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Enzyme Nomenclature
Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase
Word Map on EC 1.8.4.12
- 1.8.4.12
- thioredoxins
-
selenoproteins
-
msrbs
- selenium
- neisseria
-
sulfenic
-
metso
- trx
- methionine-s-sulfoxide
- meningitidis
-
thioredoxin-dependent
- plastidial
- synthesis
- biotechnology
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.8.4.12
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RECOMMENDED NAME
GeneOntology No.
peptide-methionine (R)-S-oxide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, Cys494 and Cys439 are involved
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
selenomethionine is essential for MsrB activity
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
three-step catalytic mechanism, influence of pH on reaction mechanism, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
mechanism, active site structure, conserved catalytic Cys residues, situated in the C-terminal end, are essential for activity, Cys residue recycling, overview
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
the active site selenocysteine SeC169 is essential for enzyme activity
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L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, modeling of substrate binding at the active site, Cys444 and Cys495 are involved
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
proposed catalytic mechanism of the reductase step of MsrB
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L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism involving residues at positions 95, 41, 97, 77, and 80, molecular modeling, role of selenocysteine- and cysteine residues in catalysis, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism and the role of cofactor recycling in vivo
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
catalytic mechanism, overview
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
formation of the MsrB substrate complex leads to an activation of the catalytic Cys-117 characterized by a decreased pKapp of about 2.7 pH units. The catalytic active MsrB form is the Cys117-/His103+ species with a pKapp of 6.6 and 8.3, respectively. His103 and to a lesser extent His100, Asn119, and Thr26 (via a water molecule) participate in the stabilization of the polarized form of the sulfoxide function and of the transition state. Trp65 is essential for the catalytic efficiency of the reductase step by optimizing the position of the substrate in the active site
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide [9]. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater [10]. The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well [11]. The enzyme from some species contains selenocysteine and Zn2+.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; 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
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strain 26695, enzyme forms MsrA and MsrB are fused together forming a single protein termed Msr
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strain MS11, variant VD300, bifunctional enzyme MsrA/B, gene pilB
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; 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
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gene msrB, enzyme SelR which is a selenoprotein, enzyme is organized in a fusion protein together with MsrA, EC 1.8.4.B2
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; 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
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strain 26695, enzyme forms MsrA and MsrB are fused together forming a single protein termed Msr
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MsrB variants one of which is also called Sel-X, encoded by distinct genes, MsrB is a selenoprotein
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; 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
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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
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
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; gene msr encodes an enzyme showing both MsrA, EC 1.8.4.B2, and MsrB activity
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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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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
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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
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2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
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the concomitant absence of both protein isoforms MSRB1 and MSRB2 results in a reduced growth for plants cultivated under high light or low temperature, double mutant lines restored for MSRB2 expression display no phenotype, the absence of plastidial MSRBs is associated with an increased chlorophyll a/b ratio, a reduced content of Lhca1 and Lhcb1 proteins, and an impaired photosynthetic performance
malfunction
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deficiency in MsrB enzyme reduces the level of Enterococcus faecalis virulence in a systemic and urinary tract infection model
malfunction
loss-of-function studies of MsrB2 using virus-induced gene silencing in pepper plants (cultivar Early Calwonder-30R) result in accelerated cell death from an incompatible bacterial pathogen, Xanthomonas axonopodis pv vesicatoria race 1, and enhanced susceptibility to a compatible bacterial pathogen, virulent Xanthomonas axonopodis pv vesicatoria race 3. Suppression of CaMsrB2 increased the production of reactive oxygen species, which in turn results in the acceleration of cell death via accumulation of reactive oxygen species
malfunction
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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
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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
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cytosolic MsrB7 and MsrB8 knockdown lines are sensitive to oxidative stress
malfunction
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deficiency in MsrB enzyme reduces the level of Enterococcus faecalis virulence in a systemic and urinary tract infection model
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physiological function
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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
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MSRB2 plays an important function in protecting cones from multiple type of oxidative stress and is critical in preserving central vision
physiological function
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MSRB2 plays an important function in protecting cones from multiple type of oxidative stress and is critical in preserving central vision
physiological function
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MsrB is important for the oxidative stress response, macrophage survival, and persistent infection with Enterococcus faecalis
physiological function
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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
MsrB2 is a defense regulator against oxidative stress and pathogen attack, MsrB2 causes enhanced resistance to Phytophthora capsici and Phytophthora infestans
physiological function
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oxidative stress can lead to oxidation of methionine residues, which are repaired by MsrB1
physiological function
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MsrB of plays only a limited role in resisting intracellular and in vitro reactive oxygen intermediates
physiological function
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neuronal expression of isoform MsrB3A renders Drosophilaflies resistant to oxidative stress. These flies also show significantly enhanced cold (4°C) and heat (37°C) tolerance. Expression of isoform MsrB3A in the whole body and nervous system extends the lifespan of fruit flies at 29°C by 43-50% and 12-37%, respectively. Additionally, isoform MsrB3A overexpression significantly delays the age-related decline in locomotor activity and fecundity
physiological function
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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
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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
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the MSRB1 gene plays a critical role in protecting against oxidative stress
physiological function
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MsrB is important for the oxidative stress response, macrophage survival, and persistent infection with Enterococcus faecalis
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin
L-methionine methyl ester + thioredoxin disulfide + H2O
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the affinity of MsrB to acetyl-L-methionine (R)-sulfoxide methyl ester is higher than to L-methionine (R)-sulfoxide
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-
?
