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Literature summary extracted from

  • Kim, H.Y.; Gladyshev, V.N.
    Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals (2007), Biochem. J., 407, 321-329.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.11
-
Escherichia coli
1.8.4.11 overexpression of bovine MsrA in Drosophila extends lifespan by 70%, as well as increased resistance to paraquat-induced oxidative stress Bos taurus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.4.11
-
Escherichia coli
1.8.4.11
-
Bos taurus
1.8.4.11
-
Mycobacterium tuberculosis
1.8.4.11
-
Populus trichocarpa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.4.11 mitochondrion
-
Mus musculus 5739
-
1.8.4.11 plastid
-
Populus trichocarpa 9536
-
1.8.4.12 endoplasmic reticulum MsrB3 has consecutive endoplasmic reticulum and mitochondrial targeting signals at the N-terminus. This protein is targeted to the endoplasmic reticulum, and the function of the mitochondrial signal appears to be masked by the endoplasmic reticulum signal peptide Mus musculus 5783
-
1.8.4.12 endoplasmic reticulum 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 Homo sapiens 5783
-
1.8.4.12 mitochondrion MsrB3B contains a different signal peptide at the N-terminus and is targeted to mitochondria Homo sapiens 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.4.11 selenium selenocysteine-containing Escherichia coli
1.8.4.11 selenium selenocysteine-containing Homo sapiens
1.8.4.11 selenium selenocysteine-containing Bos taurus
1.8.4.11 selenium selenocysteine-containing Neisseria gonorrhoeae
1.8.4.11 selenium selenocysteine-containing Neisseria meningitidis
1.8.4.11 selenium selenocysteine-containing Mycobacterium tuberculosis
1.8.4.11 selenium selenocysteine-containing Populus trichocarpa
1.8.4.11 selenium selenocysteine-containing Mus musculus
1.8.4.12 selenium selenocysteine-containing Drosophila melanogaster
1.8.4.12 selenium selenocysteine-containing Neisseria meningitidis
1.8.4.12 selenium selenocysteine-containing Homo sapiens
1.8.4.12 selenium selenocysteine-containing Mus musculus
1.8.4.12 selenium selenocysteine-containing Bacillus subtilis
1.8.4.12 Zinc zinc-containing enzyme Drosophila melanogaster
1.8.4.12 Zinc zinc-containing enzyme Homo sapiens
1.8.4.12 Zinc zinc-containing enzyme Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.11 Bos taurus
-
-
-
1.8.4.11 Escherichia coli
-
-
-
1.8.4.11 Homo sapiens
-
-
-
1.8.4.11 Mus musculus Q9D6Y7
-
-
1.8.4.11 Mycobacterium tuberculosis
-
-
-
1.8.4.11 Neisseria gonorrhoeae
-
-
-
1.8.4.11 Neisseria meningitidis
-
-
-
1.8.4.11 Populus trichocarpa
-
-
-
1.8.4.12 Bacillus subtilis P54155
-
-
1.8.4.12 Drosophila melanogaster
-
-
-
1.8.4.12 Homo sapiens Q8IXL7
-
-
1.8.4.12 Mus musculus Q8BU85
-
-
1.8.4.12 Neisseria meningitidis
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.4.11 skin up-regulation of the protein in response to UV irradiation and hydrogen peroxide, suggesting a role of MsrA in photoprotection in epidermis Homo sapiens
-

Synonyms

EC Number Synonyms Comment Organism
1.8.4.11 MsrA
-
Escherichia coli
1.8.4.11 MsrA
-
Homo sapiens
1.8.4.11 MsrA
-
Bos taurus
1.8.4.11 MsrA
-
Mycobacterium tuberculosis
1.8.4.11 MsrA
-
Populus trichocarpa
1.8.4.11 MsrA
-
Mus musculus
1.8.4.11 MsrA/MsrB bifunctional enzyme EC 1.8.4.11/EC 1.8.4.12 Neisseria gonorrhoeae
1.8.4.11 MsrA/MsrB bifunctional enzyme EC 1.8.4.11/EC 1.8.4.12 Neisseria meningitidis
1.8.4.12 MsrA/MsrB bifunctional enzyme EC 1.8.4.11/EC 1.8.4.12 Neisseria meningitidis
1.8.4.12 MsrB
-
Drosophila melanogaster
1.8.4.12 MsrB
-
Bacillus subtilis
1.8.4.12 MsrB3
-
Mus musculus
1.8.4.12 MsrB3 MsrB3 occurs in two forms, MsrB3A and MsrB3B, owing to alternative first exon splicing Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.12 additional information thioredoxin independent Homo sapiens