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

EC NUMBER
COMMENTARY
1.8.4.11
-
RECOMMENDED NAME
GeneOntology No.
peptide-methionine (S)-S-oxide reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
reaction mechanism
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
reaction mechanism
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism and structural features, roles of cysteine residues, active site structure
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism and structural features, roles of cysteine residues, active site structure
P54149
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism and structural features, roles of cysteine residues, active site structure
P14930
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism and structural features, roles of cysteine residues, active site structure
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism involves the formation of a sulfenic acid intermediate
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys52 is involved
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys72, Cys218 and Cys228 are involved
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
catalytic mechanism of MsrA, active site structure, modeling of protein-bound methionine sulfoxide recognition and repair from the crystal structure
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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
-
L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
reaction mechanism, modeling of substrate binding at the active site, Cys72 is involved
P14930
L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin
show the reaction diagram
proposed catalytic mechanism of the reductase step of MsrA
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
show the reaction diagram
-
-
-
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
show the reaction diagram
catalytic mechanism, Cys72 is essential for activity forming disulfide bonds with either Cys218 or Cys227
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin
show the reaction diagram
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
show the reaction diagram
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
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methionine S-oxide reductase (S-form oxidizing)
-
-
-
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains VT1169 and VT1530 derived from the clinical strain SUNY 465
Uniprot
Manually annotated by BRENDA team
5 genes, including 1 plastidic isozyme
-
-
Manually annotated by BRENDA team
ecotype Columbia
SwissProt
Manually annotated by BRENDA team
isozyme PMSRA1; isozyme PMSRA2; isozyme PMSRA3; isozyme PMSRA4
SwissProt
Manually annotated by BRENDA team
isozyme PMSRA5
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
gene bmsrA
-
-
Manually annotated by BRENDA team
recombinant
SwissProt
Manually annotated by BRENDA team
gene msrA
SwissProt
Manually annotated by BRENDA team
Caenorhabditis elegans N2
strain N2
-
-
Manually annotated by BRENDA team
strain NCTC 11168
-
-
Manually annotated by BRENDA team
Campylobacter jejuni NCTC 11168
strain NCTC 11168
-
-
Manually annotated by BRENDA team
strain OhILAs, also known as Alkaliphilus oremlandii
-
-
Manually annotated by BRENDA team
Clostridium sp. OhILAs
strain OhILAs, also known as Alkaliphilus oremlandii
-
-
Manually annotated by BRENDA team
strain E88
-
-
Manually annotated by BRENDA team
gene Eip71CD or Eip28/29; alternative splicing variants, overview
SwissProt
Manually annotated by BRENDA team
Erwinia chrysanthemi
-
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
gene msrA, wild-type strain 3937 or RH7006 or pin14
-
-
Manually annotated by BRENDA team
1 copy gene msrA
-
-
Manually annotated by BRENDA team
; enzyme forms MsrA and Mem-R,S-Msr
-
-
Manually annotated by BRENDA team
enzyme forms MsrA, and other enzyme forms, overview
-
-
Manually annotated by BRENDA team
gene msrA, enzyme is organized in a fusion protein together with MsrB, EC 1.8.4.B1
-
-
Manually annotated by BRENDA team
gene msrA, strain MC1061
-
-
Manually annotated by BRENDA team
strain Z19
-
-
Manually annotated by BRENDA team
strains MC1061 and SK8779
-
-
Manually annotated by BRENDA team
wild-type strain MC1061, isozyme MsrA, a membrane-associated isozyme, and a soluble isozyme MsrA1
-
-
Manually annotated by BRENDA team
Escherichia coli Z19
strain Z19
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
Manually annotated by BRENDA team
strain NRC-1
-
-
Manually annotated by BRENDA team
Halobacterium salinarum NRC-1
strain NRC-1
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
Manually annotated by BRENDA team
strain 26695, enzyme forms MsrA and MsrB are fused together forming a single enzyme termed Msr
-
-
Manually annotated by BRENDA team
strain 26695, enzyme forms MsrA and MsrB are fused together forming a single enzyme termed Msr
-
-
Manually annotated by BRENDA team
alternative splicing variants, overview
-
-
Manually annotated by BRENDA team
female caucasian individuals
-
-
Manually annotated by BRENDA team
isozyme MsrA3; alternative splicing variants, overview
SwissProt
Manually annotated by BRENDA team
gene msrA, isozymes MsrA1-3
-
-
Manually annotated by BRENDA team
strain Fusaro
-
-
Manually annotated by BRENDA team
Methanosarcina barkeri Fusaro
strain Fusaro
-
-
Manually annotated by BRENDA team
strain Go1
-
-
Manually annotated by BRENDA team
alternative splicing variants, overview
SwissProt
Manually annotated by BRENDA team
C57BL76J mice, gene msrA
-
-
Manually annotated by BRENDA team
gene msrA, strains CB3.3, 1254, and H37Rv
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
strain MS11, variant VD300, bifunctional enzyme MsrA/B, gene pilA
-
-
Manually annotated by BRENDA team
strain MS11A derivatives, bifunctional enzyme MsrA/B, gene pilB
-
-
Manually annotated by BRENDA team
strain MS11, variant VD300, bifunctional enzyme MsrA/B, gene pilA
-
-
Manually annotated by BRENDA team
Neisseria gonorrhoeae MS11A
strain MS11A derivatives, bifunctional enzyme MsrA/B, gene pilB
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
Manually annotated by BRENDA team
PilB enzyme has 2 catalytic domains showing MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity, respectively
-
-
Manually annotated by BRENDA team
cultivar Hacana SRI
-
-
Manually annotated by BRENDA team
no activity in Aeropyrum pernix K1
-
-
-
Manually annotated by BRENDA team
no activity in Aquifex aeolicus
-
-
-
Manually annotated by BRENDA team
no activity in Archaeoglobus fulgidus DSM 4304
-
-
-
Manually annotated by BRENDA team
no activity in Bifidobacterium longum
NCC2705
-
-
Manually annotated by BRENDA team
no activity in Bifidobacterium longum NCC2705
NCC2705
-
-
Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
DSM 2661
-
-
Manually annotated by BRENDA team
no activity in Methanopyrus kandleri
strain AV19
-
-
Manually annotated by BRENDA team
no activity in Methanopyrus kandleri AV19
strain AV19
-
-
Manually annotated by BRENDA team
no activity in Nanoarchaeum equitans
Kin4-M
-
-
Manually annotated by BRENDA team
no activity in Nanoarchaeum equitans Kin4-M
Kin4-M
-
-
Manually annotated by BRENDA team
no activity in Pyrobaculum aerophilum
strain IM2
-
-
Manually annotated by BRENDA team
no activity in Pyrobaculum aerophilum IM2
strain IM2
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus abyssi
strain GE5
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus abyssi GE5
strain GE5
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus furiosus
strain DSM 3638
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus horikoshii
strain OT3
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus horikoshii OT3
strain OT3
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus tokodaii
strain 7
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus tokodaii 7
strain 7
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma acidophilum
DSM 1728
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma volcanium
strain GSS1
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma volcanium GSS1
strain GSS1
-
-
Manually annotated by BRENDA team
no activity in Thermotoga maritima
-
-
-
Manually annotated by BRENDA team
strain DSM 9790
-
-
Manually annotated by BRENDA team
2 isozymes of MsrA
-
-
Manually annotated by BRENDA team
strain BY4741, enzyme MsrA
-
-
Manually annotated by BRENDA team
strain BY4743, gene msrA
-
-
Manually annotated by BRENDA team
strain BY4741, enzyme MsrA
-
-
Manually annotated by BRENDA team
strain BY4743, gene msrA
-
-
Manually annotated by BRENDA team
winter rye, cv. Halo
-
-
Manually annotated by BRENDA team
3 copies of gene msrA
-
-
Manually annotated by BRENDA team
cultivar Micro-Tom
UniProt
Manually annotated by BRENDA team
3 copies of gene msrA, encoding MsrA1, MsrA2,and MsrA3
-
-
Manually annotated by BRENDA team
MsrA, which appears in 2 enzyme forms
-
-