calmodulin-L-methionine (R)-S-oxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
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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
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-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + 1,4-dithioerythritol
dabsyl-L-methionine + 1,4-dithioerythritol disulfide + H2O
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-
-
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?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (R)-sulfoxide + glutaredoxin S12
dabsyl-L-methionine + ?
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?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
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-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
DL-methionine (R)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
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enzyme MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
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?
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
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membrane-bound enzyme form Mem-R,S-Msr
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-
?
L-methionine-(R)-S-oxide + dithioerythritol
L-methionine + dithioerythritol disulfide + H2O
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absolute stereospecific reduction, MsrB1 and MsrB2
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?
L-methionine-(R)-S-oxide + DTT
L-methionine + thioredoxin disulfide + H2O
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isozymes MsrB1, MsrB2, and MsrB3
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-
?
N-acetyl-L-methionine (R)-sulfoxide + dithiothreitol
N-acetyl-L-methionine + dithiothreitol disulfide + H2O
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-
-
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?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine (R)-sulfoxide methyl ester + thioredoxin
N-acetyl-L-methionine methyl ester + thioredoxin disulfide
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enzyme MsrB
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?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
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enzyme reduces L-methionine (R)-sulfoxide of the protein substrate
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-
?
oxidized chloroplast signal particle protein 43 + ?
reduced chloroplast signal particle protein 43 + ?
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-
-
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?
oxidized chloroplast signal particle protein 54 + ?
reduced chloroplast signal particle protein 54 + ?
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-
-
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?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
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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
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-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
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type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
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-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
Met sulfoxide residues in an Met-rich proteins can be reduced by MsrA and MsrB
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-
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
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type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
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-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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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
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-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
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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
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-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
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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
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-
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
isoforms MSRB2 and MSRB4 also show enzyme activity toward protein-based L-methionine (R)-sulfoxide with either dithiothreitol or thioredoxin as reductants, whereas isoform MSRB1 is active only with dithiothreitol
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
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thioredoxin f1, thioredoxin m1, thioredoxin m2, thioredoxin m3, thioredoxin m4, thioredoxin x, thioredoxin y1, thioredoxin y2
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
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FMsr is specific for the R-isomer
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond. Thioredoxin- and dithiothreitol-dependent activities are approximately equal
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
activity with Escherichia coli thioredoxin, NtMsrB21
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Hsp21 contains 6 methionine residues at positions 49, 52, 55, 59, 62, and 67, about half of the residues are reduced by the enzyme probably due to its stereospecificity
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide
-
the MsrB-domain of MsrABTk is strictly specific for the reduction of L-methionine (R)-sulfoxide
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of L-methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are peptides and proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
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
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Msr is specific for the R-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB is specific for the R-isomer, no activity with the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of the substrate
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the native MsrB as well as the recombinant modified MsrB show absolute specificity for the R-form of free and protein-bound methionine sulfoxide, no activity with the S-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
specific substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB activity of the tandem domains of PilB, the MsrB domain alone does not utilize the S-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the (R)-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
PilB shows absolute specificity for the R-form of free and protein-bound methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
specific substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
absolute stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
absolute stereospecific reduction, isozyme MsrB2, no activity with isozyme MsrB1
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrB accepts free and protein-bound substrates
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
isozymes MsrB1, MsrB2, and MsrB3
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, preferred substrate of isozyme MsrB2
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine-(R)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
-
highest activity by a membrane bound enzyme form Mem-R,S-Msr, which preferentially reduces the R-substrate form, no activity by enzyme forms fRMsr, fSMsr, low activity by enzyme forms MsrB
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview
-
-
-
additional information
?
-
-
substrate specificity, overview, isozyme MsrB1 is not able to reduce free L-methionine-(R)-S-oxide or N-acetyl-L-methionine-(R)-S-oxide, while isozyme MsrB2 prefers protein-bound substrates such as N-acetyl-L-methionine (R)-S-oxide, overview
-
-
-
additional information
?
-
-
the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
-
-
-
additional information
?
