1.8.4.11: peptide-methionine (S)-S-oxide reductase
This is an abbreviated version!
For detailed information about peptide-methionine (S)-S-oxide reductase, go to the full flat file.
Reaction
Synonyms
EC 1.8.4.6, ecdysone-induced protein 28/29 kDa, FMsr, LIC_10545, LIC_12978, linmsra1, linmsra2, LMJF_07_1140, methionine S-oxide reductase (S-form oxidizing), methionine sulfoxide reductase, methionine sulfoxide reductase A, methionine sulfoxide reductases A, methionine sulfoxide-S-reductase, methionine sulphoxide reductase, methionine sulphoxide reductase A, methionine-S-sulfoxide reductase, MetSO-L12 reductase, More, mrsA, MSR, MSR10, MSR180, MsrA, MSRA-1, MsrA/B, MsrA/MsrB, MsrA1, MSRA2, MSRA4, msrAB, MsrABTk, MsrBA, Peptide Met(O) reductase, peptide methionine S-sulfoxide reductase, peptide methionine sulfoxide reductase, peptide methionine sulfoxide reductase A, peptide methionine sulfoxide reductase type A, peptide methionine sulphoxide reductase, peptide-methionine (S)-S-oxide reductase, peptide-methionine sulfoxide reductase, PilA, PilB, PilB protein, PMSR, PMSRA, protein-methionine-S-oxide-reductase, sulindac reductase, TbmsrA, TCDM_14270
ECTree
1.8.4.11 peptide-methionine (S)-S-oxide reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E55A
almost completely inactive, dimerization is hardly detectable
E55A
-
almost completely inactive, dimerization is hardly detectable
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C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
D134E
-
most active among the mutant enzymes tested, less active than wild-type
D134N
-
lowest activity among all mutants tested for ac-L-Lys-L-Asn-l-Met(O)-L-Asp-L-Lys-dinitrophenol
E99Q
-
lowest activity towards all substrates tested except for ac-L-Lys-L-Asn-l-Met(O)-L-Asp-L-Lys-dinitrophenol
C107S
-
site-directed mutagenesis, the mutant shows 14% increased activity with DTT and 4% with thioredoxin compared to the wild-type enzyme
C107S/C218S
-
site-directed mutagenesis, the mutant shows 78% reduced activity with DTT and 94% with thioredoxin compared to the wild-type enzyme
C107S/C218S/C227S
-
site-directed mutagenesis, the mutant shows 61% reduced activity with DTT and 92% with thioredoxin compared to the wild-type enzyme
C107S/C227S
-
site-directed mutagenesis, the mutant shows 4% reduced activity with DTT and 86% with thioredoxin compared to the wild-type enzyme
C218S
-
site-directed mutagenesis, the mutant shows 65% reduced activity with DTT and 78% with thioredoxin compared to the wild-type enzyme
C218S/C227S
-
site-directed mutagenesis, the mutant shows 58% reduced activity with DTT and 96% with thioredoxin compared to the wild-type enzyme
C227S
-
site-directed mutagenesis, the mutant shows 11% reduced activity with DTT and 81% with thioredoxin compared to the wild-type enzyme
C72S
-
site-directed mutagenesis, inactive mutant, no disulfide bond in the mutant enzyme
C198S
-
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
C86S/C206S
KM and kcat value are 19fold higher and 40fold slower compared to wild type, respectively. The Cys198-Cys206 disulfide bond is rather reduced by thioredoxin under steady-state conditions instead of the Cys51-Cys198 disulfide bond
D197A
kcat/Km for dabsyl-L-methionine (S)-sulfoxide is 1.46fold lower than wild-type value
E193A
kcat/Km for dabsyl-L-methionine (S)-sulfoxide is 1.3fold lower than wild-type value
E193A/D197A
kcat/Km for dabsyl-L-methionine (S)-sulfoxide is 1.3fold lower than wild-type value
E339A
kcat/Km for dabsyl-L-methionine (S)-sulfoxide is 1.5fold higher than wild-type value
Y343F
kcat/Km for dabsyl-L-methionine (S)-sulfoxide is 1.25fold lower than wild-type value
V231M
mutation to corresponding residue of mouse enzyme, which is hyperoxidized by H2O2. Mutant is sensitive to hyperoxidation
C18S
exhibits lower enzymatic activity than the wild type enzyme
C25S
exhibits lower enzymatic activity than the wild type enzyme
C18S
Leptospira interrogans Fiocruz L1-130
-
exhibits lower enzymatic activity than the wild type enzyme
-
C25S
Leptospira interrogans Fiocruz L1-130
-
exhibits lower enzymatic activity than the wild type enzyme
-
M229V
mutation to corresponding residue of human enzyme, which is not hyperoxidized by H2O2. Mutant is insensitive to hyperoxidation
C198S
C206S
-
site-directed mutagenesis, MsrA domain of PILB, inactive mutant
C348S
-
site-directed mutagenesis, MsrA domain of PILB, mutant is inactive with thioredoxin, but about 10fold more active than the wild-type enzyme MsrA domain
W35F
-
site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme
W53F
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
G24A
-
site-directed mutagenesis, 60% reduced activity compared to the wild-type enzyme
G28A
-
site-directed mutagenesis, 81% reduced activity compared to the wild-type enzyme
C180S
C188S
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C194S
the mutant of isoform E4 shows strongly reduced catalytic efficiency compared to the wild type enzyme
