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Enzyme Nomenclature
Information on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.8.4.11
-
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RECOMMENDED NAME
GeneOntology No.
peptide-methionine (S)-S-oxide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
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-
-
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys72, Cys218 and Cys228 are involved
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys52 is involved
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism involves the formation of a sulfenic acid intermediate
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L-methionine (S)-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 (S)-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 (S)-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 (S)-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 (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism and structural features, roles of cysteine residues, active site structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism of MsrA, active site structure, modeling of protein-bound methionine sulfoxide recognition and repair from the crystal structure
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
catalytic mechanism of MsrA, the rate limiting step occurs after formation of the sulfenic acid intermediate and is associated with either the Cys51/Cys198 disulfide bond formation or the thioredoxin reduction process
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L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
reaction mechanism, modeling of substrate binding at the active site, Cys72 is involved
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
proposed catalytic mechanism of the reductase step of MsrA
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L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
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-
-
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
catalytic mechanism, Cys72 is essential for activity forming disulfide bonds with either Cys218 or Cys227
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
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-
-
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peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
catalytic mechanism, rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin and formation of the thiosulfenic acid intermediate on Cys51
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
presence of at least two binding subsites. The first one, whose contribution is major in the efficiency of the reductase step and in which the epsilon-methyl group of MetSO binds, is the hydrophobic pocket formed by Phe52 and Trp53, the position of the indole ring being stabilized by interactions with His186 and Tyr189. The second subsite composed of Asp129 and Tyr197 contributes to the binding of the main chain of the substrate but to a lesser extent
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SYSTEMATIC NAME
IUBMB Comments
peptide-L-methionine:thioredoxin-disulfide S-oxidoreductase [L-methionine (S)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for the reduction of the S-form of L-methionine S-oxide, acting faster on the residue in a peptide than on the free amino acid [9]. On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly [9]. 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 1.8.4.12, peptide-methionine (R)-S-oxide reductase, are found within the same protein whereas, in other species, they are separate proteins [1,4]. The reaction proceeds via a sulfenic-acid intermediate [5,10].
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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 enzyme termed Msr
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strain MS11, variant VD300, bifunctional enzyme MsrA/B, gene pilA
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strain MS11A derivatives, 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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strains VT1169 and VT1530 derived from the clinical strain SUNY 465
Uniprot
isozyme PMSRA1; isozyme PMSRA2; isozyme PMSRA3; isozyme PMSRA4
SwissProt
gene Eip71CD or Eip28/29; alternative splicing variants, overview
SwissProt
gene msrA, enzyme is organized in a fusion protein together with MsrB, EC 1.8.4.B1
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wild-type strain MC1061, isozyme MsrA, a membrane-associated isozyme, and a soluble isozyme MsrA1
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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 enzyme termed Msr
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SwissProt
; 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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posesses 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
SwissProt
2 structurally unrelated enzymes with different stereospecificity, MsrA and MsrB, EC 1.8.4.B1, which occur in different variants, but are located on one protein
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; gene msr encodes an enzyme showing both MsrA and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
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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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strains RN450 and BB270, and derivatives, 3 genes msrA1, msrA2, and msrA3 encoding MsrA enzyme forms
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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
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enzyme-deficient mice are more susceptible to kidney ischemia/reperfusion injury than wild type mice. Deletion of the enzyme enhances renal functional and morphological impairments, congestion, inflammatory responses, and oxidative stress under ischemia/reperfusion conditions
metabolism
physiological function
metabolism
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the enzyme participates in regulating methionine metabolism and the trans-sulfuration pathway under normal and ischemia/reperfusion conditions
metabolism
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methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide
physiological function
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MSRA-1 is involved in the aging process in Caenorhabditis elegans, worms carrying a deletion of the msra-1 gene are more sensitive to oxidative stress, show chemotaxis and locomotory defects, and a 30% decrease in median survival
physiological function
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methionine sulfoxide reductase A repairs oxidized methionine residues within proteins and may also function as a general antioxidant, lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span, MsrA knockout mice are more susceptible to oxidative stress induced by paraquat, there is no difference between MsrA knockout and control mice in either their median or maximum life span
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 MsrA is an active player in the protection of the cellular proteins from oxidative stress damage
physiological function
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MsrA knockout mice exhibit altered locomotor activity and brain dopamine levels as function of age, caloric restriction has a neutralization effect on MsrA ablation
physiological function
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overexpression of MsrA does not protect MEF cells from oxidative stress
physiological function
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overexpression of isoform MSR10 in Trypanosoma cruzi confers resistance to oxidative stress, as transfected cells exhibit around 2fold more tolerance to exogenous H2O2
physiological function
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the enzyme protects the kidney against ischemia/reperfusion injury. This protection is associated with reduced oxidative stress and inflammatory responses. The enzyme regulates H2S production during ischemia/reperfusion by modulating the expression and activity of the cystathionine-beta-synthase and cystathionine-gamma-lyase enzymes
physiological function
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overexpression of MSRA4 in Escherichia coli cells enhances resistance to H2O2 toxicity
physiological function
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MSRA-1 is involved in the aging process in Caenorhabditis elegans, worms carrying a deletion of the msra-1 gene are more sensitive to oxidative stress, show chemotaxis and locomotory defects, and a 30% decrease in median survival
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physiological function
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overexpression of isoform MSR10 in Trypanosoma cruzi confers resistance to oxidative stress, as transfected cells exhibit around 2fold more tolerance to exogenous H2O2
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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
alpha-synuclein + dithiothreitol
?
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alpha-synuclein is oxidized at both Met1 and Met5 but not at Met116 or Met127
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-
?
alpha-synuclein + thioredoxin disulfide + H2O
?
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Met1 and Met5 within alpha-synuclein are oxidized to (S)-methionine sulfoxide
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-
?
alpha-synuclein-L-methionine (S)-S-oxide + thioredoxin
alpha-synuclein-L-methionine + thioredoxin disulfide + H2O
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-
?
alpha1-antitrypsin + thioredoxin disulfide + H2O
?
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Met358 within alpha1-antitrypsin is oxidized to (S)-methionine sulfoxide
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-
?
apolipoprotein A-I + dithiothreitol
?
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the myristoylated enzyme reduces the methionine sulfoxides in apolipoprotein A-I four times faster than nonmyristoylated enzyme
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?
calmodulin + thioredoxin disulfide + H2O
?
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Met77 within calmodulin is oxidized to (S)-methionine sulfoxide
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r
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
calmodulin-L-methionine (S)-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 (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
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?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiohthreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
dabsyl-L-methionine (S)-sulfoxide + NADPH + H+
dabsyl-L-methionine + NADP+ + H2O
synthetic substrate, MsrA is absolutely specific for the S-form, 7fold lower activity with NADPH compared to DTT
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?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(S)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
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-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
DL-methionine (S)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
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enzyme MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
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?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
His6-Ala-Ala-Gln-MetO-Ile + DTT
His6-Ala-Ala-Gln-Met-Ile + DTT disulfide + H2O
-
-
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
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?
L-methionine (R,S)-sulfoxide + glutathione
L-methionine + GSSG + H2O
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-
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?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
L-methionine (S)-sulfoxide + dithiothreitol
?
