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UniProt
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UniProt
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UniProt
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UniProt
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brenda
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brenda
ECW-30R
UniProt
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UniProt
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enzyme belongs to the metal-containing MsrB group I
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UniProt
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UniProt
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ATCC 43049
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SwissProt
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serovar Copenhageni
SwissProt
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Leptospira interrogans Fiocruz L1-130
serovar Copenhageni
SwissProt
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in murine gut
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in murine gut
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DSM 6242
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strain delta H
UniProt
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DSM 2160
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variant VD300, bifunctional enzyme MsrA/B, gene pilB
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brenda
no activity in Aeropyrum pernix K1
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brenda
no activity in Aquifex aeolicus
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brenda
no activity in Archaeoglobus fulgidus DSM 4304
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brenda
no activity in Bifidobacterium longum
NCC2705
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brenda
no activity in Bifidobacterium longum NCC2705
NCC2705
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brenda
no activity in Clostridium tetani
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brenda
no activity in Clostridium tetani E88
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brenda
no activity in Ferroplasma acidarmanus
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brenda
no activity in Methanocaldococcus jannaschii
DSM 2661
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brenda
no activity in Methanococcus maripaludis
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brenda
no activity in Methanococcus maripaludis S2
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brenda
no activity in Methanopyrus kandleri
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brenda
no activity in Methanopyrus kandleri AV19
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brenda
no activity in Nanoarchaeum equitans
Kin4-M
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brenda
no activity in Nanoarchaeum equitans Kin4-M
Kin4-M
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brenda
no activity in Picrophilus torridus
strain DSM 9790
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brenda
no activity in Pyrobaculum aerophilum
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brenda
no activity in Pyrobaculum aerophilum IM2
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brenda
no activity in Pyrococcus abyssi
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no activity in Pyrococcus abyssi GE5
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brenda
no activity in Pyrococcus furiosus
strain DSM 3638
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brenda
no activity in Pyrococcus horikoshii
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brenda
no activity in Pyrococcus horikoshii OT3
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brenda
no activity in Sulfolobus acidocaldarius
DSM 639
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brenda
no activity in Sulfolobus solfataricus
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no activity in Sulfolobus solfataricus P2
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brenda
no activity in Sulfolobus tokodaii
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brenda
no activity in Sulfolobus tokodaii 7
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brenda
no activity in Thermococcus kodakarensis
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brenda
no activity in Thermococcus kodakarensis KOD1
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brenda
no activity in Thermoplasma acidophilum
DSM 1728
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brenda
no activity in Thermoplasma volcanium
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brenda
no activity in Thermoplasma volcanium GSS1
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brenda
no activity in Thermotoga maritima
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brenda
cv. Dongjing
UniProt
brenda
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UniProt
brenda
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UniProt
brenda
enzyme belongs to the metal-containing MsrB group I
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brenda
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brenda
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UniProt
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UniProt
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enzyme MsrB
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brenda
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UniProt
brenda
winter rye, cv. Halo
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3 copies of gene msrB
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brenda
enzyme belongs to the metal-containing MsrB group I
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brenda
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brenda
bifunctional methionine sulfoxide reductase AB, cf. EC 1.8.1.11
UniProt
brenda
bifunctional methionine sulfoxide reductase AB, cf. EC 1.8.1.11
UniProt
brenda
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brenda
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SwissProt
brenda
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SwissProt
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brenda
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brenda
3 isozymes of MsrB
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brenda
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UniProt
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UniProt
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brenda
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Yarrowia lipolytica YlCW001 v1.0
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brenda
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SwissProt
brenda
5 genes, including 1 plastidic isozyme
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brenda
ecotype Columbia
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brenda
isozymes MsrB1-3
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brenda
plastidic isozymes MsrB1 and MsrB2
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brenda
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brenda
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SwissProt
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calf
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MsrB variants one of which is also called Sel-X
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brenda
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SwissProt
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SwissProt
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brenda
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SwissProt
brenda
1 copy gene msrB
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brenda
