Structural Insights into Interaction between Mammalian Methionine Sulfoxide Reductase B1 and Thioredoxin

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Structural Insights into Interaction between Mammalian Methionine Sulfoxide Reductase B1 and Thioredoxin

Maintenance of the cellular redox balance has vital importance for correcting organism functioning. Methionine sulfoxide reductases (Msrs) are among the key members of the cellular antioxidant defence system. To work properly, methionine sulfoxide reductases need to be reduced by their biological partner, thioredoxin (Trx). This process, according to the available kinetic data, represents the s...

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Diversity of Protein and mRNA Forms of Mammalian Methionine Sulfoxide Reductase B1 Due to Intronization and Protein Processing

BACKGROUND Methionine sulfoxide reductases (Msrs) are repair enzymes that protect proteins from oxidative stress by catalyzing stereospecific reduction of oxidized methionine residues. MsrB1 is a selenocysteine-containing cytosolic/nuclear Msr with high expression in liver and kidney. PRINCIPAL FINDINGS Here, we identified differences in MsrB1 gene structure among mammals. Human MsrB1 gene co...

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Selenium and the methionine sulfoxide reductase system.

Selenium is a chemical element participating in the synthesis of selenocysteine residues that play a pivotal role in the enzymatic activity efficiency of selenoproteines. The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which reduce the R- and the S- forms of MetO, resp...

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NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus.

Isotopically labeled, 15N and 15N/13C forms of recombinant methionine-r-sulfoxide reductase 1 (MsrB1, SelR) from Mus musculus were produced, in which catalytic selenocysteine was replaced with cysteine. We report here the 1H, 13C and 15N NMR assignment of the reduced form of this mammalian protein.

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Methionine sulfoxide reductase A is a stereospecific methionine oxidase.

Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide. The enzyme participates in defense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methionine. Because oxidation of methionine residues is reversible, this covalent modification could also functio...

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ژورنال

عنوان ژورنال: Journal of Biomedicine and Biotechnology

سال: 2012

ISSN: 1110-7243,1110-7251

DOI: 10.1155/2012/586539