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
-
downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
-
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
-
additional information
?
-
-
enzyme provides protection for the cell against oxidative stress
-
-
-
additional information
?
-
Q81NK9
enzyme provides protection for the cell against oxidative stress
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
-
additional information
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
-
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
-
additional information
?
-
-
PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, regulation of MsrB expression, overview
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
-
additional information
?
-
-
The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
-
-
-
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
MsrB3 plays an important role in cold tolerance by eliminating methionine sulfoxide and reactive oxygen species that accumulate at the endoplasmic reticulum during cold acclimation
-
-
-
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
-
additional information
?
-
Q9NZV6
Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
-
-
-
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Campylobacter jejuni NCTC 11168
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithioerythritol
-
DTE
dithiothreitol
-
-
dithiothreitol
-
utilized in vitro
dithiothreitol
-
MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity
dithiothreitol
-
-
dithiothreitol
-
absolutely dependent on in vitro and in vivo with substrate Hsp21
dithiothreitol
-
results in higher activity compared to cofactor thioredoxin
dithiothreitol
-
can substitute for thioredoxin in vitro
dithiothreitol
-
can act as cofactor only in vitro showing a much higher activity than thioredoxin
NADPH
-
membrane-bound enzyme form Mem-R,S-Msr
thioredoxin
-
-
thioredoxin
-
physiologic cofactor
thioredoxin
-
dependent on
thioredoxin
-
-
thioredoxin
-
preferred cofactor
thioredoxin
-
-
thioredoxin
Q9LAM9
-
thioredoxin
-
-
thioredoxin
-
-
thioredoxin
-
dependent on
thioredoxin
-
PilB contains an N-terminal thioredoxin-like domain, the NT domain, fused to the MsrA and MSrB domains, structure overview
thioredoxin
-
isozyme MsrB2, no activity with isozyme MsrB1
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
-
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
-
-
thioredoxin
Q8P4Q6
-
thioredoxin
B7S5L1
-
dithiothreitol
-
can substitute for thioredoxin
additional information
-
no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
-
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
-
thioredoxin independent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
selenium
Q81NK9
selenoprotein
selenium
-
selenoprotein
selenium
-
selenoprotein
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
P54155
selenocysteine-containing
selenium
-
selenocysteine-containing
selenium
Q8BU85
selenocysteine-containing
selenium
-
selenocysteine-containing
selenium
-
selenoprotein. Se status affects Msr (most likely through effects on the selenoprotein MsrB)
selenium
-
selenoprotein
Zinc
-
zinc-containing enzyme
Zinc
Q8BU85
zinc-containing enzyme
Zinc
-
marginal Zn deficiency has little effect on Msr in liver and kidney
Zn2+
Q81NK9
metalloenzyme, content determination
Zn2+
-
metalloenzyme, content determination
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
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+
-
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+
-
binding by residues at positions 45, 48, 94, and 97, 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+
-
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+
-
MsrB1 is a zinc-containing protein
Zn2+
-
contains zinc
Fe2+
-
with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding
additional information
-
content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview
additional information
-
enzyme belongs to the metal-containing MsrB group I
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
PilB is a selenocysteine-containing enzyme
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
-
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
-
the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, 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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
dimedone
-
binds specifically to the sulfenic acid reaction intermediate
H2O2
-
1 mM, 40% deactivation of MSRB1
L-Methionine sulfone
-
-
additional information
-
selenium-adequate diet retains MsrB mRNA and protein expression at basal levels
-
additional information
-
enzyme expression decreases during dehardening from 4C to 22C of cold-acclimated plants, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
no inhibition by EDTA, 1,10-phenanthroline, and pyridine 2,6-dicarboxylic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression of MsrB is induced by dehydration and H2O2