enzyme belongs to the metal-containing MsrB group I
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brenda
enzyme forms MsrB and Mem-R,S-Msr
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brenda
enzyme forms MsrB, and other enzyme forms, e.g. Mem-R,S-Msr, overview
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brenda
gene msrB, enzyme SelR which is a selenoprotein, enzyme is organized in a fusion protein together with MsrA, EC 1.8.4.B2
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brenda
wild-type strain MC1061, isozyme MsrB and a membrane-associated isozyme
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brenda
isoform MsrB
UniProt
brenda
isoform MsrB2
UniProt
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isoform MsrB3
UniProt
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isoform MsrB4
UniProt
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isoform MsrB
UniProt
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isoform MsrB2
UniProt
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isoform MsrB3
UniProt
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isoform MsrB4
UniProt
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isoform MsrB1
UniProt
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isoform MsrB5
UniProt
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brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
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brenda
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brenda
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SwissProt
brenda
enzyme forms MsrA and MsrB are fused together forming a single protein termed Msr
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brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
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brenda
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brenda
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SwissProt
brenda
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SwissProt
brenda
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SwissProt
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SwissProt
brenda
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SwissProt
brenda
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SwissProt
brenda
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brenda
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SwissProt
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SwissProt
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SwissProt
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SwissProt
brenda
isozyme MsrB2
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brenda
isozymes MsrB1 or selenoprotein R, MsrB2 or CBS-1, and MsrB3
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brenda
isozymes MsrB1, MsrB2, and MsrB3
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brenda
isozymes MsrB1-3
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brenda
MsrB variants one of which is also called Sel-X, encoded by distinct genes, MsrB is a selenoprotein
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brenda
MsrB, one isozyme of which is termed CBS-1
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brenda
overexpressed in Escherichia coli BL21
SwissProt
brenda
several splicing variants resulting in three isozymes MsrB1-3
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brenda
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brenda
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SwissProt
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SwissProt
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SwissProt
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SwissProt
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brenda
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Uniprot
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brenda
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Uniprot
brenda
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SwissProt
brenda
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Uniprot
brenda
isozyme MsrB3
SwissProt
brenda
isozymes MsrB1, MsrB2, and MsrB3
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brenda
isozymes MsrB1-3
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brenda
MsrB is a selenoprotein
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brenda
overexpressed in Escherichia coli BL21
SwissProt
brenda
selenomethionine-containing enzyme MsrB
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brenda
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brenda
bifunctional enzyme MsrA/B, gene pilB
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brenda
enzyme belongs to the MsrB group IIS
SwissProt
brenda
enzyme contains 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, the MsrB domain contains a selenomethionine at position 39
SwissProt
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
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brenda
variant VD300, bifunctional enzyme MsrA/B, gene pilB
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brenda
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brenda
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UniProt
brenda
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brenda
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UniProt
brenda
2 structurally unrelated enzymes with different stereospecificity, MsrA, EC 1.8.4.B2, and MsrB, which occur in different variants, but are located on one protein
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brenda
bifunctional enzyme MsrA/B
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brenda
enzyme belongs to the MsrB group IIS
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brenda
enzyme PILB, a peptide methionine sulfoxide reductase with 2 subdomains MsrA and MsrB with opposite stereospecificity, MsrA activity belongs to EC 1.8.4.B2
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brenda
gene msr encodes an enzyme showing both MsrA, EC 1.8.4.B2, and MsrB activity
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brenda
PilB enzyme has 2 catalytic domains showing MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity, respectively
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brenda
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brenda
precursor
SwissProt
brenda
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brenda
enzyme MsrB
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brenda
isozymes MsrB1-3
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brenda
MsrB variants one of which is also called Sel-X
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brenda
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brenda
1 copy of gene msrB
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brenda
PilB
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brenda
strains RN450 and BB270, and derivatives, 1 gene msrB
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brenda
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SwissProt
brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
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brenda
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brenda
gene msr encodes an enzyme showing both MsrA, methionine S-oxide reductase (S-form oxidizing), and MsrB, methionine S-oxide reductase (R-form oxidizing), activity
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brenda
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UniProt
brenda
2 structurally unrelated enzyme forms with different stereospecificity, MsrA and MsrB, which occur in different variants
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brenda
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brenda
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UniProt
brenda