Manually annotated by BRENDA team
strains RN450 and BB270, and derivatives, 3 genes msrA1, msrA2, and msrA3 encoding MsrA enzyme forms
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
Manually annotated by BRENDA team
; gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
-
-
Manually annotated by BRENDA team
strain R6x, gene msrA
-
-
Manually annotated by BRENDA team
Streptococcus pneumoniae R6x
strain R6x, gene msrA
-
-
Manually annotated by BRENDA team
Trypanosoma sp. CL-Brener
-
-
-
Manually annotated by BRENDA team
2 isozymes of MsrA
-
-
Manually annotated by BRENDA team
2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
-
-
Manually annotated by BRENDA team
pv. phaseoli, gene msrA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
-
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
metabolism
-
the enzyme participates in regulating methionine metabolism and the trans-sulfuration pathway under normal and ischemia/reperfusion conditions
physiological function
-
both single and double inactivation mutants are viable, but more sensitive to oxidative stress agents as hydrogen peroxide, paraquat, and ultraviolet light. These strains also accumulate more carbonylated proteins when exposed to hydrogen peroxide indicating that MsrA is an active player in the protection of the cellular proteins from oxidative stress damage
physiological function
-
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
-
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
-
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
-
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
-
overexpression of MsrA does not protect MEF cells from oxidative stress
physiological function
-
overexpression of MSRA4 in Escherichia coli cells enhances resistance to H2O2 toxicity
physiological function
-
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
Caenorhabditis elegans N2
-
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
Trypanosoma sp. CL-Brener
-
overexpression of isoform MSR10 in Trypanosoma cruzi confers resistance to oxidative stress, as transfected cells exhibit around 2fold more tolerance to exogenous H2O2
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
show the reaction diagram
-
-
-
-
?
(S)-methyl 4-tolyl sulfoxide + thioredoxin
?
show the reaction diagram
-
FMsr is specific for the S-isomer
-
-
?
acetyl-L-methionine-(S)-S-oxide-NHMe + thioredoxin
?
show the reaction diagram
-
-
-
-
?
alpha-synuclein + dithiothreitol
?
show the reaction diagram
-
alpha-synuclein is oxidized at both Met1 and Met5 but not at Met116 or Met127
-
-
?
alpha-synuclein + thioredoxin disulfide + H2O
?
show the reaction diagram
-
Met1 and Met5 within alpha-synuclein are oxidized to (S)-methionine sulfoxide
-
-
?
alpha-synuclein-L-methionine (S)-S-oxide + thioredoxin
alpha-synuclein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
P54149
-
-
-
?
alpha1-antitrypsin + thioredoxin disulfide + H2O
?
show the reaction diagram
-
Met358 within alpha1-antitrypsin is oxidized to (S)-methionine sulfoxide
-
-
?
apolipoprotein A-I + dithiothreitol
?
show the reaction diagram
-
the myristoylated enzyme reduces the methionine sulfoxides in apolipoprotein A-I four times faster than nonmyristoylated enzyme
-
-
?
calmodulin + thioredoxin disulfide + H2O
?
show the reaction diagram
-
Met77 within calmodulin is oxidized to (S)-methionine sulfoxide
-
-
r
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
show the reaction diagram
-
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, 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
-
-
?
calmodulin-L-methionine (S)-S-oxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrBA is able to completely reduce (i.e., repair) MetSO in the calcium regulatory protein calmodulin. The efficient repair is the coordinate activity of the two catalytic domains in the MsrBA fusion protein, which results in a 1 order of magnitude rate enhancement in comparison to those of the individual MsrA or MsrB enzyme alone
-
-
?
calmodulin-L-methionine (S)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9D6Y7
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiohtreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
G3JX11, P54153
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
O02089
synthetic substrate, MsrA is absolutely specific for the S-form
-
-
?
dabsyl-L-methionine (S)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide
show the reaction diagram
Clostridium sp., Clostridium sp. OhILAs
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + NADPH + H+
dabsyl-L-methionine + NADP+ + H2O
show the reaction diagram
O02089
synthetic substrate, MsrA is absolutely specific for the S-form, 7fold lower activity with NADPH compared to DTT
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
synthetic substrate
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-isomer
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
FMsr is specific for the S-isomer
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
O02089
synthetic substrate, MsrA is absolutely specific for the S-form
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
?
show the reaction diagram
Caenorhabditis elegans, Caenorhabditis elegans N2
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide
show the reaction diagram
Clostridium sp., Clostridium sp. OhILAs
-
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
Q9D6Y7
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
Q9AL99
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + DTT
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine-(S)-S-oxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
dabsyl-L-methionine-(S)-S-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
DL-methionine (S)-sulfoxide + thioredoxin
DL-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme MsrA is specific for the S-form, active on free and protein-bound methionine, the latter is bound more efficiently
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
P54150
-
-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
P54150, Q9SL43
-
-
-
-
Gly-L-Met-Gly + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
His6-Ala-Ala-Gln-MetO-Ile + DTT
His6-Ala-Ala-Gln-Met-Ile + DTT disulfide + H2O
show the reaction diagram
-
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
show the reaction diagram
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21, Hsp21 contains 6 methionine residues at positions 49, 52, 55, 59, 62, and 67, about half of the residues are reduced by the enzyme probably due to its stereospecificity
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the membrane-associated isozyme reduces both R- and S-stereoisomers of methionine sulfoxide in proteins
-
-
?
L-methionine (R,S)-sulfoxide + glutathione
L-methionine + GSSG + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
-
-
-
-
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
the MsrA-domain of MsrABTk is strictly specific for the reduction of L-methionine (S)-sulfoxide
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + dithiothreitol
?
show the reaction diagram
-
the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
G3JX11, P54153
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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, 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
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Drosophila melanogaster, Erwinia chrysanthemi
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
absolute specificity for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
enzyme MsrA, absolute specificity for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
P14930
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
show the reaction diagram
-
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
show the reaction diagram
-
the 2 MsrA enzymes are absolutely specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form of L-methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + tryparedoxin I
L-methionine + tryparedoxin I disulfide + H2O
show the reaction diagram
Trypanosoma sp., Trypanosoma sp. CL-Brener
-
L-methionine (S)-sulfoxide is the specific substrate
-
-
?
L-methionine sulfoxide enkephalin + thioredoxin
L-methionine enkephalin
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
L-methionine-(S)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
show the reaction diagram
P54150, Q9SL43
stereospecific reduction, 9-fluorenylmethyl chloroformate-labeled substrate
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9UJ68
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9D6Y7
stereospecific reduction
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction, free methionine-(S)-S-oxide
-
-
?
N-acetyl-L-methionine (R)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
enzyme MsrA/B shows both MsrA and MsrB activity, free and protein-bound methionine
-
-
?