-
additional information
-
MsrB expression is induced by heat shock and alkylating methyl-methanesulfonate treatment
-
additional information
-
enzyme is induced under oxidative stress and heat shock
-
additional information
-
the msrA1-msrB operon is induced by antibiotics
-
additional information
-
oxidative stress, e.g. caused by H2O2 up to 0.4 mM, induces enzyme expresssion
-
additional information
-
48 h exposure to high light at 22C induces enzyme expression, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
heat shock, dehydration, and reactive oxygen species like H2O2 induce the expression of MsrB
-
additional information
-
starvation induces MsrB expression, also heat treatment and methylmethanesulfonate induce the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
acetyl-L-methionine (R)-S-oxide methyl ester
-
pH 5.5, 25C
2.2
acetyl-L-methionine (R)-S-oxide methyl ester
-
pH 8.0, 25C
0.00021
CDSP32
-
pH 8.0, 37C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.0091
dithiothreitol
Q9C8M2
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37C
0.03
dithiothreitol
-
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37C
0.05
dithiothreitol
-
mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37C
2
dithiothreitol
-
MsrB domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide
0.0068
glutaredoxin C4
-
isoform MSRB1 wild type enzyme
-
0.00053
glutaredoxin S12
-
pH 8.0, 37C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
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
56
L-methionine (R,S)-sulfoxide
-
MsrB activity of PILB, pH 8.0, 25C
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
0.049
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication; isoform MSRB4, pH and temperature not specified in the publication
0.026
thioredoxin
-
pH 5.5, 25C
0.034
thioredoxin
-
MsrB activity of PILB, pH 8.0, 25C
0.058
thioredoxin
-
MsrB, pH 8.0, 25C, 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 37C
7
thioredoxin
-
pH 8.0, 25C
7
thioredoxin
-
mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37C
1.3
L-methionine-(R)-S-oxide
-
recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
additional information
additional information
-
kinetics
-
additional information
additional information
-
stopped flow kinetics, steady-state kinetics
-
additional information
additional information
-
kinetic mechanism
-
additional information
additional information
-
thioredoxin- and DTT-dependent kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant MsrB
-
additional information
additional information
-
reductase step kinetic parameters of the wild-type and mutated MsrB
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
CDSP32
-
pH 8.0, 37C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
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
0.047
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 mutant C116S, in the presence of 20 mM dithioerythritol
0.064
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB2 mutant C134T, in the presence of 20 mM dithioerythritol
0.075
dabsyl-L-methionine (R)-sulfoxide
-
isoform MSRB1 wild type enzyme, in the presence of 20 mM dithioerythritol
0.09
dithiothreitol
Q9C8M2
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37C
0.02
glutaredoxin C4
-
isoform MSRB2 wild type enzyme
-
0.3
glutaredoxin C4
-
isoform MSRB2 mutant enzyme C134T
-
0.34
glutaredoxin C4
-
isoform MSRB1 mutant enzyme C116S
-
0.37
glutaredoxin C4
-
isoform MSRB1 mutant enzyme T132A
-
0.48
glutaredoxin C4
-
isoform MSRB1 wild type enzyme
-
0.03
glutaredoxin S12
-
isoform MSRB2 wild type enzyme
-
0.17
glutaredoxin S12
-
pH 8.0, 37C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.31
glutaredoxin S12
-
isoform MSRB1 mutant enzyme T132A
-
0.36
glutaredoxin S12
-
isoform MSRB2 mutant enzyme C134T
-
0.5
glutaredoxin S12
-
isoform MSRB1 mutant enzyme C116S
-
0.58
glutaredoxin S12
-
isoform MSRB1 wild type enzyme
-
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
2.8
L-methionine (R,S)-sulfoxide
-
MsrB activity of PILB, pH 8.0, 25C
0.002
L-methionine-(R)-S-oxide
-
recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
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
0.24
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
1.28
thioredoxin h1
-
isoform MSRB2 wild type enzyme
-
0.83
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
additional information
additional information
-
-
-
additional information
additional information
-
reductase step kinetic parameters of the wild-type and mutated MsrB
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
dithiothreitol
Q9C8M2
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37C
45
73.4
glutaredoxin C4
-
isoform MSRB1 wild type enzyme
0
0.09
L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
8608
1.4
L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
8608
5
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
14726
42
