Methionine sulfoxide reductase contributes to meeting dietary methionine requirements

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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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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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Reduction of methionine sulfoxide to methionine by Escherichia coli.

L-Methionine-dl-sulfoxide can support the growth of an Escherichia coli methionine auxotroph, suggesting the presence of an enzyme(s) capable of reducing the sulfoxide to methionine. This was verified by showing that a cell-free extract of E. coli catalyzes the conversion of methionine sulfoxide to methionine. This reaction required reduced nicotinamide adenine dinucleotide phosphate and a gene...

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Methionine Sulfoxide Reductase System in Health and Disease

cell cultures has been shown to protect these cells from enhanced MetO accumulations while increasing their survival rates under oxidative stress conditions [24]. In addition, several compounds have demonstrated an ability to induce Msr activity in neuronal cell cultures [25]. This observation supports the identification and development of novel compounds that may serve as therapy treatments ag...

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ژورنال

عنوان ژورنال: Archives of Biochemistry and Biophysics

سال: 2012

ISSN: 0003-9861

DOI: 10.1016/j.abb.2012.03.029