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Information on EC 1.8.4.12 - peptide-methionine (R)-S-oxide reductase and Organism(s) Homo sapiens and UniProt Accession Q8IXL7

for references in articles please use BRENDA:EC1.8.4.12
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IUBMB Comments
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide . While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater . The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well . The enzyme from some species contains selenocysteine and Zn2+.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q8IXL7
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Homo sapiens
Synonyms
methionine sulfoxide reductase, msrb1, msrb3, peptide methionine sulfoxide reductase, msrb2, msra/b, cbs-1, methionine-r-sulfoxide reductase, msrab, methionine sulfoxide reductase b1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CBS-1
CBS1
247
-
cysteine-containing methionine-R-sulfoxide reductase
247
-
methionine sulfoxide reductase
methionine sulfoxide reductase B
247
-
methionine sulfoxide reductase B1
284378
-
methionine sulfoxide reductase B2
methionine sulfoxide reductase B3
247
-
methionine sulfoxide reductases B
284367
-
methionine sulfoxide reductases B2
277223
-
MSRB1
284378
-
MsrB2
MsrB3
MsrB3A
247
isoform
peptide methionine sulfoxide reductase
247
-
peptide methionine sulfoxide reductase type B
247
-
Sel-X
247
-
selenocysteine-containing methionine-R-sulfoxide reductase
247
-
selenoprotein R
247
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-methionine (R)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
the active site selenocysteine SeC169 is essential for enzyme activity
-
peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]
The reaction occurs in the reverse direction to that shown above. The enzyme exhibits high specificity for reduction of the R-form of methionine S-oxide, with higher activity being observed with L-methionine S-oxide than with D-methionine S-oxide [9]. While both free and protein-bound methionine (R)-S-oxide act as substrates, the activity with the peptide-bound form is far greater [10]. The enzyme plays a role in preventing oxidative-stress damage caused by reactive oxygen species by reducing the oxidized form of methionine back to methionine and thereby reactivating peptides that had been damaged. In some species, e.g. Neisseria meningitidis, both this enzyme and EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase, are found within the same protein whereas in other species, they are separate proteins [3,5]. The reaction proceeds via a sulfenic-acid intermediate [5,10]. For MsrB2 and MsrB3, thioredoxin is a poor reducing agent but thionein works well [11]. The enzyme from some species contains selenocysteine and Zn2+.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dabsyl L-methionine (R)-sulfoxide + thioredoxin
dabsyl L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
cytosolic human thioredoxin 1, mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptide or Escherichia coli thioredoxin
-
-
?
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
rTrx2 physically interacts with oxidized MsrB2 through a disulfide bond. Thioredoxin- and dithiothreitol-dependent activities are approximately equal
-
-
?
dabsyl-L-methionine-(R)-S-oxide + dithiothreitol
dabsyl-L-methionine + DTT disulfide + H2O
show the reaction diagram
-
-
-
?
(R)-methyl 4-tolyl sulfoxide + thioredoxin
?
show the reaction diagram
-
-
-
-
?
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
dabsyl-L-methionine (R)-sulfoxide + dithiothreitol
dabsyl-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
-
-
-
?
dabsyl-L-methionine (R)-sulfoxide + thioredoxin
dabsyl-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
FMsr is specific for the R-isomer
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
L-methionine-(R)-S-oxide + DTT
L-methionine + DTT disulfide + H2O
show the reaction diagram
-
-
-
-
?
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
-
-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
calmodulin-L-methionine (R)-sulfoxide + thioredoxin
calmodulin-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
MsrB is specific for the R-form, enzyme provides protection against oxidative damage by reactive oxygen species and has a repair function for oxidized protein methionine residues, which restores the calmodulin binding to adenylate cyclase of the pathogen Bordetella pertussis, which is an essential step for the bacterium to enter host cells, overview
-
-
?