N-acetyl-L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
14726
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
0.000085
-
enzyme form Mem-R,S-Msr
0.00009
-
enzyme form Mem-R,S-Msr, substrate sulindac
0.00022
-
MsrB, substrate N-acetyl-L-methionine-(R)-sulfoxide
0.0004
-
membrane vesicles, substrate N-acetyl-L-methionine-(R)-sulfoxide
0.0007
-
kidney, substrate L-methionine (R)-sulfoxide
0.0012
-
msrA1 knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.0015
-
msrA1/msrA2 double knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.0019
-
liver, 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
0.0048
-
wild-type strain, substrate L-methionine (R)-sulfoxide
0.01
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.023
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.023
-
in 100 mM sodium phosphate, at 37C and pH 5.7
0.045
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.055
-
in 100 mM sodium phosphate, at 37C and pH 6.5
0.071
Q8IXL7
substrate: cytosolic human thioredoxin 1
0.074
-
in 50 mM carbonate-bicarbonate, at 37C and pH 10.0
0.075
P14930
purified recombinant MsrA/MsrB tandem domain, substrate L-methionine (R)-sulfoxide
0.085
P0A746
purified recombinant CBS-1, substrate L-methionine (R)-sulfoxide
0.092
-
purified recombinant CBS-1, substrate L-methionine (R)-sulfoxide
0.106
Q78J03
substrate: cytosolic human thioredoxin 1
0.11
P14930
purified recombinant MsrB domain alone, substrate L-methionine (R)-sulfoxide
0.11
-
in 100 mM sodium phosphate, at 37C and pH 7.0
0.119
-
in 50 mM Tris-HCl, at 37C and pH 7.6
0.12
Q8IXL7
substrate: Escherichia coli thioredoxin
0.128
Q78J03
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.142
Q78J03
substrate: Escherichia coli thioredoxin
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
Q8IXL7
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.179
Q8IXL7
substrate: dithiothreitol
0.228
-
in 100 mM sodium phosphate, at 37C and pH 7.5
0.267
-
in 50 mM Tris-HCl, at 37C and pH 8.0
0.272
-
in 50 mM carbonate-bicarbonate, at 37C and pH 9.6
0.291
Q78J03
substrate: dithiothreitol
0.386
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
0.446
-
in 50 mM Tris-HCl, at 37C and pH 8.6
0.452
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
0.462
-
in 50 mM carbonate-bicarbonate, at 37C and pH 9.2
0.484
-
in 50 mM Tris-HCl, at 37C and pH 9.0
1.78
-
purified recombinant PilB, substrate L-methionine (R)-sulfoxide
3
-
recombinant wild-type MsrB domain, cosubstrate dithiothreitol
4.2
-
recombinant wild-type MsrA/MsrB, cosubstrate dithiothreitol
12
-
recombinant wild-type MsrB domain, cosubstrate thioredoxin
170
-
recombinant wild-type MsrA/MsrB, cosubstrate thioredoxin
additional information
-
in vivo MsrB activity is below detection limit
additional information
-
tissue specific activity, activity in tissues of MsrA-deficient mutant mice
additional information
-
subcellular sulindac reducing activity in calf liver
additional information
-
-
additional information
-
recombinant activity in overexpressing yeast cells
additional information
-
-
additional information
-
thioredoxin- and DTT-dependent activities of mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
optimum pH of the MsrB domain
6.9
P0A746
assay at
6.9
-
assay at
6.9
P14930
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
MsrB domain of MsrABTk
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
P0A746
assay at
37
-
assay at
37
P14930
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.9
Q9C8M2
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isozyme MsrB1
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
Manually annotated by BRENDA team
-
Msr activity is significantly reduced by Se deficiency
Manually annotated by BRENDA team
-
isozyme MsrB2
Manually annotated by BRENDA team
-
isozymes MsrB3 and MsrB2
Manually annotated by BRENDA team
-
expression/activities of MSRA and MSRB are significantly decreased in the epidermis of patients with vitiligo compared to healthy controls
Manually annotated by BRENDA team
-
cell line WI-38, young and old cells, enzyme expression pattern during cell development, senescent cells show decreased enzyme expression and activity
Manually annotated by BRENDA team
Q9C8M2
high expression
Manually annotated by BRENDA team
Q9C8M2
high expression in red mature fruits
Manually annotated by BRENDA team
-
highly expressed
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
most abundant in ventricles, interventricular septum, and apex
Manually annotated by BRENDA team
-
isozymes MsrB3 and MsrB2
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
Manually annotated by BRENDA team
-
highest sulindac reductase activity
Manually annotated by BRENDA team
-
isozyme MsrB1 and MsrB2
Manually annotated by BRENDA team
-
marginal Zn deficiency has little effect on Msr in liver and kidney. Msr activity is significantly reduced by Se deficiency
Manually annotated by BRENDA team
-
MsrB1 is present in the renal Mg2+-transporting distal convoluted tubules
