Results 31 to 40 of about 180,383 (183)
Shipin gongye ke-ji, 2022 Methionine sulfoxide reductase (Msr) is a kind of antioxidant enzyme that can scavenge free radicals and repair oxidized proteins by reducing methionine sulfoxide to active methionine.
Xiaodong FU +5 more
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Antioxidants, 2021 Methionine is an aliphatic, sulfur-containing, essential amino acid that has been demonstrated to have crucial roles in metabolism, innate immunity, and activation of endogenous antioxidant enzymes, including methionine sulfoxide reductase A/B and the ...
Mariano Catanesi +11 more
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Frontiers in Chemistry, 2021 Chiral sulfoxides are valuable organosulfur compounds that have been widely used in medicinal and organic synthesis. Biocatalytic approaches for preparing chiral sulfoxides were developed in the past few years, mainly through asymmetric oxidation of ...
Tao Peng +4 more
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Methionine Sulfoxide Reduction in Mammals: Characterization of Methionine-R-Sulfoxide Reductases [PDF]
Molecular Biology of the Cell, 2004 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 reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase. [PDF]
Biochem J, 2018 The oxidation of methionine residues in proteins occurs during oxidative stress and can lead to an alteration in protein function. The enzyme methionine sulfoxide reductase reverses this modification.
Cao Z +9 more
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Data in Brief, 2018 Aerobic respiratory growth generates endogenous reactive oxygen species (ROS). ROS oxidize protein-bound methionine residues into methionine sulfoxide.
Jean-Paul Madeira +3 more
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mBio, 2023 Campylobacter concisus, an emerging pathogen found throughout the human oral-gastrointestinal tract, is able to grow under microaerobic or anaerobic conditions; in the latter case, N- or S-oxides could be used as terminal electron acceptors (TEAs ...
Stéphane L. Benoit, Robert J. Maier
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Drosophila methionine sulfoxide reductase A (MSRA) lacks methionine oxidase activity. [PDF]
Free Radic Biol Med, 2019 Mouse, human, and E. coli methionine sulfoxide reductase A (MSRA) stereospecifically catalyze both the reduction of S-methionine sulfoxide to methionine and the oxidation of methionine to S-methionine sulfoxide. Calmodulin has 9 methionine residues, but only Met77 is oxidized by MSRA, and this is completely reversed when MSRA operates in the reductase ...
Tarafdar S, Kim G, Levine RL.
europepmc +4 more sources
The selenoprotein methionine sulfoxide reductase B1 (MSRB1)
Free Radical Biology and Medicine, 2022 Methionine (Met) can be oxidized to methionine sulfoxide (MetO), which exist as R- and S-diastereomers. Present in all three domains of life, methionine sulfoxide reductases (MSR) are the enzymes that reduce MetO back to Met. Most characterized among them are MSRA and MSRB, which are strictly stereospecific for the S- and R-diastereomers of MetO ...
Tarrago, Lionel +5 more
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Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide. [PDF]
PLoS Pathogens, 2017 Vibrio cholerae is a diarrheal pathogen that induces accumulation of lipid droplets in enterocytes, leading to lethal infection of the model host Drosophila melanogaster. Through untargeted lipidomics, we provide evidence that this process is the product
Audrey S Vanhove +5 more
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