N-acetyl-L-methionine (R,S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide
show the reaction diagram
-
membrane-bound enzyme form Mem-R,S-Msr
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
N-acetyl-L-methionine (S)-sulfoxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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 methyl ester + thioredoxin
N-acetyl-L-methionine methyl ester + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme MsrA
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + DTT
N-acetyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
N-acetyl-L-methionine-(S)-S-oxide + thioredoxin
N-acetyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
oxidized calmodulin + thioredoxin
partially reduced calmodulin + thioredoxin disulfide
show the reaction diagram
-
enzyme reduces L-methionine (S)-sulfoxide of the protein substrate
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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 + DTT
peptide-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
show the reaction diagram
Q9UJ68
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + DTT
peptide-L-methionine + DTT disulfide + H2O
show the reaction diagram
Escherichia coli, Escherichia coli Z19
-
protein-bound substrate, stereospecific reduction, substrate is oxidized ribosomal L12 protein
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q923M1
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9UJ68
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Erwinia chrysanthemi
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9AL99
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
P08761
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8VS50
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
P54150, Q9SL43
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8VS50
physiological role, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Erwinia chrysanthemi
-
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
show the reaction diagram
-
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
show the reaction diagram
Escherichia coli, Erwinia chrysanthemi
-
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
show the reaction diagram
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
show the reaction diagram
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Erwinia chrysanthemi
-
stereospecific reduction of protein-bound methionine (S)-sulfoxide residues
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
stereospecific reduction, MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Campylobacter jejuni NCTC 11168
-
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
show the reaction diagram
Neisseria gonorrhoeae MS11A
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Streptococcus pneumoniae R6x
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Escherichia coli Z19
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction, protein-bound substrate, stereospecific reduction, substrates are oxidized ribosomal L12 protein or oxidized Met-enkephalin
-
-
?
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
P54150
-
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
MsrA is specific for the S-form, 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
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2, highest activity by enzyme MsrA, low activity by enzyme MsrA1
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT
Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O
show the reaction diagram
Escherichia coli, Escherichia coli Z19
-
oxidized Met-enkephalin
-
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Escherichia coli, Escherichia coli Z19
-
oxidized Met-enkephalin
-
-
?
L-Pro-L-Met-L-Ala-L-Ile-L-Lys-L-Lys + dithiothreitol
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
physiological role
-
-
-
additional information
?
-
-
detoxification enzyme
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, enzyme activity is not age-related
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
-
downregulation of MsrA during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
-
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, MsrA is important for virulence in mice
-
-
-
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
?
-
-
enzymes acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
MsrA is specific for the S-form of the substrate
-
-
-
additional information
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
-
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, 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
?
-
-
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
?
-
-
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 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 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 is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
-
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
-
additional information
?
-
O02089
enzyme converts free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme reduces oxidized methionine residues of the alpha-1-proteinase inhibitor, calmodulin, and thrombomodulin, which become reversibly inactivated upon oxidation
-
-
-
additional information
?
-
-
enzyme reduces oxidized methionine residues of the shaker potassium channel, which becomes reversibly inactivated upon oxidation
-
-
-
additional information
?
-
-
substrate specificities of enzymes, the reduction step is rate-determining
-
-
-
additional information
?
-
-
substrate specificity and activity of MsrB/PilB in comparison to MsrA, overview
-
-
-
additional information
?
-
-
substrate specificity of enzyme forms with S-form of free and protein-bound methionine sulfoxide, overview
-
-
-
additional information
?
-
-
substrate specificity of MsrA activity, diverse substrates, 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 enzyme also exhibits MsrB activity utilizing L-methionine (R)-sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzymes utilize free and protein-bound L-methionine and N-acetyl-L-methionine as substrates
-
-
-
additional information
?
-
-
the reduction step is rate-determining
-
-
-
additional information
?
-
P14930
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
?
-
-
MsrA is a regulator of antioxidant defense and lifespan in mammals
-
-
-
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
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
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
-
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, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, 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
?
-
-
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
?
-
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
?
-
Q8VS50
the enzyme plays an important role in the oxidative stress response
-
-
-
additional information
?
-
-
role of subcellular localization in structure-function relationship of the isozymes, 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
?
-
-
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 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
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
-
-
-
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 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
?
-
-
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 lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
-
-
-
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
-
additional information
?
-
Q9JWM8
the PilB protein of Neisseria meningitidis contains a MsrA domain and a MsrB domain
-
-
-
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
?
-
-
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
?
-
-
the enzyme fulfills both MetO reduction and protein deglutathionylation functions and is also capable of regenerating poplar peroxiredoxin IIB, the enzyme is unable to reduce insulin disulfides
-
-
-
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
?
-
Neisseria gonorrhoeae MS11A
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview, 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 also exhibits MsrB activity utilizing L-methionine (R)-sulfoxide as substrate
-
-
-
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
?
-
Streptococcus pneumoniae R6x
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
calmodulin L-methionine-(S)-sulfoxide + thioredoxin
calmodulin L-methionine + thioredoxin disulfide
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (S)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
show the reaction diagram
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
L-methionine (R,S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide
show the reaction diagram
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
?
L-methionine (S)-sulfoxide + 2 dithiothreitol
L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + dithiothreitol
?
show the reaction diagram
-
the myristoylated enzyme form reduces methionine sulfoxide in protein much faster than the nonmyristoylated form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
G3JX11, P54153
-
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
enzyme is involved in repairing of oxidized methionine residues in proteins
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is specific for the S-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Drosophila melanogaster, Erwinia chrysanthemi
-
MsrA is specific for the S-form, free and protein-bound methionine
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
MsrA is specific for the S-isomer
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrAs are specific for the (S)-form of the substrate
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
substrates are several peptides and proteins, overview
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
the enzyme is specific for the S epimer of methionine sulfoxide
-
-
r
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA specifically reduces the S-form of methionine sulfoxide
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine (S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q9AL99
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
P54150, Q9SL43
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
MsrA is involved in repair of oxidized proteins
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA is involved in the antioxidant defense
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Q8VS50
physiological role, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Erwinia chrysanthemi
-
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
show the reaction diagram
-
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
show the reaction diagram
Escherichia coli, Erwinia chrysanthemi
-
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
show the reaction diagram
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
show the reaction diagram
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
MsrA regulation, overview
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Campylobacter jejuni NCTC 11168
-
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
show the reaction diagram
Neisseria gonorrhoeae MS11A, Streptococcus pneumoniae R6x
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Escherichia coli Z19
-
substrate is oxidized ribosomal L12 protein, stereospecific reduction
-
-
?
protein-L-methionine (S)-S-oxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
ribosomal protein L12-L-methionine (S)-sulfoxide + thioredoxin
ribosomal protein L12-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
-
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide + H2O
show the reaction diagram
-
activation of the antiinflammatory drug with anti-tumorigenic activity, which acts via inhibition of cyclooxygenases 1 and 2
-
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
sulindac + thioredoxin
sulindac sulfide + thioredoxin disulfide
show the reaction diagram
-
activation of a methionine sulfoxide-containing prodrug, activity with membrane-bound enzyme form Mem-R,S-Msr and MsrA
activated drug which inhibits cyclooxygenase 1 and 2 and exhibiting anti-inflammatory activity
-
?
Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin
Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
Escherichia coli, Escherichia coli Z19
-
oxidized Met-enkephalin
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
substrates are HIV-2, which is inactivated by oxidation of its methionine residues M76 and M95, the potassium channel of the brain, the inhibitor IkappaB-alpha, or calmodulin, overview
-
-
?
additional information
?
