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Information on EC 1.8.4.11 - peptide-methionine (S)-S-oxide reductase and Organism(s) Arabidopsis thaliana and UniProt Accession P54150
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1.8.4.11 peptide-methionine (S)-S-oxide reductaseIUBMB Comments
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 . On the free amino acid, it can also reduce D-methionine (S)-S-oxide but more slowly . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.12, peptide-methionine (R)-S-oxide reductase, are found within the same protein whereas, in other species, they are separate proteins [1,4]. The reaction proceeds via a sulfenic-acid intermediate [5,10].
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
methionine sulfoxide reductase a, msra1, msra2, methionine sulfoxide reductases a, msra-1, methionine-s-sulfoxide reductase, peptide methionine sulphoxide reductase, methionine sulphoxide reductase a, peptide methionine sulfoxide reductase a, protein-methionine-s-oxide reductase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methionine S-oxide reductase (S-form oxidizing)
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-
-
-
additional information
additional information
the enzyme belongs to the peptide methionine sulfoxide reductase A, PMSRA, gene family
additional information
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the enzyme belongs to the Msr family of enzymes
additional information
the enzyme belongs to the peptide methionine sulfoxide reductase A, PMSRA, gene family
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].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
L-methionine-(S)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
stereospecific reduction, 9-fluorenylmethyl chloroformate-labeled substrate
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-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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MsrA is specific for the S-form
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-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
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-
-
?
Fmoc-L-methionine (S)-sulfoxide + dithiothreitol
Fmoc-L-methionine + dithiothreitol disulfide + H2O
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-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
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-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
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-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
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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
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-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
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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
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-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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-
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
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stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
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substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
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-
?
additional information
?
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enzyme has regulatory function in the plant cell
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-
?
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
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-
?
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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
protein-L-methionine (S)-sulfoxide + thioredoxin
protein-L-methionine + thioredoxin disulfide + H2O
enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues
-
-
?
Hsp21 L-methionine S-oxide + dithiothreitol
Hsp21 L-methionine + dithiothreitol S-oxide
-
chloroplast-localized small heat shock protein, repair function for heat shock protein Hsp21 by restoring the structure, which is crucial for cellular resistance to oxidative stress, the enzyme can protect the chaperone-like activity of Hsp21
-
-
?
L-methionine (S)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
MsrA is specific for the S-form
-
-
?
L-methionine-(S)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
-
-
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
stereospecific reduction
-
-
?
peptide-L-methionine-(S)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
-
substrate in vivo is e.g. the small heat shock protein Hsp-21 which loses its chaperone-like activity upon methionine oxidation
-
-
?
additional information
?
-
-
enzyme has regulatory function in the plant cell
-
-
?
additional information
?
-
-
recycling of free methionine, enzyme reverses the oxidative damage at methionine protein residues oxidized to methionine sulfoxide being a major cause of aging and age-related diseases, Msr can regulate protein function, be involved in signal transduction, and prevent accumulation of faulty proteins
-
-
?
additional information
?
-
-
roles of methionine sulfoxide reductases in antioxidant defense, protein regulation via alternating it between active and inactive form, and survival, MsrA protects cells from the cytotoxic effects of reactive oxygen species, ROS, overview, the enzyme is involved in age-related diseases such as Alzheimer's or Parkinson's diseases as well as in diseases caused by prions, mechanism, overview, enzyme involvement in protein repair and associated factors, protein regulation pathway, overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
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absolutely dependent on in vitro and in vivo with substrate Hsp21
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
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additional information
isozyme PMSRA5 expression is slightly suppressed by ozone
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additional information
isozyme PMSRA5 expression is slightly suppressed by ozone
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
effects of high light, ozone, and paraquat on enzyme activity and photosynthetic activity in wild-type and transgenic plants, overview
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additional information
isozyme PMSRA2 is slightly induced by paraquat, ozone, and high light conditions
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additional information
isozyme PMSRA2 is slightly induced by paraquat, ozone, and high light conditions
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additional information
isozyme PMSRA3 expression is slightly induced by ozone
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additional information
isozyme PMSRA3 expression is slightly induced by ozone
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additional information
isozyme PMSRA4 is highly induced by high light conditions, and slightly by ozone, paraquat, and cercosporin
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additional information
isozyme PMSRA4 is highly induced by high light conditions, and slightly by ozone, paraquat, and cercosporin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
recombinant isozyme PMSRA4, with DTT, pH 8.0, 22°C
2.12
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
recombinant isozyme PMSRA3, with DTT, pH 7.5, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.91
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
recombinant isozyme PMSRA3, with DTT, pH 7.5, 22°C
1.59
9-fluorenylmethyl chloroformate-labeled L-methionine-(S)-S-oxide
recombinant isozyme PMSRA4, with DTT, pH 8.0, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
relative activity in chloroplasts of wild-type and transgenic plants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
germinated, highest expression level of isozyme PMSRA4
additional information
-
high expression level of the plastidic isozyme pPMSR in photosynthetic active tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
subcellular localization of isozymes, overview
-
additional information
subcellular localization of isozymes, overview
-
additional information
subcellular localization of isozymes, overview
-
additional information
subcellular localization of isozymes, overview
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MSRA4_ARATH
258
0
28644
Swiss-Prot
Chloroplast (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C151A
-
site-directed mutagenesis, activity with Hsp21 is similar to the wild-type enzyme
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of chloroplasts from wild-type and transgenic plants
recombinant His-tagged isozyme PMSRA3 from Escherichia coli by nickel affinity chromatography
recombinant His-tagged isozyme PMSRA4 from Escherichia coli by nickel affinity chromatography
recombinant plastidic isozyme pPMSR from Escherichia coli strain BL21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expression of the plastidic isozyme pPMSR in Escherichia coli strain BL21(DE3) without the chloroplast signal sequence
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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enzyme is a target for modification of redox-dependent regulation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moskovitz, J.
Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
Biochim. Biophys. Acta
1703
213-219
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Staphylococcus aureus, Mus musculus, Sus scrofa
Gustavsson, N.; Kokke, B.P.; Harndahl, U.; Silow, M.; Bechtold, U.; Poghosyan, Z.; Murphy, D.; Boelens, W.C.; Sundby, C.
A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein
Plant J.
29
545-553
2002
Arabidopsis thaliana
Romero, H.M.; Berlett, B.S.; Jensen, P.J.; Pell, E.J.; Tien, M.
Investigations into the role of the plastidial peptide methionine sulfoxide reductase in response to oxidative stress in Arabidopsis
Plant Physiol.
136
3784-3794
2004
Arabidopsis thaliana (P54150)
Moskovitz, J.
Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival
Curr. Pharm. Des.
11
1451-1457
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Staphylococcus aureus, Mus musculus, Sus scrofa
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