-
-
MsrB3 plays an important role in cold tolerance by eliminating methionine sulfoxide and reactive oxygen species that accumulate at the endoplasmic reticulum during cold acclimation
-
-
-
additional information
?
-
-
the CDSP32 thioredoxin forms a heterodimeric complex with MSRB1 through its catalytic cysteine, Cys219, via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
enzyme provides protection for the cell against oxidative stress
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
-
additional information
?
-
-
MsrB is specific for the R-form of the substrate
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
substrate specificity of enzyme forms with R-form of free and protein-bound methionine sulfoxide, overview
-
-
-
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates, the membrane-associated isozyme also shows MsrA activity utilizing L-methionine (S)-sulfoxide and N-acetyl-L-methionine (S)-sulfoxide as substrates
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
the enzyme also exhibits MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzyme also exhibits MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
-
downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
-
additional information
?
-
-
enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
-
additional information
?
-
-
the enzyme utilizes free and protein-bound methionine-(R)-S-oxide as substrate, but prefers the latter, methionine oxidation inactivates the proteins showing equal distribution of S-MetO and R-MetO
-
-
-
additional information
?
-
-
the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
-
-
-
additional information
?
-
Sp1 transcription factor may play a central role in expression of the human MsrB1 gene. The MsrB1 promoter activity appears to be controlled by epigenetic modifications such as methylation
-
-
-
additional information
?
-
MsrB3 physically interacts with the sulfenic acid intermediate of these oxidized enzymes to directly form an intermolecular disulfide bond
-
-
-
additional information
?
-
-
methionine-oxidized amyloid fibrils (methionine-oxidized monomer and fibrillar apoC-II) are poor substrates for human methionine sulfoxide reductase B2. At Msr concentrations of more than 0.0005 mM, approximately 90% of monomeric MetO-apoCII is reduced. In contrast, at 0.0005 mM Msr, only 35% of fibrillar MetO-apoC-II is reduced, which increased to only 37% after incubation with a 4fold higher enzyme concentration
-
-
-
additional information
?
-
-
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 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
?
-
-
enzyme provides protection for the cell against oxidative stress
-
-
-
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, 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
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
-
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
?
-
-
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
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
-
-
-
additional information
?
-
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
?
-
-
The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, 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
?
-
-
PilB affects the survival of the organism to reactive oxygen species, PilB is not involved in piliation, pilin production, or adherence
-
-
-
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
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
substrate specificities of enzymes, the reduction step is rate-determining
-
-
-
additional information
?
-
-
substrate specificity of MsrB activity, diverse substrates, 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 secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
-
additional information
?
-
the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
-
-
-
additional information
?
-
NtMsrB1 shows no activity with dithiothreitol
-
-
-
additional information
?
-
-
NtMsrB1 shows no activity with dithiothreitol
-
-
-
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
?
-
-
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
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme 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 protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
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
?
-
-
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 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
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
isoform MSRB1 exhibits no activity in thioredoxin dependent system
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
-
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
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
the reduction step is rate-determining
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
-
-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine (R)-S-oxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
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
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine-(R)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme form MsrB is specific for the R-form, enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Q8INK9
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrB is specific for the R-form, MsrB enzyme form variants with specificities for either free or protein-bound methionine, Mem-R,S-Msr also posesses MsrA activity utilizing L-methionine (S)-sulfoxide as substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are peptides and proteins
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
important antioxidant enzyme and colonization factor in the gastric pathogen, a methionine repair enzyme responsible for stress resistance
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
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
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
Msr is specific for the R-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
protein-bound methionine residues
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
Q9JLC3
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is absolute specific for the R-form, no activity with the S-form, pathway overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form of the substrate
-
-
ir
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
together with the enzyme MsrA, EC 1.8.4.11, which is absolutely specific for the S-form substrate, the enzyme can repair methionine-damaged proteins and salvage free methionine under oxidative stress int the living cell
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is stereospecific for the R-epimer of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB specifically reduces the R-form of methionine sulfoxide
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the (R)-form of the substrate
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is specific for the R-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
-
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
-
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
-
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
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
-
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
-
absolute stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrB is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
r
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, the isozymes of MsrB are involved in lens cell viability and oxidative stress protection
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the cofactor thioredoxin can be recycled in vivo by thionein due to its high content of cysteines, overview
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
-
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 + H2O
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrB protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview
-
-
-
additional information
?
-
-
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
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
paraquat induces the expression of msrAB partially through an oxidation on Spx (a global oxidative stress regulator) via modification of its CXXC motif
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
Q8INK9
enzyme provides protection for the cell against oxidative stress
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
-
additional information
?
-
-
enzyme contributes to resistance against cadmium, physiological role
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, the MsrA/MsrB repair pathway is involved in the signal recognition particle-dependent protein targeting pathway, regulation mechanism of gene expression, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
-
downregulation of CBS-1 during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
-
additional information
?
-
-
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
?
-
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 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 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
?
-
-
enzyme provides protection for the cell against oxidative stress
-
-
-
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, 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
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
-
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
?
-
-
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, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
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
?
-
-
The thioredoxin domain of PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases, overview
-
-
-
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
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme 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 protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
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
?
-
-
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
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
-
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
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrB has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
-
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
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
MsrB can also utilize DTT as reductant, the membrane-isozyme shows only poor activity
dithiothreitol
-
absolutely dependent on in vitro and in vivo with substrate Hsp21
dithiothreitol
-
can act as cofactor only in vitro showing a much higher activity than thioredoxin
thioredoxin
-
PilB contains an N-terminal thioredoxin-like domain, the NT domain, fused to the MsrA and MSrB domains, structure overview
thioredoxin
-
preferred and natural cofactor, the cofactor can be recycled in vivo by reduction via zinc-containing metallothionein, Zn-MT, after removal of the zinc ion due to its high content of cysteines, mechanism, overview
thioredoxin
-
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
-
-
additional information
-
no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
-
additional information
-
DTT can partially substitute for thioredoxin in vitro, low activity
-
additional information
-
DTT can substitute for thioredoxin in vitro
-
additional information
-
DTT can substitute for thioredoxin in vitro
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
with Zn2+ in a ratio of 1 mol per mole of enzyme, tight metal binding
selenium
Zinc
Zn2+
additional information
selenium
-
the selenocysteine-containing Clostridium MsrB form exhibits 100fold higher activity than its Cys-containing form, revealing that selenocysteine provides the catalytic advantage of higher activity. A resolving Cys is required for the thioredoxin-dependent recycling process of the selenocysteine-containing form. Thus, thioredoxin can reduce the selenylsulfide bond, but its Trx-dependent recycling process is much less efficient compared to that for the disulfide bond in the Cys-containing form, demonstrating an obvious catalytic disadvantage
selenium
-
selenoprotein. Se status affects Msr (most likely through effects on the selenoprotein MsrB)
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes
Zn2+
-
binding by residues at positions 45, 48, 94, and 97, 2 CXXC-motifs, role in catalysis
Zn2+
-
with Fe2+ in a ratio of 1 mol per mole of enzyme, tight metal binding, the metal binding site is composed of two CXXC motifs located at the opposite side of the active site, role in catalysis and structural stability, overview
Zn2+
-
about 50% of MsrB binds a zinc atom in opposite direction of the active site, enzyme contains the CXXC motif, binding of Zn2+ modulates the catalytic efficiency via structural changes
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
enzyme belongs to the metal-containing MsrB group I, metal binding by 2 CXXC-motifs, role in catalysis
Zn2+
-
about 50% of MsrBs binds a zinc atom in opposite direction of the active site
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
enzyme belongs to the metal-containing MsrB group I
additional information
-
the zinc:iron ratio is 8:2 to 6:4, metal content of wild-type and mutant enzymes, overview
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
native isozyme MsrB1 contains selenocysteine, while native isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
additional information
-
isozyme MsrB1 contains selenocysteine, while isozymes MsrB2 and MsrB3 contain cysteine residues, the thioredoxin dependence is different for selenocysteine- and cysteine-containing enzyme, overview
additional information
-
content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview
additional information
-
wild-type MsrB of Neisseria meningitidis is no metal-binding enzyme, but contains a preformed metal binding site, metal binding to MsrB results in inhibition of binary complex formation between oxidized MsrB and reduced thioredoxin but not between reduced MsrB and substrate, metal content of wild-type and mutant enzymes, overview
additional information
-
the major isozyme of MsrB, MsrB1, is a selenoprotein, selenium affects the expression of MsrB
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
dimedone
-
binds specifically to the sulfenic acid reaction intermediate
additional information
-
no inhibition by EDTA, 1,10-phenanthroline, and pyridine 2,6-dicarboxylic acid
-
additional information
-
selenium-adequate diet retains MsrB mRNA and protein expression at basal levels
-
additional information
-
enzyme expression decreases during dehardening from 4°C to 22°C of cold-acclimated plants, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
selenium-adequate diet retains MsrB mRNA and protein expression at basal levels