L-methionine (R)-sulfoxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
L-methionine-(R)-S-oxide + thioredoxin
L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
peptide-L-methionine-(R)-S-oxide + thioredoxin
peptide-L-methionine + thioredoxin disulfide + H2O
show the reaction diagram
-
upon oxidative stress, the overexpression of methionine sulfoxide reductase B2 leads to the preservation of mitochondrial integrity by decreasing the intracellular reactive oxygen species build-up through its scavenging role, hence contributing to cell survival and protein maintenance
-
-
?
protein L-methionine (R)-sulfoxide + thioredoxin
protein L-methionine + thioredoxin disulfide
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
protein-L-methionine (R)-sulfoxide + dithiothreitol
protein-L-methionine + dithiothreitol disulfide + H2O
show the reaction diagram
-
type B enzyme CBS1 is stereospecific for the R-stereomer of methionine residues of peptides and proteins
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
thioredoxin
additional information
-
thioredoxin independent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
selenium
-
selenocysteine-containing
Zinc
-
zinc-containing enzyme
selenium
-
selenoprotein
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
-
1 mM, 40% deactivation of MSRB1
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
oxidative stress, e.g. caused by H2O2 up to 0.4 mM, induces enzyme expresssion
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
additional information
additional information
-
thioredoxin- and DTT-dependent kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83
L-methionine-(R)-S-oxide
-
recombinant wild-type isozyme MsrB3 expressed in Escherichia coli
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.071
substrate: cytosolic human thioredoxin 1
0.12
substrate: Escherichia coli thioredoxin
0.173
substrate: mitochondrial rat thioredoxin 2 lacking a mitochondrial signal peptid
0.179
substrate: dithiothreitol
0.023
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and thioredoxin
0.092
-
purified recombinant CBS-1, substrate L-methionine (R)-sulfoxide
0.452
-
purified recombinant wild-type isozyme MsrB3 expressed in Escherichia coli, substrates are L-methionine-(R)-S-oxide and DTT
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
assay at
7.4
-
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozyme MsrB1
Manually annotated by BRENDA team
-
isozymes MsrB3 and MsrB2
Manually annotated by BRENDA team
-
epithelia and fibers, isozymes MsrB1 or selenoprotein R, MsrB2 or CBS-1, and MsrB3, differential expression patterns of isozymes, overview
Manually annotated by BRENDA team
-
polymorphonuclear
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
epidermal
Manually annotated by BRENDA team
-
i.e. HLE cell, transformed human lens epithelial cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
MsrB3A contains an endoplasmic reticulum signal peptide at the N-terminus and an endoplasmic reticulum retention signal at the C-terminus, and is targeted to the endoplasmic reticulum
Manually annotated by BRENDA team
additional information
-
subcellular targeting is determined by alternative splicing
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knockdown of MsrB3A in mammalian cells leads to a significant decrease in the resistance to thapsigargin-induced endoplasmic reticulum (ER) stress, but had no effects on the resistance to either dithiothreitol- or tunicamycin-induced ER stress
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
MSRB3_HUMAN
192
0
20702
Swiss-Prot
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C105S
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
C169S
-
site-directed mutagenesis, active site mutant, completely inactive mutant
H77G
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to highly reduced activity with cofactor thioredoxin or DTT compared to wild-type MsrB3
H77G/I81E/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
H77G/N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, inactive mutant
I81E
-
site-directed mutagenesis, mutation of isozyme MsrB3 leads to slightly increased activity with cofactor thioredoxin and reduced activcity with DTT compared to wild-type MsrB3
N97F
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant is inactive with cofactor thioredoxin and shows highly reduced activity with cofactor DTT compared to wild-type MsrB3
N97Y
-
site-directed mutagenesis, mutation of isozyme MsrB3, the mutant shows highly reduced activity with cofactor DTT or thioredoxin compared to wild-type MsrB3
W110A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
additional information
-
substitution of Cys residues abolish the enzyme's activity with thioredoxin and increase the DTT-dependent activity, overview
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partially by subcellular fractionation
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant MsrB from Escherichia coli strain BL21(DE3)
-
recombinant wild-type and mutant isozyme MsrB3 from Escherichia coli strain BL21(DE3)
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
CBS-1, overexpression of the His-tagged enzyme in Escherichia coli
-
expressed in Drosophila melanogaster
-
expressed in Drosophila melanogaster, in A-549 cells and human dermal fibroblasts
-
expression analysis in subcellular fractions of melanocytes, overview
-
expression of MsrB in Escherichia coli strain BL21(DE3)
-
expression of wild-type and mutant isozyme MsrB3 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
-
overexpression of truncated wild-type and mutant enzymes as His-tagged proteins in Escherichia coli, functional coexpression of CBS1 in oocytes with Drosophila melanogaster ShC/B potassium channel
-
transfection of MOLT-4 cell line by human MsrB2
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moskovitz, J.; Poston, J.M.; Berlett, B.S.; Nosworthy, N.J.; Szczepanowski, R.; Stadtman, E.R.
Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
J. Biol. Chem.
275
14167-14172
2000
Homo sapiens
Manually annotated by BRENDA team
Weissbach, H.; Resnick, L.; Brot, N.
Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
Biochim. Biophys. Acta
1703
203-212
2005
Bos taurus, Escherichia coli, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus, Neisseria gonorrhoeae, Neisseria meningitidis, Saccharomyces cerevisiae, Streptococcus gordonii (Q9LAM9), Streptococcus gordonii, Streptococcus pneumoniae
Manually annotated by BRENDA team
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, Escherichia coli, Homo sapiens, Mus musculus, Saccharomyces cerevisiae, Staphylococcus aureus, Sus scrofa
Manually annotated by BRENDA team
Petropoulos, I.; Friguet, B.
Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases
Biochim. Biophys. Acta
1703
261-266
2005
Drosophila melanogaster, Escherichia coli, Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Jung, S.; Hansel, A.; Kasperczyk, H.; Hoshi, T.; Heinemann, S.H.
Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1
FEBS Lett.
527
91-94
2002
Homo sapiens
Manually annotated by BRENDA team
Picot, C.R.; Perichon, M.; Cintrat, J.C.; Friguet, B.; Petropoulos, I.
The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts
FEBS Lett.
558
74-78
2004
Homo sapiens
Manually annotated by BRENDA team
Vougier, S.; Mary, J.; Dautin, N.; Vinh, J.; Friguet, B.; Ladant, D.
Essential role of methionine residues in calmodulin binding to Bordetelle pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases
J. Biol. Chem.
279
30210-30218
2004
Homo sapiens
Manually annotated by BRENDA team
Lowther, W.T.; Weissbach, H.; Etienne, F.; Brot, N.; Matthews, B.W.
The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
Nat. Struct. Biol.
9
348-352
2002
Escherichia coli (P0A746), Homo sapiens (Q9Y3D2), Neisseria gonorrhoeae, Neisseria gonorrhoeae (P14930)
Manually annotated by BRENDA team
Schallreuter, K.U.; Rubsam, K.; Chavan, B.; Zothner, C.; Gillbro, J.M.; Spencer, J.D.; Wood, J.M.
Functioning methionine sulfoxide reductases A and B are present in human epidermal melanocytes in the cytosol and in the nucleus
Biochem. Biophys. Res. Commun.
342
145-152
2006
Homo sapiens
Manually annotated by BRENDA team
Moskovitz, J.
Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival
Curr. Pharm. Des.
11
1451-1457
2005
Arabidopsis thaliana, Homo sapiens, Mus musculus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Marchetti Maria, A.; Pizarro Gresin, O.; Sagher, D.; Deamicis, C.; Brot, N.; Hejtmancik, J.F.; Weissbach, H.; Kantorow, M.
Methionine sulfoxide reductases B1, B2, and B3 are present in the human lens and confer oxidative stress resistance to lens cells
Invest. Ophthalmol. Vis. Sci.
46
2107-2112
2005
Homo sapiens
Manually annotated by BRENDA team
Kim, H.Y.; Gladyshev, V.N.
Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases
PLoS Biol.
3
2080-2089
2005
Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
Sagher, D.; Brunell, D.; Hejtmancik, J.F.; Kantorow, M.; Brot, N.; Weissbach, H.