Manually annotated by BRENDA team
Q9C8M2
high expression
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
high expression level in cold-hardened plants at 4C
Manually annotated by BRENDA team
-
epithelia and fibers, isozymes MsrB1 or selenoprotein R, MsrB2 or CBS-1, and MsrB3, differential expression patterns of isozymes, overview
Manually annotated by BRENDA team
-
polymorphonuclear
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
highly expressed
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
Manually annotated by BRENDA team
-
marginal Zn deficiency has little effect on Msr in liver and kidney. Msr activity is significantly reduced by Se deficiency
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q9C8M2
low expression
Manually annotated by BRENDA team
-
highest expression in roots
Manually annotated by BRENDA team
-
highly expressed
Manually annotated by BRENDA team
-
isozymes MsrB1 and MsrB2
Manually annotated by BRENDA team
-
chronic sun-exposure would result in a decreased expression of two main components of the methionine sulfoxide reductase system, MsrA and MsrB2
Manually annotated by BRENDA team
-
isozyme MsrB1
Manually annotated by BRENDA team
-
i.e. HLE cell, transformed human lens epithelial cells
Manually annotated by BRENDA team
Q9C8M2
low expression
Manually annotated by BRENDA team
-
embryonic fibroblast, activity during development: downregulation during replicative senescence
Manually annotated by BRENDA team
-
fibroblast, young and old cells, enzyme expression pattern during cell development
Manually annotated by BRENDA team
-
MsrB2 is downregulated during replicative senescence of WI-38 human fibroblasts
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
additional information
-
expression pattern analysis
Manually annotated by BRENDA team
additional information
-
enzyme expression level and methionine sulfoxide content in fibroblasts during development, overview
Manually annotated by BRENDA team
additional information
-
high expression level of the plastidic isozyme pPMSR in photosynthetic active tissue
Manually annotated by BRENDA team
additional information
-
tissue distribution, main expression of CBS1 in muscle tissues, overview
Manually annotated by BRENDA team
additional information
-
expression analysis of MsrB isozymes
Manually annotated by BRENDA team
additional information
-
tissue-specific expression of MsrB isozymes, overview
Manually annotated by BRENDA team
additional information
-
presence of MsrABTk is greater in Thermococcus kodakaraensis cells grown at suboptimal temperatures (60 to 70C) and could not be detected at 80 to 90C. The amount of intracellular MsrABTk protein increases with exposure to higher dissolved oxygen levels, but only at suboptimal growth temperatures
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
plastidic isozyme pPMSR
Manually annotated by BRENDA team
-
plastidic isozymes MsrB1 and MsrB2, analysis of subcellular localization
Manually annotated by BRENDA team
-
Sel-X, a MsrB enzyme form variant
Manually annotated by BRENDA team
-
Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf
Manually annotated by BRENDA team
-
Sel-X, a MsrB enzyme variant
Manually annotated by BRENDA team
-
isozyme MsrB1 or selenoprotein R
Manually annotated by BRENDA team
Q8BU85
specific isozyme MsrB3
Manually annotated by BRENDA team
Q8BU85
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
secretion of MsrA, EC 1.8.4.11, and MsrB fused together
-
Manually annotated by BRENDA team
-
outer cell membrane
Manually annotated by BRENDA team
-
enzyme form Mem-R,S-Msr
Manually annotated by BRENDA team
-
membrane-associated enzyme MsrB
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
-
Manually annotated by BRENDA team
-
Sel-X, a MsrB enzyme form variant
Manually annotated by BRENDA team
-
Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf
Manually annotated by BRENDA team
-
Sel-X, a MsrB enzyme variant
Manually annotated by BRENDA team
-
isozyme MsrB2 or CBS-1, and isozyme MsrB3
Manually annotated by BRENDA team
-
isozymes MsrB2 and MsrB3
Manually annotated by BRENDA team
-
isozyme MsrB1 or selenoprotein R
Manually annotated by BRENDA team
-
MsrB3B contains a different signal peptide at the N-terminus and is targeted to mitochondria
Manually annotated by BRENDA team
additional information
-
no activity in the cytoplasm
-
Manually annotated by BRENDA team
additional information
-
subcellular sulindac reducing activity distribution in calf liver
-
Manually annotated by BRENDA team
additional information
Q8BU85
subcellular localization analysis, no localization of MsrB3 in the mitochondria
-
Manually annotated by BRENDA team
additional information
-
subcellular targeting is determined by alternative splicing
-
Manually annotated by BRENDA team
additional information
-
no activity in the cytoplasm
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5000
-