-
-
physiological role
-
-
-
additional information
?
-
-
detoxification enzyme
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, enzyme activity is not age-related
-
-
-
additional information
?
-
-
cellular system of balancing native proteins and oxidatively damaged proteins by use of protein biosynthesis, protein oxidative modification, protein elimination, and oxidized protein repair involving the enzyme, overview, enzyme protects against oxidative damage of proteins, loss of enzyme activity is age-related
-
-
-
additional information
?
-
-
downregulation of MsrA during replicative senescence of cells leads to accumulation of oxidized proteins and age-related increased oxidative damage
-
-
-
additional information
?
-
-
enzyme acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, e.g. the heat shock protein and chaperone Hsp16.3, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics
-
-
-
additional information
?
-
-
enzyme repairs oxidatively damaged free and protein bound methionine and recycles it from methionine sulfoxide, role of the MsrA/MsrB repair pathway in cellular protein dynamics, MsrA is important for virulence in mice
-
-
-
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
?
-
-
enzymes acts on free and protein-bound methionine
-
-
-
additional information
?
-
-
potential role of the enzyme in cold-acclimation, enzyme may protect the cells from photodamage
-
-
-
additional information
?
-
-
protection of the cells against reactive oxidizing species, biological consequences of methionine oxidation, physiological role, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins, MsrA has several different physiological repair and regulatory functions, overview
-
-
-
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, 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
?
-
-
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
?
-
-
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 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 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 is important in protection of the cell against oxidative damage by oxidation of methionine residues in proteins, biological function
-
-
-
additional information
?
-
-
the enzyme protect cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related misfunctions, the membrane-bound enzyme form Mem-R,S-Msr also utilizes the R-isomer of methionine sulfoxide as substrate
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related and neurological diseases, like Parkinsons or Alzheimers disease
-
-
-
additional information
?
-
-
the enzyme protects cells against oxidative damage and plays a role in age-related diseases
-
-
-
additional information
?
-
-
the MsrA1/MsrB system is physiologically more significant in Staphylococcus aureus than MsrA2
-
-
-
additional information
?
-
-
MsrA is a regulator of antioxidant defense and lifespan in mammals
-
-
-
additional information
?
-
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
MsrA is a virulence determinant for the plant pathogen required for full virulence
-
-
-
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
?
-
-
MsrA protects the bacterium against oxidative damage from reactive nitrogen intermediates
-
-
-
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, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
-
-
-
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, 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
?
-
-
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
?
-
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
?
-
Q8VS50
the enzyme plays an important role in the oxidative stress response
-
-
-
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 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
?
-
-
MsrA can protect cells against oxidative damage. Increased sensitivity to H2O2 of the Escherichia coli MsrA mutant
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
MsrA can protect cells against oxidative damage. MsrA mutants of Erwinia chrysanthemi have a defective interaction with plant cells
-
-
-
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 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
?
-
-
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 lack of the MsrA gene in conjunction with prolonged selenium deficient diet causes decreased antioxidant capability and enhanced protein oxidation
-
-
-
additional information
?
-
-
the secreted form of the PilB protein was proposed to be involved in pathogen survival fighting against the defensive hosts oxidative burst
-
-
-
additional information
?
-
-
the enzyme catalyzes its own autooxidation as well as oxidation of free methionine and methionine residues in peptides and proteins
-
-
-
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
?
-
Neisseria gonorrhoeae MS11A, Streptococcus pneumoniae R6x
-
the enzyme contributes to the maintenance of adhesins in the pathogen, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
utilized in vitro
dithiothreitol
O02089
preferred cofactor in vitro
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
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
-
NADPH
-
membrane-bound enzyme form Mem-R,S-Msr
thioredoxin
-
physiologic cofactor
thioredoxin
-
preferred cofactor
thioredoxin
-
; rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin in catalysis
thioredoxin
-
dependent on
thioredoxin
-
-
thioredoxin
-
-
thioredoxin
-
cytosolic thioredoxins 1 and 2 are involved in regulation of MsrA exression
thioredoxin
Q8VS50
-
thioredoxin
P54150, Q9SL43
;
thioredoxin
Erwinia chrysanthemi
-
-
thioredoxin
-
-
thioredoxin
-
Clostridium MsrA is inefficiently reducible by thioredoxin
thioredoxin
-
-
thioredoxin
G3JX11, P54153
;
thioredoxin
-
-
dithiothreitol
-
-
additional information
-
no activity with DTT as cofactor by membrane-bound enzyme form Mem-R,S-Msr
-
additional information
-
DTT can substitute for thioredoxin in vitro
-
additional information
-
DTT can partially substitute for thioredoxin in vitro, low activity
-
additional information
-
DTT can substitute for thioredoxin in vitro
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
-
enzyme prefers high ionic strength, activation
Na2SO4
-
enzyme prefers high ionic strength, activation
NaCl
-
enzyme prefers high ionic strength, activation
NaF
-
enzyme prefers high ionic strength, activation
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
Mg2+
-
activates
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-carboxy 4-nitrobenzenethiol
-
binds specifically to the sulfenic acid reaction intermediate
dimedone
-
binds specifically to the sulfenic acid reaction intermediate
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
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
P54150
effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
-
additional information
-
enzyme expression decreases during dehardening from 4C to 22C of cold-acclimated plants, effects of light and temperature on enzyme expression and activity, overview
-
additional information
P54150, Q9SL43
isozyme PMSRA5 expression is slightly suppressed by ozone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Na2SO4
-
enzyme prefers high ionic strength, activation
NaCl
-
enzyme prefers high ionic strength, activation
NaF
-
enzyme prefers high ionic strength, activation
KCl
-
enzyme prefers high ionic strength, activation
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
-
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
-
oxacillin induces MsrA expression and enzyme formation
-
additional information
-
gene msrA is induced during biofilm formation
-
additional information
-
enzyme is induced under oxidative stress and heat shock
-
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
-
oxidative stress, e.g. caused by H2O2 up to 0.4 mM, induces enzyme expresssion
-
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
P54150
effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
-
additional information
-
48 h exposure to high light at 22C induces enzyme expression, effects of light and temperature on enzyme expression and activity, overview
-
additional information
-
starvation induces the expression of MsrA
-
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
-
the antibiotic oxacillin induces MsrA expression
-
additional information
-
chronic dietary intake of soybean protein induces the expression of MsrA
-
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
Q8VS50
the enzyme shows an oxidant-inducible expression pattern independent of gene oxyR
-
additional information
-
MsrA is upregulated by UVA radiation in keratinocytes
-
additional information
P54150, Q9SL43
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
P54150, Q9SL43
recombinant isozyme PMSRA4, with DTT, pH 8.0, 22C
2.12
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
P54150, Q9SL43
recombinant isozyme PMSRA3, with DTT, pH 7.5, 22C
0.197
Calmodulin
-
myristoylated enzyme, in 20 mM Tris-HCl, pH 7.5, 1 mM CaCl2, at 37C
1.18
dabsyl L-methionine-(S)-sulfoxide
O02089
pH 7.4, 37C, recombinant enzyme
0.34
dabsyl-L-methionine-(S)-S-oxide
-
recombinant wild-type MsrA, with DTT, pH 7.5, 37C
4.3
dabsyl-L-methionine-(S)-S-oxide