Thionein can serve as a reducing agent for the methionine sulfoxide reductases
Proc. Natl. Acad. Sci. USA
103
8656-8661
2006
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Cabreiro, F.; Picot, C.R.; Perichon, M.; Friguet, B.; Petropoulos, I.
Overexpression of methionine sulfoxide reductases A and B2 protects MOLT-4 cells against zinc-induced oxidative stress
Antioxid. Redox Signal.
11
215-225
2009
Homo sapiens (Q9Y3D2)
Manually annotated by BRENDA team
Kim, H.Y.; Kim, J.R.
Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine
Biochem. Biophys. Res. Commun.
371
490-494
2008
Homo sapiens (Q8IXL7), Mus musculus (Q78J03)
Manually annotated by BRENDA team
Kim, H.Y.; Gladyshev, V.N.
Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals
Biochem. J.
407
321-329
2007
Bacillus subtilis (P54155), Drosophila melanogaster, Homo sapiens (Q8IXL7), Mus musculus (Q8BU85), Neisseria meningitidis
Manually annotated by BRENDA team
De Luca, A.; Sacchetta, P.; Nieddu, M.; Di Ilio, C.; Favaloro, B.
Important roles of multiple Sp1 binding sites and epigenetic modifications in the regulation of the methionine sulfoxide reductase B1 (MsrB1) promoter
BMC Mol. Biol.
8
39
2007
Homo sapiens, Homo sapiens (Q9NZV6)
Manually annotated by BRENDA team
Picot, C.R.; Moreau, M.; Juan, M.; Noblesse, E.; Nizard, C.; Petropoulos, I.; Friguet, B.
Impairment of methionine sulfoxide reductase during UV irradiation and photoaging
Exp. Gerontol.
42
859-863
2007
Homo sapiens, Homo sapiens (Q8IXL7), Homo sapiens (Q9Y3D2)
Manually annotated by BRENDA team
Cabreiro, F.; Picot, C.R.; Perichon, M.; Castel, J.; Friguet, B.; Petropoulos, I.
Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage
J. Biol. Chem.
283
16673-16681
2008
Homo sapiens (Q9Y3D2)
Manually annotated by BRENDA team
Schallreuter, K.U.; Ruebsam, K.; Gibbons, N.C.; Maitland, D.J.; Chavan, B.; Zothner, C.; Rokos, H.; Wood, J.M.
Methionine sulfoxide reductases A and B are deactivated by hydrogen peroxide (H2O2) in the epidermis of patients with vitiligo
J. Invest. Dermatol.
128
808-815
2008
Homo sapiens, Homo sapiens (Q9NZV6)
Manually annotated by BRENDA team
Binger, K.J.; Griffin, M.D.; Heinemann, S.H.; Howlett, G.J.
Methionine-oxidized amyloid fibrils are poor substrates for human methionine sulfoxide reductases A and B2
Biochemistry
49
2981-2983
2010
Homo sapiens
Manually annotated by BRENDA team
Pascual, I.; Larrayoz, I.M.; Campos, M.M.; Rodriguez, I.R.
Methionine sulfoxide reductase B2 is highly expressed in the retina and protects retinal pigmented epithelium cells from oxidative damage
Exp. Eye Res.
90
420-428
2010
Homo sapiens, Macaca mulatta
Manually annotated by BRENDA team
Lim, D.H.; Han, J.Y.; Kim, J.R.; Lee, Y.S.; Kim, H.Y.
Methionine sulfoxide reductase B in the endoplasmic reticulum is critical for stress resistance and aging in Drosophila
Biochem. Biophys. Res. Commun.
419
20-26
2012
Homo sapiens
Manually annotated by BRENDA team
Kwak, G.H.; Lim, D.H.; Han, J.Y.; Lee, Y.S.; Kim, H.Y.
Methionine sulfoxide reductase B3 protects from endoplasmic reticulum stress in Drosophila and in mammalian cells
Biochem. Biophys. Res. Commun.
420
130-135
2012
Homo sapiens
Manually annotated by BRENDA team
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