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the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
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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-(S)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
stereospecific reduction, 9-fluorenylmethyl chloroformate-labeled substrate
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
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the membrane-associated isozyme reduces both R- and S-stereoisomer of methionine sulfoxide in proteins
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
N-acetyl-L-methionine (S)-sulfoxide methyl ester + thioredoxin
N-acetyl-L-methionine methyl ester + thioredoxin disulfide + H2O
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enzyme MsrA
-
-
?
N-acetyl-L-methionine-(S)-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 (S)-sulfoxide of the protein substrate
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
MsrA suppresses dopaminergic cell death and protein aggregation induced by the complex I inhibitor rotenone or mutant alpha-synuclein, but not by the proteasome inhibitor MG132. MsrA protects against Parkinson's disease-related stresses primarily via methionine sulfoxide repair rather than by scavenging reactive oxygen species
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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Met sulfoxide residues in Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
-
FMsr is specific for the S-isomer
-
-
?
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
-
MsrA is specific for the S-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-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
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MsrA is specific for the S-form, recombinant human calmodulin, recombinant rat enzyme, artificial system, determination of oxidized methionine residues being reduced by the enzyme, overview
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
synthetic substrate, MsrA is absolutely specific for the S-form
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
synthetic substrate, MsrA is absolutely specific for the S-form
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
FMsr is specific for the S-isomer
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
synthetic substrate
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
-
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
Hsp21 contains 6 methionine residues at positions 49, 52, 55, 59, 62, and 67, about half of the residues are reduced by the enzyme probably due to its stereospecificity
-
-
?
L-methionine (R,S)-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
-
-
-
-
-
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 (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
the MsrA-domain of MsrABTk is strictly specific for the reduction of L-methionine (S)-sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of L-methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, there exist MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-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 (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
oxidation of protein-bound methionine results in loss of protein function, but can be reversed by the enzyme activity reducing methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
absolute specificity for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme MsrA, absolute specificity for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
MsrA activity of the tandem domains of PilB, the MsrA domain alone does very poorly utilize the R-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme MsrA shows absolute specificity for the S-form of free methionine sulfoxide, no activity with the R-form, enzyme MsrA is oxidized at Cys51/Cys198 forming a disulfide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA activity of the tandem domains of PilB, the MsrA domain alone does not utilize the R-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the 2 MsrA enzymes are absolutely specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
L-methionine (S)-sulfoxide is the specific substrate
-
-
?
L-methionine (S)-sulfoxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
-
L-methionine (S)-sulfoxide is the specific substrate
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-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-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, free methionine-(S)-S-oxide
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
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 (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA and soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrate is oxidized ribosomal L12 protein
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrate is oxidized ribosomal L12 protein
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-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
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in oxidized protein repair
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
hormonal regulation of MsrA is implicated in conferring protection against oxidative stress in the Drosophila. Cells that are able to express MsrA were twice as resistant to H2O2 in comparison with cells that are not able to express this gene
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrates are oxidized ribosomal L12 protein or oxidized Met-enkephalin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
protein-bound substrate, stereospecific reduction, substrates are oxidized ribosomal L12 protein or oxidized Met-enkephalin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction, the enzyme is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized A-type potassium channel ShC/B whose activity strongly depends on the oxidative state of a methionine residue in the N-terminal part of the polypeptide
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
the enzyme protects the epidermis cells against irradiation and oxidative damages, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in repair of oxidized proteins by reducing oxidized methionine residues, which is required for resistance to hydrogen peroxide and other reactive oxygen species, and for adherence to host cell surfaces
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
physiological role, overview
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
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 and MsrA
-
-
?
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
-
-
-
-
?
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 enzyme MsrA, low activity by enzyme MsrA1
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, mutation of gene msrA has no effect on virulence, and on resistance to oxidative agents, and causes no defect in cell envelope, msrA is probably linked to biofilm formation, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
the enzyme is not a major virulence determinant in the oral pathogen, MsrA is required for protein repair and protection against oxidative damage as well as for the proper expression or maintenance of functional adhesins
-
-
-
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, MsrA 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
?
-
-
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 protects neuronal cells against brief hypoxia/reoxygenation, the enzyme is involved in oxidized protein repair and protects cells against reactive oxygen species and oxidative damage preventing apoptosis, overview
-
-
-
additional information
?
-
enzyme converts free and protein-bound methionine
-
-
-
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 protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
additional information
?
-
-
MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
-
-
-
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
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
enzyme reduces oxidized methionine residues of the shaker potassium channel, which becomes reversibly inactivated upon oxidation
-
-
-
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 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
?
-
-
MsrA is specific for the S-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, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
-
additional information
?
-
-
substrate specificity of enzyme forms with S-form of free and protein-bound methionine sulfoxide, overview
-
-
-
additional information
?
-
-
substrate specificity of the different enzyme forms, overview, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate, enzyme reduces oxidized methionine residues of the ribosomal protein L12, which becomes reversibly inactivated and forms monomers instead of dimers upon oxidation
-
-
-
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates
-
-
-
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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 contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
additional information
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
-
additional information
?
-
-
the enzyme fulfills both MetO reduction and protein deglutathionylation functions and is also capable of regenerating poplar peroxiredoxin IIB
-
-
-
additional information
?
-
-
the enzyme is unable to reduce insulin disulfides
-
-
-
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 MsrB activity utilizing L-methionine (R)-sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzyme also exhibits MsrB activity utilizing L-methionine (R)-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 MsrA 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, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme is an essential regulator of longevity and is important for lens cell viability and resistance to oxidative stress, methionine sulfoxide is the major oxidative stress product, up to 60%, in cataract while being essentially absent in clear lens
-
-
-
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, MsrA 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
?
-
-
identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
-
-
-
additional information
?
-
-
MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
-
-
-
additional information
?
-
-
MsrA repairs methionine oxidized alpha-crystallin and restores the chaperone activity of alpha-crystallin lost upon methionine oxidation, Met-68 of alphabeta-crystallin is oxidized to protein methionine sulfoxide in the actual lens
-
-
-
additional information
?
-
-
the enzyme catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, MsrA 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
?
-
-
MsrA is a regulator of antioxidant defense and lifespan in mammals
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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
?
-
-
role of subcellular localization in structure-function relationship of the isozymes, overview
-
-
-
additional information
?
-
-
MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking
-
-
-
additional information
?
-
-
MsrA null mutant mice exhibit a shortened lifespan and present higher levels of protein carbonyls when exposed to hyperoxia, which indicates an increased sensitivity towards oxidative stress
-
-
-
additional information
?
-
-
the lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
-
-
-
additional information
?
-
-
MsrA repairs methionine oxidized alpha-crystallin and restores the chaperone activity of alpha-crystallin lost upon methionine oxidation, Met-68 of alphabeta-crystallin is oxidized to protein methionine sulfoxide in the actual lens
-
-
-
additional information
?
-
-
no oxidation or reduction of L-methionine in 14-3-3 zeta/delta protein, actin, alpha-crystallin A, alpha-crystallin B, apolipoprotein A, glutamine synthetase, peroxiredoxin 6, and thioredoxin
-
-
-
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
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
-
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
-
-
-
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
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 posesses MsrB activity utilizing L-methionine (R)-sulfoxide as substrate, the MsrB domain alone does not utilize the S-isomer
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, 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 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 separately on the enzyme molecule, overview
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, 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
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzymes acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
substrate specificities of enzymes, the reduction step is rate-determining
-
-
-
additional information
?
-
-
substrate specificity of MsrA activity, diverse substrates, overview
-
-
-
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive host’s oxidative burst
-
-
-
additional information
?
-
the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
-
-
-
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
?
-
-
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, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA 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
?
-
-
MsrA protects the cell against damage caused by oxidative stress through treatment with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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
-
-
-
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
?
-
-
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, MsrA is important for virulence in mice
-
-
-
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, MsrA 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
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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 is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
additional information
?
-
-
MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60%
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, 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, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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 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
-
-
-
additional information
?
-
the enzyme plays an important role in the oxidative stress response
-
-
-
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-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-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
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
L-methionine (S)-sulfoxide + dithiothreitol
?
-
the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
P54149
MsrA suppresses dopaminergic cell death and protein aggregation induced by the complex I inhibitor rotenone or mutant alpha-synuclein, but not by the proteasome inhibitor MG132. MsrA protects against Parkinson's disease-related stresses primarily via methionine sulfoxide repair rather than by scavenging reactive oxygen species
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
Met sulfoxide residues in Met-rich proteins can be reduced by MsrA and MsrB
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
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
-
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 (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
FMsr is absolutely specific for the S-isomer of free methionine sulfoxide, no activity with protein bound methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
membrane-bound enzyme form Mem-R,S-Msr, enzyme form MsrA is specific for the S-form, MsrA enzyme form variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-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 (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
oxidation of protein-bound methionine results in loss of protein function, but can be reversed by the enzyme activity reducing methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, there exist enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme variants with specificities for either free or protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
G3JX11, P54153
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-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-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Q9AL99
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
P54150, Q9SL43
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-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
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA and MsrB significantly contribute to the protection of Campylobacter jejuni against oxidative and nitrosative stress
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in oxidized protein repair
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
hormonal regulation of MsrA is implicated in conferring protection against oxidative stress in the Drosophila. Cells that are able to express MsrA were twice as resistant to H2O2 in comparison with cells that are not able to express this gene
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction, MsrA is essential for protein repair and protection against oxidative damage
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in regulation of protein function and in elimination of reactive oxygen species via reversible methionine formation besides protein repair in human skin
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Q9UJ68
stereospecific reduction, the enzyme is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate is oxidized A-type potassium channel ShC/B whose activity strongly depends on the oxidative state of a methionine residue in the N-terminal part of the polypeptide
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
the enzyme protects the epidermis cells against irradiation and oxidative damages, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues, the enzyme is involved in repair of oxidized proteins by reducing oxidized methionine residues, which is required for resistance to hydrogen peroxide and other reactive oxygen species, and for adherence to host cell surfaces
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Q8VS50
physiological role, overview
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
P54150
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA and the soluble isozyme MsrA1 are specific for the S-form, the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide, N-acetylmethionine sulfoxide, and D-Ala-Met-enkephalin
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
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
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
-
oxidized Met-enkephalin
-
-
?
additional information
?
-
-
role of the MsrA/MsrB repair pathway in cellular protein dynamics, mutation of gene msrA has no effect on virulence, and on resistance to oxidative agents, and causes no defect in cell envelope, msrA is probably linked to biofilm formation, enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
Q9AL99
the enzyme is not a major virulence determinant in the oral pathogen, MsrA is required for protein repair and protection against oxidative damage as well as for the proper expression or maintenance of functional adhesins
-
-
-
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, MsrA 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
?
-
-
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 protects neuronal cells against brief hypoxia/reoxygenation, the enzyme is involved in oxidized protein repair and protects cells against reactive oxygen species and oxidative damage preventing apoptosis, 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
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
additional information
?
-
-
MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
-
-
-
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
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
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 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, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
-
additional information
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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 contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
additional information
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
-
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 MsrA 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, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
the enzyme is an essential regulator of longevity and is important for lens cell viability and resistance to oxidative stress, methionine sulfoxide is the major oxidative stress product, up to 60%, in cataract while being essentially absent in clear lens
-
-
-
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, MsrA 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
?
-
-
identification of some of the target proteins potentially regulated by or interacting with MsrA. These proteins are implicated in aging, defense against oxidative stress and cell death
-
-
-
additional information
?
-
-
MSRA inhibits development of the locomotor and circadian rhythm defects caused by ectopic expression of human alpha-synuclein in the Drosophila nervous system. One way to enhance the MSRA antioxidant system is dietary supplementation with S-methyl-L-cysteine, found abundantly in garlic, cabbage, and turnips. S-methyl-L-cysteine prevents the alpha-synuclein-induced abnormalities
-
-
-
additional information
?
-
-
the enzyme catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, MsrA 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
?
-
-
MsrA is a regulator of antioxidant defense and lifespan in mammals
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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
?
-
-
MsrA knockout mice have a shorter life span, are more sensitive to hyperbaric oxygen and had a neurological defect that resuls in abnormal walking
-
-
-
additional information
?
-
-
MsrA null mutant mice exhibit a shortened lifespan and present higher levels of protein carbonyls when exposed to hyperoxia, which indicates an increased sensitivity towards oxidative stress
-
-
-
additional information
?
-
-
the lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
-
-
-
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
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
additional information
?
-
-
enzymes 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 host’s 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
?
-
-
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, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA 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
?
-
-
MsrA protects the cell against damage caused by oxidative stress through treatment with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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
-
-
-
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, MsrA is important for virulence in mice
-
-
-
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, MsrA 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
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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 is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
additional information
?
-
-
MsrA can protect cells against oxidative damage. A strain of Streptococcus pneumoniae that is defective in binding to lung cells has a mutation in the MsrA gene. The adherence of the MsrA mutant organism to lung cells is inhibited by about 60%
-
-
-
additional information
?
-
-
the enzyme contributes to the maintenance of adhesins in the pathogen, 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, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA 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
?
-
Q8VS50
the enzyme plays an important role in the oxidative stress response
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
MsrA can also utilize DTT as reductant, the membrane-isozyme shows only poor activity, while MsrA1 is not active with DTT
dithiothreitol
-
absolutely dependent on in vitro and in vivo with substrate Hsp21
thioredoxin
-
; rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin in catalysis
thioredoxin
-
-
thioredoxin
-
cytosolic thioredoxins 1 and 2 are involved in regulation of MsrA exression
thioredoxin
-
-
thioredoxin
-
-
thioredoxin
-
-
394111, 658212, 658213, 658217, 660380, 667434, 668357, 668581, 669752, 695897, 696438, 698124, 726370
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
selenium
additional information
selenium
-
selenoprotein, has a single selenocysteine residue at the catalytic site, the selenocysteine-containing MsrA exhibits at least a 20fold higher activity than its cysteine mutant form U16C, indicating a critical role of selenocysteine in the catalytic activity of the enzyme
additional information
-
the enzyme does not require meal ions for activity, free sulfhydryl content and disulfide bond numbers in wild-type and mutant enzymes, overview
additional information
-
content of free cysteinyl residues in wild-type and mutant enzymes, MsrA and MsrB domains, overview
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethyl sulfoxide
-
DMSO competitively inhibits the methionine-sulfoxide reduction ability of MsrA (12% residual activity at 0.1% (v/v) DMSO) and inhibits the antioxidant function of MsrA in yeast cells, resulting in higher sensitivity to oxidative stress
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
H2O2
-
1 mM, 85% deactivation. The active site of this enzyme is significantly altered after H2O2-mediated oxidation of L-methionine, L-tryptophan, and L-cysteine residues in its active site
H2O2
-
the enzyme is only inactivated by high doses of H2O2, when treated with 0.5 mM H2O2 MsrA loses 20% of its activity and this inhibition reaches approximately 40% with 1 mM H2O2, MsrA is not significantly inhibited by lower concentrations of H2O2 (0.050 and 0.1 mM)
additional information
effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
-
additional information
isozyme PMSRA5 expression is slightly suppressed by ozone
-
additional information
isozyme PMSRA5 expression is slightly suppressed by ozone
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
-
additional information
isozyme PMSRA2 is slightly induced by paraquat, ozone, and high light conditions; isozyme PMSRA3 expression is slightly induced by ozone; isozyme PMSRA4 is highly induced by high light conditions, and slightly by ozone, paraquat, and cercosporin
-
additional information
isozyme PMSRA2 is slightly induced by paraquat, ozone, and high light conditions; isozyme PMSRA3 expression is slightly induced by ozone; isozyme PMSRA4 is highly induced by high light conditions, and slightly by ozone, paraquat, and cercosporin
-
additional information
-
MsrA expression and enzyme formation is induced in the stationary growth phase or on starvation for amino acids, glucose, or nitrogen
-
additional information
-
oxidative stress, e.g. caused by H2O2 up to 0.4 mM, induces enzyme expresssion
-
additional information
-
MsrA is upregulated by UVA radiation in keratinocytes
-
additional information
-
enzyme is induced under oxidative stress and heat shock
-
additional information
-
enzyme expression is induced, together with the glutathione S-transferase, by toxic concentrations of aromatic substrates such as phenol and 4-chlorophenol which cause production of reactive oxygen species
-
additional information
-
MsrA expression is induced by oxidizing diamide treatment and gamma-irradiation, the factor calcium-phosphate-binding protein CPBP, a homologue of elongation factor 1-gamma participates in transcription of gene msrA as part of a transcription regulation complex
-
additional information
-
the calcium phospholipid-binding protein, CPBP, is an analogue of the elongation factor 1-gamma and regulates MsrA expression by binding to the MsrA promoter, starvation induces MsrA expression, also diamide treatment and gamma-irradiation induce the enzyme
-
additional information
-
H2O2 induces MsrA expression in a thioredoxin-dependent manner, msrA promoter and calcium phospholipid binding protein, CPBP, form a complex and enhance msrA expression, cytosolic thioredoxins 1 and 2 are involved in the regulation
-
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
-
oxacillin induces MsrA expression and enzyme formation
-
additional information
-
the msrA1-msrB operon is induced by antibiotics, expression of msrA1 is increased in the stationary phase but not affected by H2O2
-
additional information
-
the antibiotic oxacillin induces MsrA expression
-
additional information
-
chronic dietary intake of soybean protein induces the expression of MsrA
-
additional information
the enzyme shows an oxidant-inducible expression pattern independent of gene oxyR
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.197
Calmodulin
-
myristoylated enzyme, in 20 mM Tris-HCl, pH 7.5, 1 mM CaCl2, at 37°C
1.18
dabsyl L-methionine-(S)-sulfoxide
pH 7.4, 37°C, recombinant enzyme
15
dithiothreitol
-
MsrA domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide
1.1
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
recombinant isozyme PMSRA4, with DTT, pH 8.0, 22°C
2.12
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
recombinant isozyme PMSRA3, with DTT, pH 7.5, 22°C
0.34
dabsyl-L-methionine-(S)-S-oxide
-
recombinant wild-type MsrA, with DTT, pH 7.5, 37°C
4.3
dabsyl-L-methionine-(S)-S-oxide
-
recombinant truncated MsrA DELTA(1-46), with DTT, pH 7.5, 37°C
4
dabsylated L-methionine (S)-sulfoxide
-
purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
10.2
dabsylated L-methionine (S)-sulfoxide
-
wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.044
L-methionine (S)-sulfoxide
-
recombinant wild-type enzyme, pH 7.5, 37°C
0.069
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSRA, at 30°C and pH 7.5
0.12
L-methionine (S)-sulfoxide
-
recombinant wild-type enzyme, pH 7.5, 37°C
0.723
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSR10, at 30°C and pH 7.5
19
L-methionine (S)-sulfoxide
-
MsrA domain of MsrABTk, in the presence of 100 mM dithiothreiol
0.00322
thioredoxin
wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.00343
thioredoxin
mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.0189
thioredoxin
mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.0218
thioredoxin
wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.02265
thioredoxin
mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.0233
thioredoxin
mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.0404
thioredoxin
-
in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37°C
0.013
tryparedoxin I
-
recombinant enzyme. isoform MSRA, at 30°C and pH 7.5
-
0.033
tryparedoxin I
-
recombinant enzyme. isoform MSR10, at 30°C and pH 7.5
-
additional information
additional information
-
detailed kinetics, wild-type and mutants MsrAs; kinetics of disulfide formation in MsrA at Cys52/Cys198 at pH 5.5 and pH 8.0, 25°C, single turnover experiments, steady-state kinetics
-
additional information
additional information
-
steady-state and reductase step kinetic parameters of wild-type and mutated MsrAs
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
dabsyl L-methionine-(S)-sulfoxide
Caenorhabditis elegans
O02089
pH 7.4, 37°C, recombinant enzyme
3.7
L-methionine (S,R)-sulfoxide
Neisseria meningitidis
-
MsrB activity of PILB, pH 8.0, 25°C
0.91
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
Arabidopsis thaliana
P54150, Q9SL43
recombinant isozyme PMSRA3, with DTT, pH 7.5, 22°C
1.59
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
Arabidopsis thaliana
P54150, Q9SL43
recombinant isozyme PMSRA4, with DTT, pH 8.0, 22°C
0.28
dabsyl-L-methionine-(S)-S-oxide
Mus musculus
-
recombinant wild-type MsrA, with DTT, pH 7.5, 37°C
0.78
dabsyl-L-methionine-(S)-S-oxide
Mus musculus
-
recombinant truncated MsrA DELTA(1-46), with DTT, pH 7.5, 37°C
3.8
dabsylated L-methionine (S)-sulfoxide
Clostridium sp.
-
purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
84
dabsylated L-methionine (S)-sulfoxide
Clostridium sp.
-
wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.32
L-methionine (S)-sulfoxide
Trypanosoma sp.
-
recombinant enzyme. isoform MSRA, at 30°C and pH 7.5
0.52
L-methionine (S)-sulfoxide
Trypanosoma sp.
-
recombinant enzyme. isoform MSR10, at 30°C and pH 7.5
0.6
L-methionine (S)-sulfoxide
Neisseria meningitidis
-
pH 5.5, 25°C, MsrA, steady-state conditions
7
L-methionine (S)-sulfoxide
Neisseria meningitidis
-
pH 8.0, 25°C, MsrA, steady-state conditions
0.048
thioredoxin
Nicotiana tabacum
-
in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37°C
0.1
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C; mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.11
thioredoxin
Solanum lycopersicum
G3JX11, P54153
wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.13
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.15
thioredoxin
Solanum lycopersicum
G3JX11, P54153
wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.17
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
0.52
tryparedoxin I
Trypanosoma sp.
-
recombinant enzyme. isoform MSR10, at 30°C and pH 7.5
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0086
L-methionine (S)-sulfoxide
Trypanosoma sp.
-
recombinant enzyme. isoform MSR180, at 30°C and pH 7.5
4384
4.6
L-methionine (S)-sulfoxide
Trypanosoma sp.
-
recombinant enzyme. isoform MSRA, at 30°C and pH 7.5
4384
7.2
L-methionine (S)-sulfoxide
Trypanosoma sp.
-
recombinant enzyme. isoform MSR10, at 30°C and pH 7.5
4384
1.197
thioredoxin
Nicotiana tabacum
-
in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37°C
121
4.3
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
121
4.9
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C
121
5.1
thioredoxin
Solanum lycopersicum
G3JX11, P54153
wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C
121
6.9
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
121
46.5
thioredoxin
Solanum lycopersicum
G3JX11, P54153
wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
121
49.5
thioredoxin
Solanum lycopersicum
G3JX11, P54153
mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C
121
24
tryparedoxin I
Trypanosoma sp.
-
recombinant enzyme. isoform MSRA, at 30°C and pH 7.5
19406
77
tryparedoxin I
Trypanosoma sp.
-
recombinant enzyme. isoform MSR180, at 30°C and pH 7.5
19406
180
tryparedoxin I
Trypanosoma sp.
-
recombinant enzyme. isoform MSR10, at 30°C and pH 7.5
19406
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000015
-
wild-type Saccharomyces cerevisiae strain, substrate L-methionine-(S)-S-oxide
0.00006
-
msrA1/msrA2 double knockout strain RN450; msrA1/msrA2 double knockout strain RN450, substrate L-methionine (S)-sulfoxide
0.000068
-
wild-type Saccharomyces cerevisiae strain, substrate dabsyl-L-methionine-(S)-S-oxide
0.00008
-
msrA1 knockout strain RN450; msrA1 knockout strain RN450, substrate L-methionine (S)-sulfoxide
0.00019
0.0002
-
cytosol, overall Msr activity, substrate is a mixture of S- and R-form of dabsyl L-methionine sulfoxide
0.00021
-
mitochondria, overall Msr activity, substrate is a mixture of S- and R-form of dabsyl L-methionine sulfoxide
0.00024
-
msrA2 knockout strain RN450; msrA2 knockout strain RN450, substrate L-methionine (S)-sulfoxide
0.00026
-
wild-type strain RN450; wild-type strain RN450, substrate L-methionine (S)-sulfoxide
0.0003
-
recombinant Saccharomyces cerevisiae strain overexpressing MsrA, substrate L-methionine-(S)-S-oxide
0.0017
-
recombinant Saccharomyces cerevisiae strain overexpressing MsrA, substrate dabsyl-L-methionine-(S)-S-oxide
0.014
-
purified cysteine mutant form U16C, using human thioredoxin as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.023
-
purified cysteine mutant form U16C, using thioredoxin from Escherichia coli as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.034
-
purified wild type enzyme, using human thioredoxin as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.063
-
purified recombinant MsrA1, substrate L-methionine (S)-sulfoxide
0.07
-
purified wild type enzyme, using Escherichia coli thioredoxin as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.083
purified recombinant MsrA/MsrB tandem domain, substrate L-methionine (S)-sulfoxide
0.099
-
purified recombinant truncated MsrA DELTA(1-46), substrates DTT and dabsyl-L-methionine-(S)-S-oxide
0.15
purified recombinant MsrA domain alone, substrate L-methionine (S)-sulfoxide
0.238
-
purified recombinant wild-type MsrA, substrates DTT and dabsyl-L-methionine-(S)-S-oxide
0.24
-
purified recombinant MsrA2, substrate L-methionine (S)-sulfoxide
0.464
-
purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
0.96
purified enzyme, substrate dabsyl L-methionine-(S)-sulfoxide with dithiothreitol
4.185
-
purified wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C
4.2
43
-
purified recombinant wild-type enzyme, substrate dabsyl-L-methionine (S)-sulfoxide
additional information
4.2
-
purified recombinant wild-type enzyme, substrate L-methionine (S)-sulfoxide
additional information
relative activity in chloroplasts of wild-type and transgenic plants
additional information
-
virulence on chicory leaves of wild-type and recombinant strains, overview
additional information
-
subcellular distribution of MsrA activity in eye tissue, overview
additional information
-
activities in wild-type and mutant mice in different organs during 2 days, overview
additional information
-
activity in wild-type strain and recombinant Escherichia coli strain
additional information
-
recombinant activity in overexpressing yeast cells
additional information
-
cell survival rates after treatement with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
additional information
-
69% of wild-type strain RB450 MsrA activity belongs to MsrA1, 8% to MsrA2, and 23% to MsrA3
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
42
-
the activity declines sharply after 42°C, falling to the minimum at 57°C (17.6% of maximal activity)
60
-
MsrA domain of MsrABTk, substrate: dabsyl-L-methionine-(S)-S-oxide
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 47
-
the enzyme retains over 77% relative activity between 37 and 47°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
primary keratinocytes, expression level at normal light and UV-light conditions
-
chronic sun exposure of human epidermis and high dose UVA irradiation of cultured human keratinocytes results in a decline of MsrA expression and/or Msr activity
germinated; germinated; germinated, highest expression level of isozyme PMSRA4
; highest expression level of isozyme PMSRA2; highest expression level of isozyme PMSRA5
-
overexpression of MsrA in human T-lymphocyte cells protects them against oxidative stress
-
splice variant msrA2a. Multiple MSRA variants participate in the repair of oxidized proteins in vascular smooth muscle cells mitochondria
additional information
-
a knockout mouse strain of the methionine sulfoxide reductase A gene (MsrA-/-) causes an enhanced neurodegeneration in brain hippocampus relative to its wild-type control mouse brain. Deficiency in MsrA activity fosters oxidative-stress that is manifested by the accumulation of faulty proteins (via methionine oxidation), deposition of aggregated proteins, and premature brain cell death
-
MsrA-/- mice have compromised complex task learning capabilities relative to wild-type mice. MsrA-/- mice exhibit lower locomotor activity and altered gait that exacerbate with age. MsrA-/- mice are less responsive to amphetamine treatment. Relative to wild-type mice, MsrA-/- brains contain significantly higher levels of dopamine up to 12 months of age, while lower levels of dopamine are observed at 16 months of age. Striatal regions of MsrA-/- mice show an increase of dopamine release parallel to observed dopamine levels. It is suggested that dopamine regulation and signaling pathways are impaired in MsrA-/- mice, which may contribute to their abnormal behavior
-
chronic sun exposure of human epidermis and high dose UVA irradiation of cultured human keratinocytes results in a decline of MsrA expression and/or Msr activity
-
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
-
overexpression of MsrA protects immortalized WI-38 SV40 human fibroblasts against H2O2–mediated oxidative stress by reducing the amount of intracellular reactive oxygen species and the extent of irreversible protein oxidative damage
-
the msra-1 gene is expressed in most tissues, particularly in the intestine
-
the msra-1 gene is expressed in most tissues, particularly in the intestine
-
-
the msra-1 gene is expressed in most tissues, particularly in the nervous system
-
the msra-1 gene is expressed in most tissues, particularly in the nervous system
-
-
up-regulation of the protein in response to UV irradiation and hydrogen peroxide, suggesting a role of MsrA in photoprotection in epidermis
-
MsrA exhibits a strong expression in keratinocytes and melanocytes and a lower expression in dermal fibroblasts. Repetitive exposure of human skin to solar-stimulated light results in an enhanced expression of MsrA in the epidermis. Exposure to relatively high doses of UVA results in a downregulation of MsrA. 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
additional information
-
high expression level of the plastidic isozyme pPMSR in photosynthetic active tissue
additional information
quantitative expression profile analysis; quantitative expression profile analysis
additional information
quantitative expression profile analysis; quantitative expression profile analysis
additional information
-
enzyme expression level and methionine sulfoxide content in fibroblasts during development, overview
additional information
-
tissue expression analysis of MsrA, wide tissue distribution, no expression in leukemia and lymphoma cell lines
additional information
-
presence o 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 and MsrB, methionine S-oxide reductase (R-form oxidizing), fused together
-
additional information
subcellular localization analysis, overview
-
MsrA contains a mitochondrial targeting sequence which is not necessary for catalytic activity
additional information
subcellular localization of isozymes, overview; subcellular localization of isozymes, overview
-
additional information
subcellular localization of isozymes, overview; subcellular localization of isozymes, overview
-
additional information
-
subcellular sulindac reducing activity distribution in calf liver
-
additional information
subcellular localization is regulated by alternative splicing, overview
-
additional information
-
subcellular localization analysis, the subcellular localization is not tissue-dependent
-
additional information
-
subcellular localization is regulated by alternative splicing, overview; subcellular localization is regulated by alternative splicing, overview
-
additional information
subcellular localization is regulated by alternative splicing, overview; subcellular localization is regulated by alternative splicing, overview
-
additional information
-
subcellular distribution of isozymes MsrA1-3 expression in eye tissue, overview, no localization in endosomes, lysosomes, endoplasmic reticulum, and Golgi apparatus
-
additional information
-
post-translationally occuring subcellular targeting and distribution of isozymes, overview, several forms are generated from a single translation form
-
additional information
subcellular localization is regulated by alternative splicing, overview
-
additional information
-
subcellular distribution of the enzyme in cells grown on 4-chlorophenol
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
25000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
amino acid sequence comparison, structure analysis, active enzyme possesses no N-terminal coil before the core
additional information
-
the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity
additional information
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
-
residual dipolar coupling determination and analysis, comparison with the crystal structure, protein fold and tertiary structure determination
additional information
-
the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity
additional information
-
amino acid sequence comparison, analysis of three-dimensional structures, N-terminal coil, structure comparison to enzymes from other species
additional information
-
residual dipolar coupling determination and analysis, comparison with the crystal structure, protein fold and tertiary structure determination
additional information
-
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
-
the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
enzyme domain and active site structure, MsrA domain comprises residues 181-362, overview
additional information
-
MsrA activity is located on the central domain of PILB, the fused domains are folded entities
additional information
-
MsrA and enzyme MsrB, methionine S-oxide reductase (R-form oxidizing), form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
-
the enzyme forms are produced as individual folded entities, but in vivo the enzyme is part of a three-domain protein named PILB, with the central domain exhibiting MsrA activity, and the C-terminal domain showing MsrB activity
additional information
-
solution structure and dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
enzyme precursor contains a cleavable N-terminal signal sequence for targeting to the mitochondria
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
15-50 mg/ml purified recombinant MsrA in 50 mM Tris-HCl, pH 8.0, 2 mM EDTA, and 10 mM DTT, hanging drop vapour diffusion method, droplet size is 0.004-0.008 ml, equal volumes of protein and precipitant solution, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
single crystals of recombinant N-terminally 10His-tagged enzyme MsrA complexed with protein-bound methionine, hanging drop method, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 1 mM EDTA, 1 mM tris(carboxyethyl)phosphine hydrochloride, precipitant solution contains 2.0 M sodium formate, 0.1 M sodium citrate, pH 6.0, 4°C, 1 week, prior to data collection, crystals are soaked in 6.3 M sodium formate, 0.1 M sodium citrate, pH 6.0, for 2 min, and are flash-cooled, X-ray diffraction structure determination and analysis at 1.5 A resolution, polycrystalline clusters are obtained by sitting drop vapor diffusion method
-
crystals are obtained using the microbatch-under-oil method, four structures of the MsrA domain of the PilB protein from Neisseria meningitidis, representative of four catalytic intermediates of the MsrA catalytic cycle, are determined by X-ray crystallography
-
three-dimensional structure of MsrA in complex with AcMetSONHMe obtained by X-ray crystallography
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
-
half-life of MsrABTk is 30 min. Half-life of the MsrA domain within the MsrABTk protein is 27 min. The recombinant MsrA protein shows a half-life of less than 1 min. The MsrA domain is stabilized through its physical interaction with the more thermostable MsrB domain
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM Tris-HCl pH 7.5, 1 mM EDTA, and 4% (v/v) glycerol, at least 12 months, the purified recombinant enzyme remains stable
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography, phenyl Sepharose column chromatography, and ACA 44 gel filtration
-
native enzyme by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration
-
purification of chloroplasts from wild-type and transgenic plants
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion
recombinant His-tagged isozyme PMSRA3 from Escherichia coli by nickel affinity chromatography; recombinant His-tagged isozyme PMSRA4 from Escherichia coli by nickel affinity chromatography
recombinant His-tagged MsrA from Escherichia coli strain BL21(DE3) by nickel affinity and ion exchange chromatography, 425fold
recombinant His-tagged MsrA1, and MsrA2 from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and DELTA(1-22) deletion mutant from Escherichia coli strain M15 by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
-
recombinant His10-tagged MsrA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His6-tagged MsrA from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
-
recombinant N-terminally 10His-tagged enzyme MsrA from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography
-
recombinant N-terminally His-tagged wild-type and mutant MsrAs from Escherichia coli by nickel affinity chromatography and dialysis
-
recombinant plastidic isozyme pPMSR from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant MsrAs from Escherichia coli strain BE002
-
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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
-
; gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, functional overexpression of MsrB from gene msrB or yeaA
-
; gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, overexpression of MsrA leads to increased resistance to reactive oxygen species
-
complementation of the msrA1/msrA2 double mutant with the msr1 construct, promotor exchange between msrA1 and msrA2
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; 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 GFP-tagged wild-type MsrA and several GFP-tagged deletion mutants in several mammalian cell lines, overview, expression of His-tagged wild-type and DELTA(1-22) deletion mutant in Escherichia coli strain M15
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
expression of the plastidic isozyme pPMSR in Escherichia coli strain BL21(DE3) without the chloroplast signal sequence
-
expression of wild-type and mutant MsrAs in Escherichia coli strain BE002
-
functional overexpression of EGFP-tagged MSRA in PC-12 cells using adenovirus-mediated gene transfer protecting the cells against apoptosis caused by hyperoxia, overview
-
gene bmsrA, expression of GFP-tagged enzyme in syncytial blastoderm-stage embryos of Drosophila melanogaster
-
gene msrA, DNA and amino acid sequence determination and analysis
gene msrA, DNA and amino acid sequence determination and analysis, determination of expression pattern
gene msrA, DNA and amino acid sequence determination and analysis, expression analysis, co-expression of A-type potassium channel ShC/B and MsrA in Xenopus laevis oocytes significantly accelerating the inactivation of the channel protein, functional expression of MsrA as GST-fusion protein in Escherichia coli strain BL21
-
gene msrA, DNA and amino acid sequence determination and analysis, expression in an msrA-deficient Escherichia coli mutant strain Tn903::msrA conferring resistance against oxidative damage from reactive nitrogen intermediates
-
gene msrA, DNA and amino acid sequence determination and analysis, expression of His6-tagged MsrA in Escherichia coli strain BL21
-
gene msrA, expression in an msrA-deficient Escherichia coli mutant strain Tn903::msrA conferring resistance against oxidative damage from reactive nitrogen intermediates
-
gene msrA, expression in Escherichia coli strain BL21(DE3) as His-tagged enzyme
-
gene msrA, expression in Escherichia coli strain BL21(DE3) as N-terminally His-tagged enzyme, the HIs-tag does not influence enzyme activity
gene msrA, genetic structure, DNA and amino acid sequence determination and analysis, expression of isozymes MsrA1-3 in ARPE cells in the cytosol and in mitochondria
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gene msrA, located in the chromosome at 95.69 min, respectively, recombinant expression of msrA, regulation mechanism of gene expression, overview
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gene msrA, msrA promoter and calcium phopsholipid binding protein, CPBP, form a complex and enhance msrA expression in absence of presence of H2O2, cytosolic thioredoxins 1 and 2 are involved in the regulation, overview
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gene msrA, subcloning in Escherichia coli, stable functional overexpression of MsrA in Saccharomyces cerevisiae and human T cells
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genes msrA and msrB, methionine S-oxide reductase (R-form oxidizing), are translationally fused
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genomic structure, alternative splicing variants, overview, expression of GFP-tagged and/or His-tagged mitochondrial and cytosolic MsrAs in CV-1 cells
genomic structure, alternative splicing variants, overview; genomic structure, alternative splicing variants, overview