-
recombinant truncated MsrA DELTA(1-46), with DTT, pH 7.5, 37C
4
dabsylated L-methionine (S)-sulfoxide
-
purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
10.2
dabsylated L-methionine (S)-sulfoxide
-
wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
15
dithiothreitol
-
MsrA domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide
9
L-methionine (R,S)-sulfoxide
-
MsrB activity of PILB, pH 8.0, 25C
0.044
L-methionine (S)-sulfoxide
-
recombinant wild-type enzyme, pH 7.5, 37C
0.069
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSRA, at 30C and pH 7.5
0.12
L-methionine (S)-sulfoxide
-
recombinant wild-type enzyme, pH 7.5, 37C
0.723
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSR10, at 30C and pH 7.5
1.9
L-methionine (S)-sulfoxide
-
pH 8.0, 25C, cofactor thioredoxin
0.00322
thioredoxin
G3JX11, P54153
wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.00343
thioredoxin
G3JX11, P54153
mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.01
thioredoxin
-
pH 8.0, 25C, substrate L-methionine (S)-sulfoxide
0.0189
thioredoxin
G3JX11, P54153
mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.0218
thioredoxin
G3JX11, P54153
wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28C
0.02265
thioredoxin
G3JX11, P54153
mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28C
0.0233
thioredoxin
G3JX11, P54153
mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.0404
thioredoxin
-
in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37C
0.075
thioredoxin
-
MsrA activity of PILB, pH 8.0, 25C
0.013
tryparedoxin I
-
recombinant enzyme. isoform MSRA, at 30C and pH 7.5
-
0.033
tryparedoxin I
-
recombinant enzyme. isoform MSR10, at 30C and pH 7.5
-
19
L-methionine (S)-sulfoxide
-
MsrA domain of MsrABTk, in the presence of 100 mM dithiothreiol
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetic mechanism
-
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, 25C, single turnover experiments, steady-state kinetics
-
additional information
additional information
-
steady-state and reductase step kinetic parameters of wild-type and mutated MsrAs
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.91
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
P54150, Q9SL43
recombinant isozyme PMSRA3, with DTT, pH 7.5, 22C
1.59
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
P54150, Q9SL43
recombinant isozyme PMSRA4, with DTT, pH 8.0, 22C
0.06
dabsyl L-methionine-(S)-sulfoxide
O02089
pH 7.4, 37C, recombinant enzyme
0.28
dabsyl-L-methionine-(S)-S-oxide
-
recombinant wild-type MsrA, with DTT, pH 7.5, 37C
0.78
dabsyl-L-methionine-(S)-S-oxide
-
recombinant truncated MsrA DELTA(1-46), with DTT, pH 7.5, 37C
3.8
dabsylated L-methionine (S)-sulfoxide
-
purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
84
dabsylated L-methionine (S)-sulfoxide
-
wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
0.32
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSRA, at 30C and pH 7.5
0.52
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSR10, at 30C and pH 7.5
0.6
L-methionine (S)-sulfoxide
-
pH 5.5, 25C, MsrA, steady-state conditions
3.7
L-methionine (S)-sulfoxide
-
pH 8.0, 25C, cofactor thioredoxin
7
L-methionine (S)-sulfoxide
-
pH 8.0, 25C, MsrA, steady-state conditions
0.048
thioredoxin
-
in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37C
0.1
thioredoxin
G3JX11, P54153
mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28C; mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.11
thioredoxin
G3JX11, P54153
wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28C
0.13
thioredoxin
G3JX11, P54153
mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.15
thioredoxin
G3JX11, P54153
wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.17
thioredoxin
G3JX11, P54153
mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
0.32
tryparedoxin I
-
recombinant enzyme. isoform MSRA, at 30C and pH 7.5
-
0.52
tryparedoxin I
-
recombinant enzyme. isoform MSR10, at 30C and pH 7.5
-
3.7
L-methionine (S,R)-sulfoxide
-
MsrB activity of PILB, pH 8.0, 25C
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0086
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSR180, at 30C and pH 7.5
4384
4.6
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSRA, at 30C and pH 7.5
4384
7.2
L-methionine (S)-sulfoxide
-
recombinant enzyme. isoform MSR10, at 30C and pH 7.5
4384
1.197
thioredoxin
-
in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37C
121
4.3
thioredoxin
G3JX11, P54153
mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
121
4.9
thioredoxin
G3JX11, P54153
mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28C
121
5.1
thioredoxin
G3JX11, P54153
wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28C
121
6.9
thioredoxin
G3JX11, P54153
mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
121
46.5
thioredoxin
G3JX11, P54153
wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
121
49.5
thioredoxin
G3JX11, P54153
mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28C
121
24
tryparedoxin I
-
recombinant enzyme. isoform MSRA, at 30C and pH 7.5
0
77
tryparedoxin I
-
recombinant enzyme. isoform MSR180, at 30C and pH 7.5
0
180
tryparedoxin I
-
recombinant enzyme. isoform MSR10, at 30C and pH 7.5
0
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
0.00009
-
enzyme form Mem-R,S-Msr, substrate sulindac
0.00019
-
enzyme form MsrA
0.00019
-
enzyme form MsrA, substrate sulindac
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
0.0004
-
membrane vesicles, substrate N-acetyl-L-methionine-(R)-sulfoxide
0.00044
-
MsrA, substrate N-acetyl-L-methionine-(S)-sulfoxide
0.00047
-
membrane vesicles, substrate N-acetyl-L-methionine-(S)-sulfoxide
0.0017
-
recombinant Saccharomyces cerevisiae strain overexpressing MsrA, substrate dabsyl-L-methionine-(S)-S-oxide
0.0018
-
wild-type strain, substrate L-methionine (S)-sulfoxide
0.014
-
purified cysteine mutant form U16C, using human thioredoxin as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
0.023
-
purified cysteine mutant form U16C, using thioredoxin from Escherichia coli as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
0.034
-
purified wild type enzyme, using human thioredoxin as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
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 37C
0.083
P14930
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
P14930
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
0.33
-
in vitro, substrate free L-methionine (R)-sulfoxide
0.464
-
purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
0.96
O02089
purified enzyme, substrate dabsyl L-methionine-(S)-sulfoxide with dithiothreitol
3
-
recombinant wild-type MsrA domain, cosubstrate dithiothreitol
4.185
-
purified wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37C
4.2
-
purified recombinant wild-type enzyme, substrate L-methionine (S)-sulfoxide
4.2
-
recombinant wild-type MsrA/MsrB, cosubstrate dithiothreitol
43
-
purified recombinant wild-type enzyme, substrate dabsyl-L-methionine (S)-sulfoxide
170
-
recombinant wild-type MsrA/MsrB, cosubstrate thioredoxin
220
-
recombinant wild-type MsrA domain, cosubstrate thioredoxin
additional information
-
activities in wild-type and mutant mice in different organs during 2 days, overview
additional information
-
-
additional information
-
-
additional information
-
activity in wild-type and recombinant strain
additional information
-
activity in wild-type strain and recombinant Escherichia coli strain
additional information
-
subcellular sulindac reducing activity in calf liver
additional information
-
activity in mutant strains
additional information
-
-
additional information
-
69% of wild-type strain RB450 MsrA activity belongs to MsrA1, 8% to MsrA2, and 23% to MsrA3
additional information
P54150
relative activity in chloroplasts of wild-type and transgenic plants
additional information
-
recombinant activity in overexpressing yeast cells
additional information
-
subcellular distribution of MsrA activity in eye tissue, overview
additional information
-
-
additional information
-
cell survival rates after treatement with H2O2, paraquat, or 2,2'-azobis-(2-amidinopropane) dihydrochloride
additional information
Erwinia chrysanthemi
-
virulence on chicory leaves of wild-type and recombinant strains, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9
P14930
assay at
7 - 7.5
O02089
-
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.4
Erwinia chrysanthemi
-
assay at
7.5 - 8
P54150, Q9SL43
assay at
7.5 - 8
-
optimum pH of the MsrA domain
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.5
P54150, Q9SL43
assay at
7.8
-
assay at
8 - 9
-
activity drops dramatically below pH 8.0 or above pH 9.0
8
-
L-methionine formation
8
P54150
assay at
8
Q9SL43
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
O02089
sharp decrease below pH 6.5 and above pH 8.5
7.5 - 9.5
-
the enzyme shows more than 50% activity between pH 7.5 and 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
P54150, Q9SL43
assay at
25
Erwinia chrysanthemi
-
assay at
37
-
assay at
37
-
assay at
37
O02089
about
37
-
assay at
37
P14930
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
42
-
the activity declines sharply after 42C, falling to the minimum at 57C (17.6% of maximal activity)
60
-
MsrA domain of MsrABTk, substrate: dabsyl-L-methionine-(S)-S-oxide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17 - 57
O02089
activity rapidly decreases below 17C and above 57C
37 - 47
-
the enzyme retains over 77% relative activity between 37 and 47C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high MsrA expression level
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
P54150, Q9SL43
highest expression level of isozyme PMSRA4
Manually annotated by BRENDA team
-
high MsrA expression level
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
expression/activities of MSRA and MSRB are significantly decreased in the epidermis of patients with vitiligo compared to healthy controls
Manually annotated by BRENDA team
Trypanosoma sp. CL-Brener
-
-
-
Manually annotated by BRENDA team
-
cell line WI-38, young and old cells, enzyme expression pattern during cell development, senescent cells show decreased enzyme expression and activity
Manually annotated by BRENDA team
-
overexpression of MsrA protects immortalized WI-38 SV40 human fibroblasts against H2O2mediated oxidative stress by reducing the amount of intracellular reactive oxygen species and the extent of irreversible protein oxidative damage
Manually annotated by BRENDA team
-
mature, after anthesis
Manually annotated by BRENDA team
-
primary keratinocytes, expression level at normal light and UV-light conditions
Manually annotated by BRENDA team
-
ventricle, high MsrA expression level
Manually annotated by BRENDA team
-
high MsrA expression level
Manually annotated by BRENDA team
-
human lens epithelial cell line
Manually annotated by BRENDA team
-
weak expression in the hypodermis
Manually annotated by BRENDA team
Caenorhabditis elegans N2
-
weak expression in the hypodermis
-
Manually annotated by BRENDA team
-
the msra-1 gene is expressed in most tissues, particularly in the intestine
Manually annotated by BRENDA team
Caenorhabditis elegans N2
-
the msra-1 gene is expressed in most tissues, particularly in the intestine
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
Manually annotated by BRENDA team
-
highest sulindac reductase activity
Manually annotated by BRENDA team
-
high MsrA expression level
Manually annotated by BRENDA team
-
MsrA mRNA is highly expressed
Manually annotated by BRENDA team
-
high expression level in cold-hardened plants at 4C
Manually annotated by BRENDA team
-
cortical and nuclear components
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
Manually annotated by BRENDA team
-
high MsrA expression level, especially in fetal liver
Manually annotated by BRENDA team
-
nontransgenic embryonic fibroblasts lack MsrA
Manually annotated by BRENDA team
-
the msra-1 gene is expressed in most tissues, particularly in the nervous system
Manually annotated by BRENDA team
Caenorhabditis elegans N2
-
the msra-1 gene is expressed in most tissues, particularly in the nervous system
-
Manually annotated by BRENDA team
-
occasional expression in neurons
Manually annotated by BRENDA team
Caenorhabditis elegans N2
-
occasional expression in neurons
-
Manually annotated by BRENDA team
P54150, Q9SL43
highest expression level of isozyme PMSRA3
Manually annotated by BRENDA team
P54150, Q9SL43
germinated, highest expression level of isozyme PMSRA4
Manually annotated by BRENDA team
-
accumulation in the upper dermis
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
up-regulation of the protein in response to UV irradiation and hydrogen peroxide, suggesting a role of MsrA in photoprotection in epidermis
Manually annotated by BRENDA team
P54150, Q9SL43
-
Manually annotated by BRENDA team
P54150, Q9SL43
highest expression level of isozyme PMSRA2
Manually annotated by BRENDA team
P54150, Q9SL43
highest expression level of isozyme PMSRA5
Manually annotated by BRENDA team
-
overexpression of MsrA in human T-lymphocyte cells protects them against oxidative stress
Manually annotated by BRENDA team
-
splice variant msrA2a. Multiple MSRA variants participate in the repair of oxidized proteins in vascular smooth muscle cells mitochondria
Manually annotated by BRENDA team
-
embryonic fibroblast, activity during development: downregulation during replicative senescence
Manually annotated by BRENDA team
-
fibroblast, young and old cells, enzyme expression pattern during cell development
Manually annotated by BRENDA team
-
overexpressing methionine sulfoxide reductase A
Manually annotated by BRENDA team
additional information
-
expression pattern analysis
Manually annotated by BRENDA team
additional information
-
enzyme expression level and methionine sulfoxide content in fibroblasts during development, overview
Manually annotated by BRENDA team
additional information
-
high expression level of the plastidic isozyme pPMSR in photosynthetic active tissue
Manually annotated by BRENDA team
additional information
-
organ-specific expression patterns
Manually annotated by BRENDA team
additional information
-
expression analysis of MsrA
Manually annotated by BRENDA team
additional information
-
quantitative expression profile analysis
Manually annotated by BRENDA team
additional information
-
tissue expression analysis of MsrA, wide tissue distribution, no expression in leukemia and lymphoma cell lines
Manually annotated by BRENDA team
additional information
-
presence o MsrABTk is greater in Thermococcus kodakaraensis cells grown at suboptimal temperatures (60 to 70C) and could not be detected at 80 to 90C. The amount of intracellular MsrABTk protein increases with exposure to higher dissolved oxygen levels, but only at suboptimal growth temperatures
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
P54150
plastidial isozyme PMSR4, soluble fraction
Manually annotated by BRENDA team
-
plastidic isozyme pPMSR
Manually annotated by BRENDA team
P54150, Q9SL43
isozyme PMSRA3
Manually annotated by BRENDA team
P54150, Q9SL43
isozyme PMSRA4
Manually annotated by BRENDA team
Trypanosoma sp. CL-Brener
-
-
-
Manually annotated by BRENDA team
-
cytosolic isozyme of MsrA
Manually annotated by BRENDA team
P54150, Q9SL43
cytosolic isozyme PMsrA1
Manually annotated by BRENDA team
Q9UJ68
isozyme MsrA3
Manually annotated by BRENDA team
P54150, Q9SL43
isozyme PMSRA2
Manually annotated by BRENDA team
Q9D6Y7
splicing variant MsrA(S)
Manually annotated by BRENDA team
Q9AL99
subcellular localization analysis, overview
Manually annotated by BRENDA team
-
the myristoylated enzyme form is found in cytosol
Manually annotated by BRENDA team
-
secretion of MsrA and MsrB, methionine S-oxide reductase (R-form oxidizing), fused together
-
Manually annotated by BRENDA team
-
outer cell membrane
Manually annotated by BRENDA team
-
enzyme form Mem-R,S-Msr
Manually annotated by BRENDA team
-
membrane-associated isozyme, MsrA
Manually annotated by BRENDA team
-
calf, sulindac reducing activity
-
Manually annotated by BRENDA team
-
matrix, mitochondrial isozyme of MsrA
Manually annotated by BRENDA team
Q9D6Y7
mitochondrial splicing variant MsrA
Manually annotated by BRENDA team
Q9D6Y7
splicing variant MsrA(S)
Manually annotated by BRENDA team
-
soluble isozyme MsrA1
-
Manually annotated by BRENDA team
-
MsrA contains a mitochondrial targeting sequence which is not necessary for catalytic activity
Manually annotated by BRENDA team
additional information
-
no activity in the cytoplasm
-
Manually annotated by BRENDA team
additional information
-
subcellular distribution of the enzyme in cells grown on 4-chlorophenol
-
Manually annotated by BRENDA team
additional information
-
subcellular sulindac reducing activity distribution in calf liver
-
Manually annotated by BRENDA team
additional information
-
post-translationally occuring subcellular targeting and distribution of isozymes, overview, several forms are generated from a single translation form
-
Manually annotated by BRENDA team
additional information
-
subcellular distribution of isozymes MsrA1-3 expression in eye tissue, overview, no localization in endosomes, lysosomes, endoplasmic reticulum, and Golgi apparatus
-
Manually annotated by BRENDA team
additional information
-
subcellular localization of isozymes, overview
-
Manually annotated by BRENDA team
additional information
-
subcellular localization analysis, the subcellular localization is not tissue-dependent
-
Manually annotated by BRENDA team
additional information
-
subcellular localization is regulated by alternative splicing, overview
-
Manually annotated by BRENDA team
additional information
P08761
subcellular localization is regulated by alternative splicing, overview
-
Manually annotated by BRENDA team
additional information
Q9D6Y7
subcellular localization is regulated by alternative splicing, overview
-
Manually annotated by BRENDA team
additional information
-
no activity in the cytoplasm
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Alkaliphilus oremlandii (strain OhILAs)
Alkaliphilus oremlandii (strain OhILAs)
Alkaliphilus oremlandii (strain OhILAs)
Alkaliphilus oremlandii (strain OhILAs)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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)
Rhizobium meliloti (strain 1021)
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
deduced from amino acid sequence
712074
23000
-
His-tagged enzyme isoform MSRA, SDS-PAGE
712074
24000
-
His-tagged enzyme isoform MSR10, SDS-PAGE
712074
25000
-
SDS-PAGE
712073
30000
-
His-tagged enzyme isoform MSR180, SDS-PAGE
712074
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Erwinia chrysanthemi
-
x * 27000, SDS-PAGE
?
-
x * 22000, SDS-PAGE
?
-
x * 21000, SDS-PAGE
?
-
x * 21898, about, recombinant MsrA domain, mass spectrometry
?
O02089
x * 29700, recombinant MsrA, SDS-PAGE
?
-
x * 43000, Msr, SDS-PAGE
?
-
x * 57000, MsrA/B
?
-
x * 21000-27000, about, recombinant MsrA, SDS-PAGE
?
-
x * 20900, calculated from amino acid sequence
?
-
x * 23649, calculated from amino acid sequence
?
-
x * 43000, Msr, SDS-PAGE
-
heterodimer
-
1 * 23000 + 1 * 16000, SDS-PAGE
homodimer
-
2 * 16000, SDS-PAGE
monomer
-
1 * 20000, deduced from amino acid sequence
monomer
Trypanosoma sp. CL-Brener
-
1 * 20000, deduced from amino acid sequence
-
additional information
-
amino acid sequence comparison
additional information
-
amino acid sequence comparison, analysis of three-dimensional structures, N-terminal coil, structure comparison to enzymes from other species
additional information
P54149
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
P14930
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
-
amino acid sequence comparison, analysis of three-dimensional structures, structure comparison to enzymes from other species
additional information
-
amino acid sequence comparison, structure analysis, active enzyme possesses no N-terminal coil before the core
additional information
P14930
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
-
MsrA and MsrB, EC 1.8.4.12, are fused together
additional information
-
the 2 enzyme activities, MsrA and MsrB, form domains of a single polypeptide together with a third thioredoxin-like domain
additional information
-
the Cys residue within the conserved sequence motif GCFWG at the N-terminus is essential for catalytic activity
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
Escherichia coli, Erwinia chrysanthemi
-
residual dipolar coupling determination and analysis, comparison with the crystal structure, protein fold and tertiary structure determination
additional information
-
solution structure and dynamics of the N-terminal domain from Neisseria meningitidis, in its reduced and oxidized forms
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
myristoylation
proteolytic modification
-
enzyme precursor contains a cleavable N-terminal signal sequence for targeting to the mitochondria
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, 4C, 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
-
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
687392
85
-
75% decrease in activity after 2.5 min, MsrABTk
687392
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of chloroplasts from wild-type and transgenic plants
P54150
recombinant His-tagged isozyme PMSRA3 from Escherichia coli by nickel affinity chromatography; recombinant His-tagged isozyme PMSRA4 from Escherichia coli by nickel affinity chromatography
P54150, Q9SL43
recombinant plastidic isozyme pPMSR from Escherichia coli strain BL21(DE3)
-
-
P54149
partially, cell fragmentation
-
recombinant N-terminally His-tagged wild-type and mutant MsrAs from Escherichia coli by nickel affinity chromatography and dialysis
-
recombinant His-tagged MsrA from Escherichia coli strain BL21(DE3) by nickel affinity and ion exchange chromatography, 425fold
O02089
Talon-metal affinity resin chromatography
-
recombinant His6-tagged MsrA from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
Erwinia chrysanthemi
-
native enzyme by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration
-
partially
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
-
recombinant MsrA
-
recombinant MsrA from strain B834(DE3)
-
DEAE column chromatography, phenyl Sepharose column chromatography, and ACA 44 gel filtration
-
partially by subcellular fractionation
-
recombinant His-tagged wild-type and DELTA(1-22) deletion mutant from Escherichia coli strain M15 by nickel affinity chromatography
-
native enzyme partially from retina by subcellular fractionation
-
Ni-NTA column chromatography
-
recombinant N-terminally 10His-tagged enzyme MsrA from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography
-
recombinant His10-tagged MsrA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged full length tandem enzyme, MsrA, and MsrB domains from Escherichia coli, tags are removed by thrombin digestion
P14930
recombinant wild-type and mutant MsrAs from Escherichia coli strain BE002
-
Ni2+ affinity resin column chromatography
-
MsrA from cytosolic and mitochondrial fractions
-
recombinant MsrA from Escherichia coli strain BL21(DE3)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
-
Talon-metal affinity column chromatography
-
recombinant enzyme from Escherichia coli
-
recombinant His-tagged MsrA1, and MsrA2 from Escherichia coli by nickel affinity chromatography
-
Co2+-IDA-Sepharose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene msrA, DNA and amino acid sequence determination and analysis
Q9AL99
expression of the plastidic isozyme pPMSR in Escherichia coli strain BL21(DE3) without the chloroplast signal sequence
-
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
P54150, Q9SL43
genes msrA and msrB, EC 1.8.4.12, form an operon
-
; gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, overexpression of MsrA leads to increased resistance to reactive oxygen species
-
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
-
overexpression of bovine MsrA in Drosophila extends lifespan by 70%, as well as increased resistance to paraquat-induced oxidative stress
-
overexpression of N-terminally His-tagged wild-type and mutant MsrAs in Escherichia coli
-
gene msrA, expression in Escherichia coli strain BL21(DE3) as N-terminally His-tagged enzyme, the HIs-tag does not influence enzyme activity
O02089
expression His-tagged MsrA in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
genomic structure, alternative splicing variants, overview
P08761
gene msrA, DNA and amino acid sequence determination and analysis, expression of His6-tagged MsrA in Escherichia coli strain BL21
Erwinia chrysanthemi
-
; gene msrA, DNA and amino acid sequence determination and analysis, recombinant expression, functional overexpression of MsrB from gene msrB or yeaA
-
gene msrA
-
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 strain B834(DE3)
-
gene msrA, located in the chromosome at 95.69 min, respectively, recombinant expression of msrA, regulation mechanism of gene expression, overview
-
expressed in Escherichia coli BL21(DE3) cells
-
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
-
Drosophila line overexpresses both human alpha-synuclein and MSRA
-
expression analysis in suncellular fractions of melanocytes, overview
-
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
-
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
-
genomic structure, alternative splicing variants, overview; genomic structure, alternative splicing variants, overview
Q9UJ68
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
-
overexpression of MsrA in T-lymphocytes and PC12 cells leads to increased resistance of the cells to reactive oxygen species and apoptotic death
-
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
-
expressed in Escherichia coli BL21(DE3) cells
-
genomic structure, alternative splicing variants, overview, expression of GFP-tagged and/or His-tagged mitochondrial and cytosolic MsrAs in CV-1 cells
Q9D6Y7
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
-
overexpression of MsrA leads to increased resistance to reactive oxygen species
-
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
-
overexpression of N-terminally 10His-tagged enzyme MsrA in Escherichia coli strain Bl21(DE3)
-
overexpression of His10-tagged MsrA in Escherichia coli strain BL21(DE3)
-
gene msr or pilB, DNA sequence determination and analysis
-
gene pilB, expression in Escherichia coli
-
genes msrA and msrB are translationally fused
-
overexpression of the full length tandem enzyme, the MsrA, and the MsrB domains, all His-tagged, in Escherichia coli
P14930
expression in Escherichia coli
-
expression of wild-type and mutant MsrAs in Escherichia coli strain BE002
-
genes msrA and msrB, methionine S-oxide reductase (R-form oxidizing), are translationally fused
-
overexpression of wild-type and mutant enzymes in Escherichia coli
-
expressed in Escherichia coli strain BL21 (DE3)
-
expressed in Escherichia coli
-
expression of MsrA in Escherichia coli strain BL21(DE3)
-
human MOLT-4 cell line are stably transfected with the pLXSN retroviral expression vector based on the Moloney murine leukemia virus and Moloney murine sarcoma virus to generate a replication-deficient recombinant retrovirus containing the rat MsrA and the human MsrB2 cDNA. The oxidized protein repair enzymes MsrA and MsrB2, when overexpressed in the cells, are able to counteract the zinc-mediated damaging effects
A6NCQ5
mitochondrial and cytosolic isozymes are encoded by a single gene
-
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
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
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
-
gene msrA, subcloning in Escherichia coli, stable functional overexpression of MsrA in Saccharomyces cerevisiae and human T cells
-
overexpression of MsrA in a yeast strain, expression of MsrA as N-terminally 6His-tagged protein in Escherichia coli strain BL-21
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
the chromosome contains 2 copies of gene msrA, a plasmid harbors 1 copy of gene msrA
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expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
G3JX11, P54153
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
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complementation of the msrA1/msrA2 double mutant with the msr1 construct, promotor exchange between msrA1 and msrA2
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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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gene msrA, expression in Escherichia coli as GST-fusion protein
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expression inm Escherichia coli, recombinant proteins corresponding to MsrABTk and the individual domains (MsrATk and MsrBTk) are produced
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expressed in Escherichia coli BL21(DE3) cells
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chromosome 1 contains 1 gene msrA, chromosome 2 contains 1 gene msrA
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gene msrA, DNA and amino acid sequence determination and analysis, determination of expression pattern
Q8VS50
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
msra-1 mRNA is increased by 2fold in daf-2 mutants compared to wild type controls when worms are cultured at 23 and 25C, there is a notorious increase in MSRA-1 activity in daf-2 mutants as the worms age, at 23C 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 25C, there is a notorious increase in MSRA-1 activity in daf-2 mutants as the worms age, at 23C MSRA-1 expression is dramatically enhanced in the nervous system
Caenorhabditis elegans N2
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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 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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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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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
G3JX11, P54153
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
C72S/C107S/C227S
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site-directed mutagenesis, inactuve mutant
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
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site-directed mutagenesis, inactive mutant, no protection of the cell against reactive oxygen species
C198S
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site-directed mutagenesis, altered kinetics compared to the wild-type enzyme, site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme
C206S
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site-directed mutagenesis, MsrA domain of PILB, inactive mutant
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
C25S
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site-directed mutagenesis, inactive mutant
F26A
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site-directed mutagenesis, inactive mutant
F26H
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site-directed mutagenesis, inactive mutant
G24A
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site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme
C180S
G3JX11, P54153
the mutant of isoform E4 shows wild type activity
C180S
G3JX11, P54153
the mutant of isoform MSRA2 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C188S
G3JX11, P54153
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C194S
G3JX11, P54153
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
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
Q9AL99
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
C151A
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site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
additional information
P54150
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
C72S/C218S
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site-directed mutagenesis, inactive mutant
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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free sulfhydryl content and disulfide bond numbers in wild-type and mutant enzymes, 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
Clostridium sp. OhILAs
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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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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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transgenic flies overexpressing MsrA show increased extended life span, with extended time of physical and sexual activity, and increased resistance to paraquat
additional information
Erwinia chrysanthemi
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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
Erwinia chrysanthemi
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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
C52S
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site-directed mutagenesis, reduced activity compared to the wild-type, no complementation of a msrA knockout mutant
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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construction of a MsrA/MsrB double mutant
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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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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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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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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C72A
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active-site mutant
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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knockout mutants show shortened life span and have neurological lesions
additional information
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construction of the truncated MsrA DELTA(1-46) mutant
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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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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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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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 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
additional information
Neisseria gonorrhoeae MS11A
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mutation of pilB affects the adherence of gonococci to epithelial cells, overview
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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
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
G28A
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site-directed mutagenesis, 81% reduced activity compared to the wild-type enzyme
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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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
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
W27A
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site-directed mutagenesis, inactive mutant
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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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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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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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 is 60% reduced binding to host lung cells
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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mutation of msrA affects the adherence of pneumococci to epithelial cells, overview
additional information
Streptococcus pneumoniae R6x
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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
P54149
MsrA efficiently reduces oxidized methionine residues in recombinant alpha-synuclein. Enhancing MsrA function may be a reasonable therapeutic strategy in Parkinson's disease
synthesis
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enzyme can be useful in the development and action of anti-cancer and anti-inflammation drugs
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 Parkinsons disease and potentially for other neurodegenerative diseases involving oxidative stress
medicine
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MSRA gene on chromosome 8p might possess metastasis suppressor activity in hepatocellular carcinoma