Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase [PDF]
Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D‐sulfoxide diastereomer of CaM ...
Christian Schöneich +2 more
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Methionine sulfoxide reductase contributes to meeting dietary methionine requirements [PDF]
Methionine sulfoxide reductases are present in all aerobic organisms. They contribute to antioxidant defenses by reducing methionine sulfoxide in proteins back to methionine. However, the actual in vivo roles of these reductases are not well defined.
Rodney L Levine, Geumsoo Kim
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Reduction of methionine sulfoxide to methionine by Escherichia coli [PDF]
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.
S I, Ejiri, H, Weissbach, N, Brot
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Methionine sulfoxide reductase A is a stereospecific methionine oxidase [PDF]
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.
Jung Chae, Lim +3 more
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Selenium and methionine sulfoxide reduction
Methionine residues in proteins can be readily oxidized to a diastereomeric mixture of methionine sulfoxides by reactive oxygen species. In most organisms, methionine sulfoxides are reversibly and stereospecifically reduced back to methionine by two distinct classes of repair enzymes, methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide ...
Kim, Hwa-Young, Gladyshev, Vadim N.
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Monitoring of Methionine Sulfoxide Content and Methionine Sulfoxide Reductase Activity [PDF]
The sulfur-containing amino acid methionine (Met) plays critical roles in protein synthesis, methylation, and sulfur metabolism. Both in its free form and in the form of an amino acid residue, it can be oxidized to the R and S diastereomers of methionine sulfoxide (MetO).
Tarrago, Lionel +3 more
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Inhibition of methionine sulfoxide reduction by dimethyl sulfoxide
Dimethyl sulfoxide (DMSO) is widely used in chemistry and biology as a solvent and as a cryoprotectant. It is also used as a pharmaceutical agent for the treatment of interstitial cystitis and rheumatoid arthritis. Previous reports described DMSO as being reduced by methionine-S-sulfoxide reductase (MsrA).
Geun-Hee, Kwak +3 more
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Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases [PDF]
Methionine residues in proteins are susceptible to oxidation by reactive oxygen species, but can be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductase (MsrA) and methionine-R-sulfoxide reductase (MsrB).
Kim, Hwa-Young, Gladyshev, Vadim
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Methionine Sulfoxide Reduction and the Aging Process [PDF]
Abstract: Aging has been described for multicellular and asymmetrically dividing organisms, but the mechanisms are poorly understood. Oxidation of proteins is considered to be one of the major factors that leads to aging. Oxidative damage to proteins results in the oxidation of certain amino acid residues, among which oxidation of sulfur‐containing ...
Koç, Ahmet, Gladyshev, Vadim N.
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Methionine Sulfoxide Reductases of Archaea [PDF]
Methionine sulfoxide reductases are found in all domains of life and are important in reversing the oxidative damage of the free and protein forms of methionine, a sulfur containing amino acid particularly sensitive to reactive oxygen species (ROS). Archaea are microbes of a domain of life distinct from bacteria and eukaryotes.
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