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
locus At2g18030, isozyme PMSRA5, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression in Escherichia coli strain BL21(DE3), prediction of cis-elements in the promoter, overview; locus At4g25130, isozyme PMSRA4, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His-tagged isozyme PMSRA4 in Escherichia coli, prediction of cis-elements in the promoter, overview; locus At5g07460, isozyme PMSRA2, DNA and amino acid sequence determination and analysis, phylogenetic tree, prediction of cis-elements in the promoter, overview; locus At5g07470, isozyme PMSRA3, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of His-tagged isozyme PMSRA3 in Escherichia coli, prediction of cis-elements in the promoter, overview; locus At5g61640, isozyme PMSRA1, DNA and amino acid sequence determination and analysis, phylogenetic tree, prediction of cis-elements in the promoter, overview
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
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mrsA1, and msrA2 are transcribed as polycistronic transcript, overexpression of MsrA1, and MsrA2 as His-tagged proteins in Escherichia coliBL21(DE3)
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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
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msrA, DNA and amino acid sequence determination and analysis, expression of C-terminally His-tagged or GFP-tagged wild-type or truncated MsrA in Escherichia coli strain BL21(DE3), expression of MsrA isozymes in Saccharomyces cerevisiae, subcellular localization of the recombinant enzymes in cytosol and mitochondria, overview
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overexpression of bovine MsrA in Drosophila extends lifespan by 70%, as well as increased resistance to paraquat-induced oxidative stress
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overexpression of His10-tagged MsrA in Escherichia coli strain BL21(DE3)
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overexpression of msrA gene in HLE cells protects against oxidative stress, while silencing of the gene by short interfering RNA-targeted gene silencing method renders the lens epithelial cells more sensitive to oxidative stress damage
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overexpression of MsrA in a yeast strain, expression of MsrA as N-terminally 6His-tagged protein in Escherichia coli strain BL-21
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overexpression of MsrA in T-lymphocytes and PC12 cells leads to increased resistance of the cells to reactive oxygen species and apoptotic death
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overexpression of MsrA leads to increased resistance to reactive oxygen species
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overexpression of N-terminally 10His-tagged enzyme MsrA in Escherichia coli strain Bl21(DE3)
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overexpression of N-terminally His-tagged wild-type and mutant MsrAs in Escherichia coli
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overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli
the chromosome contains 2 copies of gene msrA, a plasmid harbors 1 copy of gene msrA
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is declined gradually when the plants are exposed to high salt, H2O2 and absisic acid conditions and decrease to lower level at 12 h
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msra-1 mRNA is increased by 2fold in daf-2 mutants compared to wild type controls when worms are cultured at 23 and 25°C, there is a notorious increase in MSRA-1 activity in daf-2 mutants as the worms age, at 23°C MSRA-1 expression is dramatically enhanced in the nervous system
serum anti-MSRA levels are significantly elevated in systemic sclerosis patients with pulmonary fibrosis, cardiac involvement, or decreased total antioxidant power compared with those without them
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the expression is slightly up-regulated in a time-dependent manner after treatment with low temperature and drought within 12 h
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the transcript level of isoform MSRA2 is significantly accumulated in both leaves and green fruits after ethephon treatment
the upstream (promoter 1) regulates the msrA1 transcript that codes for the mitochondrial form of MSRA, the downstream promoter (promoter 2) regulates the msrA2/3 transcripts that code for the cytosolic/nuclear forms of MSRA and is generally less active, both promoters are partially regulated by all-trans retinoic acid
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msra-1 mRNA is increased by 2fold in daf-2 mutants compared to wild type controls when worms are cultured at 23 and 25°C, there is a notorious increase in MSRA-1 activity in daf-2 mutants as the worms age, at 23°C MSRA-1 expression is dramatically enhanced in the nervous system
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msra-1 mRNA is increased by 2fold in daf-2 mutants compared to wild type controls when worms are cultured at 23 and 25°C, there is a notorious increase in MSRA-1 activity in daf-2 mutants as the worms age, at 23°C MSRA-1 expression is dramatically enhanced in the nervous system
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C151A
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site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
C107S
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site-directed mutagenesis, the mutant shows 14% increased activity with DTT and 4% with thioredoxin compared to the wild-type enzyme
C107S/C218S
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site-directed mutagenesis, the mutant shows 78% reduced activity with DTT and 94% with thioredoxin compared to the wild-type enzyme
C107S/C218S/C227S
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site-directed mutagenesis, the mutant shows 61% reduced activity with DTT and 92% with thioredoxin compared to the wild-type enzyme
C107S/C227S
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site-directed mutagenesis, the mutant shows 4% reduced activity with DTT and 86% with thioredoxin compared to the wild-type enzyme
C218S
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site-directed mutagenesis, the mutant shows 65% reduced activity with DTT and 78% with thioredoxin compared to the wild-type enzyme
C218S/C227S
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site-directed mutagenesis, the mutant shows 58% reduced activity with DTT and 96% with thioredoxin compared to the wild-type enzyme
C227S
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site-directed mutagenesis, the mutant shows 11% reduced activity with DTT and 81% with thioredoxin compared to the wild-type enzyme
C72S
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site-directed mutagenesis, inactive mutant, no disulfide bond in the mutant enzyme
C198S
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MsrA mutant, mutation of one recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, probably due to formation of a nonproductive complex between sulfenic intermediate and thioredoxin
C52S
C198S
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site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme; site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
C206S
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site-directed mutagenesis, MsrA domain of PILB, inactive mutant
C348S
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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
W35F
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site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme
W53F
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site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
G24A
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site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme
G28A
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site-directed mutagenesis, 81% reduced activity compared to the wild-type enzyme
C180S
the mutant of isoform E4 shows wild type activity; the mutant of isoform MSRA2 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C188S
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C194S
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
additional information
C52S
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site-directed mutagenesis, reduced activity compared to the wild-type, no complementation of a msrA knockout mutant
C52S
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site-directed mutagenesis, inactive mutant, no protection of the cell against reactive oxygen species
additional information
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mutation of gene msrA has no effect on virulence, and on resistance to oxidative agents, and causes no defect in cell envelope, msrA is probably linked to biofilm formation
additional information
msrA gene inactivation by chromosomal insertion via allele replacement mutagenesis does not lead to increased sensitivity against oxidative stress but to complete loss of enzymatic activity with synthetic substrates
additional information
construction of several transgenic plant lines with altered expression level of the plastidic isozyme PMSR4 of 40-600% compared to wild-type expression level, which results in no phenotype under optimal growing conditions, but at oxidative stress conditions differences in the photosynthesis rate, and the rate of oxidized methionine residues in the chloroplast occur, overexpressing plants are more resistant to oxidative stress, while antisense plants show increased sensitivity, expression analysis
additional information
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free sulfhydryl content and disulfide bond numbers in wild-type and mutant enzymes, overview
additional information
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expression of GFP-tagged MsrA in syncytial blastoderm-stage embryos of Drosophila melanogaster leads to a phenotype with extended lifespan of the mutant fruit flies, resistance to paraquat-induced oxidative stress, and to deleyed senescence-induced decline in general activity and reproductive capacity, overview
additional information
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the cysteine mutant form U16C exhibits at least a 20fold lower activity than the selenocysteine-containing wild type MsrA enzyme
additional information
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the cysteine mutant form U16C exhibits at least a 20fold lower activity than the selenocysteine-containing wild type MsrA enzyme
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additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows defective interaction with plant host cells
additional information
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construction of several mutants with reduced virulence via transposon mutagenesis involving mutation of msrA, mutation of msrA leads o increased sensitivity to oxidative agents, non-motility, and reduced spreading-out and life-span of the pathogen in plants
additional information
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transgenic flies overexpressing MsrA show increased extended life span, with extended time of physical and sexual activity, and increased resistance to paraquat
additional information
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overexpression of MsrA leads to extended life span of the flies up to 70%, the resistance against paraquat-induced oxidative stress is increased
additional information
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mutants defective in the pilA-pilB locus show affected ligand binding and impaired hemagglutination, the mutants' ability to bind eukaryotic receptors is altered, overview
additional information
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construction of knockout mutants which show higher sensitivity to hydrogen peroxide compared to wild-type cells which can be compensated by complementation with the wild-type msrA gene from either Escherichia coli or Mycobacterium tuberculosis, but a mutant C52S msrA gene cannot restore activity in the knockout mutant strain, mutants show reduced type 1 fimbriae-mediated mannose-dependent agglutination of erythrocytes
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells, 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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mutation of msrA results in reduced development of mature biofilm
additional information
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mutation of the 2 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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bacterial cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(R)-S-oxide accumulation
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
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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generation of MsrA-deficient mutant mice, the mutant mice show tip-toe-walking, reduced lifespan under hyperoxic conditions and increased sensitivity to oxidative stress compared to wild-type mice, phenotype overview
additional information
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knockout mutants show shortened life span and have neurological lesions
additional information
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construction of a MsrA null mutant which exhibits a neurological disorder in the form of ataxia, is more sensitive to oxidative stress, and has by about 40% shorter life span than the wild-type mice at normal oxygen conditions and 10% at hyperoxic conditions
additional information
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msrA gene disruption leads to a shortened life span both under normoxic and hyperoxic conditions, MsrA null mutant mice shows greater sensitivity to hyperoxic conditions compared to wild-type mice, construction of MsrA overexpressing strains, phenotypes, overview
additional information
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construction of a msrA mutant which shows drastically reduced ability to survive in macrophages compared to the wild-type strain, the mutant shows increased sensitivity to cumene hydroperoxide and tert-butyl hydroperoxide, but not to H2O2, paraquat, or sodium nitrite
additional information
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msrA gene disruption leads to loss of pathogenicity of the bacterium due to loss of ability to colonize host cells in humans
additional information
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msrA disruption mutants, constructed by insertion mutagenesis, show highly increased sensitivity to H2O2 and reduced capability to adhere to host cell surfaces for infection, overview
additional information
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a msrA mutant exhibited reduced adherence to erythrocytes as well as increased sensitivity to H2O2 and tert-butyl hydroperoxide killing, the mutant is not able to survive in hamster lungs
additional information
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mutation of pilB affects the adherence of gonococci to epithelial cells, overview
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
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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mutation of pilB affects the adherence of gonococci to epithelial cells, overview
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additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
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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a knockout MsrA mutant strain is sensitive to reactive oxygen species
additional information
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H2O2 shortens the life span of cells in constructed null mutants
additional information
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yeast cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(S)-S-oxide accumulation
additional information
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thioredoxin-deficient yeast strains show increased sensitivity to H2O2
additional information
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overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae, resulting in a strain with 25fold increased activity, and Molt-4 human lymphocyte cells provides them with high resistance to oxidative stress by H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride, the recombinant yeast strain grows better and and shows a higher survival rate compared to the wild-type parent strain
additional information
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thioredoxin-deficient yeast strains show increased sensitivity to H2O2
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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
additional information
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construction of a msrA2 knockout mutant, a msrA1 knockout mutant, and a msrA1/msrA2 double knockout mutant, the msrA2 mutant strain and the msrA1/msrA2 double mutant strain show H2O2 tolerance like the wild-type parent strain, but the double mutant strain complemented by msrA2 is H2O2 susceptible, effects of H2O2 or oxidative stress are related to the promotors, overview
additional information
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bacterial cells lacking MsrA show increased sensitivity to oxidative damage, a shortened lifespan under hyperoxic conditions, and methionine-(R)-S-oxide accumulation
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
additional information
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mutation of msrA affects the adherence of pneumococci to epithelial cells, overview
additional information
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a knockout mutant shows reduced ability to attach to host lung and vein epithelial cells
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and is 60% reduced binding to host lung cells
additional information
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mutation of msrA affects the adherence of pneumococci to epithelial cells, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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enzyme is a target for modification of redox-dependent regulation
medicine
synthesis
medicine
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MSRA gene on chromosome 8p might possess metastasis suppressor activity in hepatocellular carcinoma
medicine
MsrA efficiently reduces oxidized methionine residues in recombinant alpha-synuclein. Enhancing MsrA function may be a reasonable therapeutic strategy in Parkinson's disease
medicine
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interventions focusing on the enzymatic reduction of oxidized methionine catalyzed by MSRA represents a new prevention and therapeutic approach for Parkinson’s disease and potentially for other neurodegenerative diseases involving oxidative stress
synthesis
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enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs
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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