MsrB1 occurs in two protein forms that migrate as 14000 and 5000 Da proteins, SDS-PAGE
713362
13300
-
calculated from amino acid sequence
713571
14000
-
MsrB1 occurs in two protein forms that migrate as 14000 and 5000 Da proteins, SDS-PAGE
713362
15000
-
SDS-PAGE
713571
16610
-
reduced isoform MSRB1, MALDI-TOF mass spectrometry
698915
16620
-
reduced isoform MSRB1, calculated from amino acid sequence
698915
16860
-
reduced isoform MSRB2, calculated from amino acid sequence; reduced isoform MSRB2, MALDI-TOF mass spectrometry
698915
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 13000, native wild-type MsrB, SDS-PAGE
?
-
x * 16372.0, recombinant MsrB, mass spectrometry, x * 16467.2, recombinant selenomethionine-MsrB, mass spectrometry
?
-
x * 16374, about, recombinant wild-type MsrB domain, mass spectrometry
?
-
x * 43000, Msr, SDS-PAGE
?
-
x * 57000, MsrA/B
?
-
x * 15000-35000, recombinant His-tagged PilB forms, SDS-PAGE
?
A7U629
x * 14800, calculated from sequence
?
Q9C8M2
x * 21200, calculated from amino acid sequence
?
-
x * 43000, Msr, SDS-PAGE
-
?
-
x * 15000-35000, recombinant His-tagged PilB forms, SDS-PAGE
-
additional information
-
analysis of three-dimensional structure and active site structure
additional information
P14930
analysis of three-dimensional structure and active site structure
additional information
-
analysis of three-dimensional structure and active site structure
additional information
P14930
enzyme domain and active site structure, MsrB domain comprises residues 375-522, overview
additional information
-
MsrA, EC 1.8.4.11, and MsrB are fused together
additional information
-
MsrB activity is located on the C-terminal domain of PILB, the fused domains are folded entities
additional information
-
MsrB and enzyme MsrA, EC 1.8.4.11, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
-
MsrB has a highly conserved sequence among organisms
additional information
-
the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
-
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
-
solution structure and dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms
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
-
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
P14930
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 -170C
-
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 20C, 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
Q8P4Q6
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
half-life of MsrABTk is 30 min, half-life of MsrB domain is 31 min
687392
85
-
75% decrease in activity after 2.5 min, MsrABTk
687392
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap column chromatography and Sephadex G-25 gel filtration
-
recombinant plastidic isozyme pPMSR from Escherichia coli strain BL21(DE3)
-
recombinant plastidic isozymes MsrB1 and MsrB2 from Escherichia coli
-
partially, cell fragmentation
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
Q81NK9
recombinant enzyme from Escherichia coli strain DH5alpha
-
recombinant His-tagged enzyme from Escherichia coli
P0A746
recombinant MsrB
-
partially by subcellular fractionation
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant MsrB from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant isozyme MsrB3 from Escherichia coli strain BL21(DE3)
-
Ni-NTA column chromatography, and gel filtration
-
partial purification of native MsrB from liver, recombinant modified MsrB from Escherichia coli
-
recombinant C-terminally His-tagged wild-type and mutant MsrB to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heparin affinity chromatography
-
recombinant wild-type and mutant isozymes MsrB1 and MsrB2 from Escherichia coli strain BL21(DE3) and NIH-3T3 cells
-
Talon Co2+ affinity resin column chromatography
-
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion
P14930
recombinant His-tagged PilB forms in Escherichia coli strain Xl-1 blue 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 MsrB domain from Escherichia coli
-
recombinant enzyme from Escherichia coli
-
Ni2+-affinity column chromatography
Q9C8M2
recombinant His-tagged PilB from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis of plastidic isozymes MsrB1 and MsrB2, functional expression in Escherichia coli
-
expressed in Escherichia coli M15rep4 cells
-
expression of the plastidic isozyme pPMSR in Escherichia coli strain BL21(DE3) without the chloroplast signal sequence
-
genes msrA, EC 1.8.4.11, and msrB form an operon
-
expression His-tagged MsrB in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
B7S5L1
expression of the wild-type and mutant forms of MsrB in Escherichia coli
-
gene selR, DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli strain BL21(DE3)
Q81NK9
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
-
yeaA, overexpression of the His-tagged enzyme in Escherichia coli
P0A746
expressed in Escherichia coli BL21(DE3) cells and in yeast cytosol
-
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