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
expression of MsrB is induced by dehydration and H2O2
-
additional information
-
heat shock, dehydration, and reactive oxygen species like H2O2 induce the expression of MsrB
-
additional information
-
oxidative stress, e.g. caused by H2O2 up to 0.4 mM, induces enzyme expresssion
-
additional information
-
enzyme is induced under oxidative stress and heat shock
-
additional information
-
MsrB expression is induced by heat shock and alkylating methyl-methanesulfonate treatment
-
additional information
-
starvation induces MsrB expression, also heat treatment and methylmethanesulfonate induce the enzyme
-
additional information
-
48 h exposure to high light at 22°C induces enzyme expression, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
the msrA1-msrB operon is induced by antibiotics
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00021
CDSP32
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.00053
glutaredoxin S12
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
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
0.0091
dithiothreitol
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C
0.03
dithiothreitol
-
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
0.05
dithiothreitol
-
mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
2
dithiothreitol
-
MsrB domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide
1.451
L-methionine (R)-sulfoxide
-
isoform MSRB4, pH and temperature not specified in the publication
2.093
L-methionine (R)-sulfoxide
-
isoform MSRB2, pH and temperature not specified in the publication
67
L-methionine (R)-sulfoxide
-
MsrB domain of MsrABTk, in the presence of 20 mM dithiothreiol
0.054
L-methionine-(R)-S-oxide
-
recombinant isozyme MsrB2, with dithioerythritol
0.079
L-methionine-(R)-S-oxide
-
recombinant isozyme MsrB1, with dithioerythritol
0.31
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB2 expressed in Escherichia coli
0.5
L-methionine-(R)-S-oxide
-
recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.8
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
1.3
L-methionine-(R)-S-oxide
-
recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.058
thioredoxin
-
MsrB, pH 8.0, 25°C, substrate acetyl-L-methionine (R)-sulfoxide N-methyl ester
0.66
thioredoxin
-
wild type enzyme, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
7
thioredoxin
-
mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C
additional information
additional information
-
stopped flow kinetics, steady-state kinetics
-
additional information
additional information
-
thioredoxin- and DTT-dependent kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
thioredoxin- and DTT-dependent kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant MsrB
-
additional information
additional information
-
thermodynamics and kinetics of wild-type and mutant MsrB
-
additional information
additional information
-
reductase step kinetic parameters of the wild-type and mutated MsrB
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
CDSP32
Arabidopsis sp.
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.09
dithiothreitol
Solanum lycopersicum
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C
2.8
L-methionine (R,S)-sulfoxide
Neisseria meningitidis
-
MsrB activity of PILB, pH 8.0, 25°C
0.002
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB1 wild type enzyme, in the presence of 20 mMTris(2-carboxyethyl) phosphine hydrochloride
0.005
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB1 mutant T132C, in the presence of 20 mM dithioerythritol
0.012
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB1 mutant T132A, in the presence of 20 mM dithioerythritol
0.014
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB2 wild type enzyme, in the presence of 20 mMTris(2-carboxyethyl) phosphine hydrochloride
0.028
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB2 wild type enzyme, in the presence of 20 mM dithioerythritol
0.047
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB1 mutant C116S, in the presence of 20 mM dithioerythritol
0.064
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB2 mutant C134T, in the presence of 20 mM dithioerythritol
0.075
dabsyl-L-methionine (R)-sulfoxide
Arabidopsis thaliana
-
isoform MSRB1 wild type enzyme, in the presence of 20 mM dithioerythritol
0.17
glutaredoxin S12
Arabidopsis sp.
-
pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity
-
0.13
L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB4, pH and temperature not specified in the publication
2.86
L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB2, pH and temperature not specified in the publication
0.002
L-methionine-(R)-S-oxide
Mus musculus
-
recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.02
L-methionine-(R)-S-oxide
Arabidopsis thaliana
-
recombinant isozyme MsrB2, with dithioerythritol
0.07
L-methionine-(R)-S-oxide
Arabidopsis thaliana
-
recombinant isozyme MsrB1, with dithioerythritol
0.22
L-methionine-(R)-S-oxide
Mus musculus
-
recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells
0.46
L-methionine-(R)-S-oxide
Mus musculus
-
recombinant wild-type isozyme MsrB2 expressed in Escherichia coli
0.83
L-methionine-(R)-S-oxide
Homo sapiens
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
0.24
N-acetyl-L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB4, pH and temperature not specified in the publication
2.04
N-acetyl-L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB2, pH and temperature not specified in the publication
additional information
additional information
Neisseria meningitidis
-
reductase step kinetic parameters of the wild-type and mutated MsrB
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
dithiothreitol
Solanum lycopersicum
-
recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C
45
0.09
L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB4, pH and temperature not specified in the publication
8608
1.4
L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB2, pH and temperature not specified in the publication
8608
5
N-acetyl-L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB4, pH and temperature not specified in the publication
14726
42
N-acetyl-L-methionine (R)-sulfoxide
Glycine max
-
isoform MSRB2, pH and temperature not specified in the publication
14726
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000029
-
wild-type strain RN450, substrate L-methionine (R)-sulfoxide
0.00003
-
msrA2 knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.000046
-
purified recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.0012
-
msrA1 knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.0015
-
msrA1/msrA2 double knockout strain RN450, substrate L-methionine (R)-sulfoxide
0.002
-
purified recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and DTT
0.01
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.023
0.045
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.075
purified recombinant MsrA/MsrB tandem domain, substrate L-methionine (R)-sulfoxide
0.085
purified recombinant CBS-1, substrate L-methionine (R)-sulfoxide
0.11
0.128
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.17
-
purified recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells, substrates are L-methionine-(R)-S-oxide and DTT
0.173
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.386
-
purified recombinant wild-type isozyme MsrB2 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
0.452
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
additional information
0.023
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.11
purified recombinant MsrB domain alone, substrate L-methionine (R)-sulfoxide
additional information
-
thioredoxin- and DTT-dependent activities of mutant enzymes, overview
additional information
-
tissue specific activity, activity in tissues of MsrA-deficient mutant mice
additional information
-
thioredoxin- and DTT-dependent activities of mutant enzymes, overview
additional information
-
recombinant activity in overexpressing yeast cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
7.4
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
epithelia and fibers, isozymes MsrB1 or selenoprotein R, MsrB2 or CBS-1, and MsrB3, differential expression patterns of isozymes, overview
additional information
-
expression/activities of MSRA and MSRB are significantly decreased in the epidermis of patients with vitiligo compared to healthy controls
-
cell line WI-38, young and old cells, enzyme expression pattern during cell development, senescent cells show decreased enzyme expression and activity
-
marginal Zn deficiency has little effect on Msr in liver and kidney. Msr activity is significantly reduced by Se deficiency
-
MsrB1 is present in the renal Mg2+-transporting distal convoluted tubules
-
marginal Zn deficiency has little effect on Msr in liver and kidney. Msr activity is significantly reduced by Se deficiency
-
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
-
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
-
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
-
chronic sun-exposure would result in a decreased expression of two main components of the methionine sulfoxide reductase system, MsrA and MsrB2
-
fibroblast, young and old cells, enzyme expression pattern during cell development
-
embryonic fibroblast, activity during development: downregulation during replicative senescence
-
MsrB2 is downregulated during replicative senescence of WI-38 human fibroblasts
additional information
-
high expression level of the plastidic isozyme pPMSR in photosynthetic active tissue
additional information
-
tissue distribution, main expression of CBS1 in muscle tissues, overview
additional information
-
enzyme expression level and methionine sulfoxide content in fibroblasts during development, overview
additional information
-
presence of MsrABTk is greater in Thermococcus kodakaraensis cells grown at suboptimal temperatures (60 to 70°C) and could not be detected at 80 to 90°C. The amount of intracellular MsrABTk protein increases with exposure to higher dissolved oxygen levels, but only at suboptimal growth temperatures
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secretion of MsrA, EC 1.8.4.11, and MsrB fused together
-
additional information
-
plastidic isozymes MsrB1 and MsrB2, analysis of subcellular localization
-
Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf
-
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
-
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
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
-
Sel-X, a MsrB enzyme form variant, sulindac reducing activity in calf
-
MsrB3B contains a different signal peptide at the N-terminus and is targeted to mitochondria
additional information
-
subcellular sulindac reducing activity distribution in calf liver
-
additional information
-
subcellular targeting is determined by alternative splicing
-
additional information
subcellular localization analysis, no localization of MsrB3 in the mitochondria
-
additional information
-
subcellular targeting is determined by alternative splicing
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5000
-
MsrB1 occurs in two protein forms that migrate as 14000 and 5000 Da proteins, SDS-PAGE
14000
-
MsrB1 occurs in two protein forms that migrate as 14000 and 5000 Da proteins, SDS-PAGE
16374
-
x * 16374, about, recombinant wild-type MsrB domain, mass spectrometry
16860
-
reduced isoform MSRB2, calculated from amino acid sequence; reduced isoform MSRB2, MALDI-TOF mass spectrometry
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 16374, about, recombinant wild-type MsrB domain, mass spectrometry
?
-
x * 16372.0, recombinant MsrB, mass spectrometry, x * 16467.2, recombinant selenomethionine-MsrB, mass spectrometry
additional information
-
analysis of three-dimensional structure and active site structure
additional information
-
MsrB has a highly conserved sequence among organisms
additional information
-
analysis of three-dimensional structure and active site structure
additional information
-
the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
analysis of three-dimensional structure and active site structure
additional information
enzyme domain and active site structure, MsrB domain comprises residues 375-522, overview
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
-
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
-
analysis of three-dimensional structure and active site structure
additional information
-
solution structure and dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging-drop vapor-diffusion method. The crystals belong to the trigonal space group P3, with unit-cell parameters a = b = 136.096, c = 61.918 , and diffracted to 2.5 A resolution
-
purified recombinant detagged MsrB domain containing SeMet39, hanging drop vapour-diffusion method, 15 mg/ml protein in 20 mM Tris, pH 8.5, 10% v/v glycerol, against a well solution containing 0.1 M sodium cacodylate, pH 6.5, 30% w/v PEG 4000, room temperature, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
purified recombinant PilB mutant L38M/L41M, vapour diffusion method, 30 mg/ml protein in 20 mM HEPES, pH 7.5, and 100 mM NaCl, is mixed with well solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 26% PEG 2000 monomethylester, and 25% glycerol, X-ray diffraction structure determination and analysis at 1.6 A resolution, multiwavelength anomalous dispersion at -170°C
-
batch method, using 30% PEG 400, 0.1 M Tris-HCl (pH 8.5), and 0.2 M Na-citrate
-
selenomethionine-substituted peptide methionine sulfoxide reductase B domain, hanging drop vapour diffusion method in multiwell tissue-culture plates, 0.004 ml protein solution containing 75 mg/ml protein in 50 mM Tris-HCl, pH 8.0, mixed with 0.004 ml precipitant solution at 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution
-
batch method, crystals of the oxidized form are obtained by 32% PEG 4000, 0.8 M LiCl, and 0.1 M Tris HCl (pH 8.5), no crystal is obtained for wild type Xanthomonas campestris MsrB in its reduced form
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
half-life of MsrABTk is 30 min, half-life of MsrB domain is 31 min
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial purification of native MsrB from liver, recombinant modified MsrB from Escherichia coli
-
recombinant His-tagged enzyme from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion
recombinant His-tagged PilB forms in Escherichia coli strain Xl-1 blue by nickel affinity chromatography
-
recombinant His-tagged PilB from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant N-terminally His-tagged full-length PilB and MsrB domain variants from Escherichia coli by nickel affinity chromatography followed by cleavage of the His-Tag through thrombin, followed by gel filtration and ion exchange chomatography
-
recombinant plastidic isozyme pPMSR from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heparin affinity chromatography
-
recombinant wild-type and mutant isozyme MsrB3 from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant isozymes MsrB1 and MsrB2 from Escherichia coli strain BL21(DE3) and NIH-3T3 cells
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 genes msrA and 1 gene msrB form an operon, one of the 3 msrA genes is fused to the msrB gene, genetic organization and regulation, overview
-
co-expressed with transient receptor potential melastatin type 6 in HEK-293 cells
-
DNA and amino acid sequence determination and analysis of plastidic isozymes MsrB1 and MsrB2, functional expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
endoplasmic reticulum isozyme MsrB3, DNA and amino acid sequence determination and analysis, expression of different constructs of GFP-tagged MsrB3 in monkey kidney CV-1 cells or in mouse fibroblast NIH 3T3 cells
expressed in Drosophila melanogaster, in A-549 cells and human dermal fibroblasts
-
expressed in Escherichia coli BL21 (DE3)cells and in Saccharomyces cerevisiae strain BY4741
-
expressed in Escherichia coli BL21(DE3) cells
expression inm Escherichia coli, recombinant proteins corresponding to MsrABTk and the individual domains (MsrATk and MsrBTk) are produced
-
expression of the plastidic isozyme pPMSR in Escherichia coli strain BL21(DE3) without the chloroplast signal sequence
-
expression of wild-type and mutant isozyme MsrB3 in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant isozymes MsrB1 and MsrB2 in Escherichia coli strain BL21(DE3) and in NIH-3T3 cells
-
gene msrB with the codon for selenomehinonine is exchanged for methionine, overexpression in Escherichia coli
-
gene msrB, located in the chromosome at 40.09 min, respectively, regulation mechanism of gene expression, overview
-
gene msrB, overexpression of wild-type enzyme and mutant enzymes in Escherichia coli strain DH5alpha
-
gene pilB, expression of N-terminally His-tagged full-length wild-type and mutant PilB and MsrB domain variants in Escherichia coli
-
gene pilB, transposon insertion, truncated PilB enzyme forms of the enzyme lacking the MsrA domain from strain MS11, variant VD300, overexpression of the His-tagged PilB forms in Escherichia coli strain Xl-1 blue
-
gene selR, DNA and amino acid sequence determination and analysis, expression as His-tagged enzyme in Escherichia coli strain BL21(DE3)
human MOLT-4 cell line are stably transfected with the pLXSN retroviral expression vector based on the Moloney murine leukemia virus and Moloney murine sarcoma virus to generate a replication-deficient recombinant retrovirus containing the rat MsrA and the human MsrB2 cDNA. The oxidized protein repair enzymes MsrA and MsrB2, when overexpressed in the cells, are able to counteract the zinc-mediated damaging effects
-
mitochondrial and cytosolic isozymes are encoded on a single gene with 2 initiations sites, delivering an N-terminal signal peptide to the mitochondrial enzyme form
-
msr gene, DNA sequence determination and analysis, subcloning in Escherichia coli strain DH5-alpha, functional complementation of the enzyme-deficient mutant with the wild-type gene
-
MsrB2DELTAS containing one extra amino acid in N-terminal (Met) and a C-terminal His-tag is expressed in Escherichia coli
-
overexpression of MsrB in a yeast strain, expression of MsrB as N-terminally 6His-tagged protein in Escherichia coli strain BL-21
-
overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli
overexpression of the MsrB domain in Escherichia coli, strain B834(DE3) produces a selenomethionine-substituted MsrB
-
overexpression of truncated wild-type and mutant enzymes as His-tagged proteins in Escherichia coli, functional coexpression of CBS1 in oocytes with Drosophila melanogaster ShC/B potassium channel
-
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpression of wild-type and mutants in Escherichia coli, expression as N- or C-terminally 6His-tagged protein lowers the recombinant expression level to 3% of total enzyme expressed, labeling of expressed wild-type with 75SeMet
-
pilB is transcribed as polycistronic transcript, overexpression of PilB as His-tagged protein in Escherichia coliBL21(DE3)
-
the chromosome contains 2 copies of gene msrB, a plasmid harbors 1 copy of gene msrB
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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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
C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
T132A
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
T132C
-
MSRB1 mutant with decreased kcat values for dabsyl-L-methionine (R)-sulfoxide compared to the wild type enzyme
C45D/C48S/C94S/C97S
-
site-directed mutagenesis, the mutant MsrB loses binding ability for Zn2+ and Fe2+, and shows no catalytic activity in presence of thioredoxin or DTT, substitution of the two cysteine residues of MsrB results in complete loss of the enzyme's metal binding and reductase activity
C105S
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
C169S
-
site-directed mutagenesis, active site mutant, completely inactive mutant
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to highly reduced activity with cofactor thioredoxin or DTT compared to wild-type MsrB3
H77G/I81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
I81E
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to slightly increased activity with cofactor thioredoxin and reduced activcity with DTT compared to wild-type MsrB3
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB3
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant shows highly reduced activity with cofactor DTT or thioredoxin compared to wild-type MsrB3
W110A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
C98S
-
the mutant show increased Km values with dithiothreitol (1.7fold) and thioredoxin (6fold) compared to the wild type enzyme
E81V
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB1s
F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, the selenocysteine-containing mutant shows reduced activity with either cofactor thioredoxin and DTT compared to wild-type selenocysteine MsrB1, while the cysteine-containing mutant shows activity and kinetics similar to the wild-type cysteine MsrB1
G77H/E81V/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
G77H/F97N
-
site-directed mutagenesis, mutation in the selenocysteine-containing or the cysteine-containing isozyme MsrB1, both mutants show altered activity and kinetics compared to wild-type MsrB1s
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB2 leads to highly reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
H77G/N97F
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site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
H77G/V81E/N97F
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site-directed mutagenesis, mutation of isozyme MsrB2, inactive mutant
N97F
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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
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site-directed mutagenesis, mutation of isozyme MsrB2, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB2
V81E
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site-directed mutagenesis, mutation of isozyme MsrB2 leads to reduced activity with either cofactor thioredoxin and DTT compared to wild-type MsrB2
L38M/L41M
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site-directed mutagenesis, mutation of the NT domain of PilB, thioredoxin binding structure, crystal structure analysis, overview
C439S
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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
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site-directed mutagenesis, MsrA domain of PILB, inactive mutant
C63S
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site-directed mutagenesis, the mutant accumulates the sulfenic acid intermediate, while the wild-type accumulates the disulfide intermediate
D45C/S48C/S94C/A97C
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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
W65F
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site-directed mutagenesis, structural change of substrate binding and active site structure compared to the wild-type enzyme
additional information
additional information
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cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation
additional information
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construction of a msrA/msrB double mutant for detection of additional enzyme form activities
additional information
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H2O2 shortens the life span of cells in constructed null mutants
additional information
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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
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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
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additional information
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substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
additional information
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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
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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
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additional information
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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
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construction of MsrB null mutant and of overexpressing strains, phenotypes, overview
additional information
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substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
additional information
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mutant strains produce a truncated version of fused MsrA/MsrB with increased sensitivity to H2O2 and superoxide anions
additional information
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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
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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
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additional information
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mutation of the recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, while exchange of the catalytic Cys for Ser causes complete loss of activity
additional information
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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
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yeast cells lacking MsrB show increased sensitivity to oxidative damage, and methionine-(R)-S-oxide accumulation
additional information
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H2O2 shortens the life span of cells in constructed null mutants
additional information
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mutation of the msr genes impair virulence, overview, mutation of the msrA1 operon leads to increased susceptibility to H2O2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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enzyme is a target for modification of redox-dependent regulation
synthesis
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enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs
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