C285S
kcat value is similar to that of wild-type, while its Km value is slightly higher than that of the wild type
additional information
C52S
-
site-directed mutagenesis, inactive mutant, no protection of the cell against reactive oxygen species
C52S
-
site-directed mutagenesis, reduced activity compared to the wild-type, no complementation of a msrA knockout mutant
C198S
-
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
C198S
-
site-directed mutagenesis, altered kinetics and disulfide bond formation compared to the wild-type enzyme
C180S
the mutant of isoform MSRA2 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
msrA gene inactivation by chromosomal insertion via allele replacement mutagenesis does not lead to increased sensitivity against oxidative stress but to complete loss of enzymatic activity with synthetic substrates
additional information
construction of several transgenic plant lines with altered expression level of the plastidic isozyme PMSR4 of 40-600% compared to wild-type expression level, which results in no phenotype under optimal growing conditions, but at oxidative stress conditions differences in the photosynthesis rate, and the rate of oxidized methionine residues in the chloroplast occur, overexpressing plants are more resistant to oxidative stress, while antisense plants show increased sensitivity, expression analysis
additional information
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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
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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
site-directed mutagenesis confirms that Cys56 is the peroxidatic cysteine that is oxidized to sulfenic acid, while Cys204 and Cys213 are the resolving Cys residues that form an intramolecular disulfide bond
additional information
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site-directed mutagenesis confirms that Cys56 is the peroxidatic cysteine that is oxidized to sulfenic acid, while Cys204 and Cys213 are the resolving Cys residues that form an intramolecular disulfide bond
additional information
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site-directed mutagenesis confirms that Cys56 is the peroxidatic cysteine that is oxidized to sulfenic acid, while Cys204 and Cys213 are the resolving Cys residues that form an intramolecular disulfide bond
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additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows defective interaction with plant host cells
additional information
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construction of several mutants with reduced virulence via transposon mutagenesis involving mutation of msrA, mutation of msrA leads o increased sensitivity to oxidative agents, non-motility, and reduced spreading-out and life-span of the pathogen in plants
additional information
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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
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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 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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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 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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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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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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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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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
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mutation of pilB affects the adherence of gonococci to epithelial cells, overview
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additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species and shows decreased adherence to host cells
additional information
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mutation of the recycling Cys to Ser results in an enzyme forming methionine but without recycling activity, while exchange of the catalytic Cys for Ser causes complete loss of activity
additional information
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a knockout MsrA mutant strain is sensitive to reactive oxygen species
additional information
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H2O2 shortens the life span of cells in constructed null mutants
additional information
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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
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
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mutation of msrA affects the adherence of pneumococci to epithelial cells, overview
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