-
CBS-1, overexpression of the His-tagged enzyme in Escherichia coli
-
expressed in Drosophila melanogaster
-
expressed in Drosophila melanogaster, in A-549 cells and human dermal fibroblasts
-
expression analysis in subcellular fractions of melanocytes, overview
-
expression of MsrB in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant isozyme MsrB3 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
-
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
-
transfection of MOLT-4 cell line by human MsrB2
-
subcloning in Escherichia coli
-
co-expressed with transient receptor potential melastatin type 6 in HEK-293 cells
-
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
Q8BU85
expressed in Escherichia coli BL21(DE3) and in HEK-293 cells
-
expressed in Escherichia coli ER2566 cells
-
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
-
MsrB2DELTAS containing one extra amino acid in N-terminal (Met) and a C-terminal His-tag is expressed in Escherichia coli
-
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
-
expressed in Escherichia coli BL21(DE3) cells
-
gene msr or pilB, DNA sequence determination and analysis
-
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
-
genes msrA and msrB are translationally fused
-
overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli
P14930
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
-
genes msrB and msrA, EC 1.8.4.11, are translationally fused
-
overexpression of the MsrB domain in Escherichia coli, strain B834(DE3) produces a selenomethionine-substituted MsrB
-
overexpression of wild-type and mutant enzymes in Escherichia coli
-
expression in Escherichia coli BL21
A7U629
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
-
overexpression of MsrB in a yeast strain, expression of MsrB as N-terminally 6His-tagged protein in Escherichia coli strain BL-21
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
the chromosome contains 2 copies of gene msrB, a plasmid harbors 1 copy of gene msrB
-
expressed in Escherichia coli BL21 (DE3)cells and in Saccharomyces cerevisiae strain BY4741
Q9C8M2
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
-
pilB is transcribed as polycistronic transcript, overexpression of PilB as His-tagged protein in Escherichia coliBL21(DE3)
-
expression inm Escherichia coli, recombinant proteins corresponding to MsrABTk and the individual domains (MsrATk and MsrBTk) are produced
-
chromosome 1 contains 2 genes msrB, chromosome 2 contains 1 gene msrB
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoforms MsrB7 and MsrB8 are induced by oxidative stress
-
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
B7S5L1
ENGINEERING
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
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
C121S
-
the mutant of isoform MSRB2 is inactive
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
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
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
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
U95C
-
the mutant has a significantly decreased activity
V81E
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
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
C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
additional information
-
cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation
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
additional information
-
construction of a MsrA/MsrB double mutant
additional information
-
construction of a msrA/msrB double mutant for detection of additional enzyme form activities
additional information
-
H2O2 shortens the life span of cells in constructed null mutants
C68S
-
the mutant of isoform MSRB2 is inactive
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
-
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
-
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
additional information
-
substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
W110A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
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
-
H77G/V81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
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
L38M/L41M
-
site-directed mutagenesis, mutation of the NT domain of PilB, thioredoxin binding structure, crystal structure analysis, 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
-
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 actvity but no thioredoxin recycling activity
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
W65F
-
site-directed mutagenesis, structural change of substrate binding and active site structure compared to the wild-type enzyme
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
C181S
Q9C8M2
inactive
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
enzyme is a target for modification of redox-dependent regulation
synthesis
-
enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs