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- W67760834 abstract "Methionine sulfoxide reductases (Msrs) are oxidoreductases that catalyze thiol-dependent reduction of oxidized methionines. MsrA and MsrB are well known Msr enzymes, which have reduce methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO), respectively. Recently, an additional Msr specific for free Met-R-SO from an Escherichia coli was discovered. Here, we characterized occurrence and function of fRMsr homologs via comparative genomics and experimental analyses in Saccharomyces cerevisiae. We also propose a reaction mechanism of this enzyme based on an enzyme-substrate docking model using computational molecular dynamics and on the experiments involving trapping fRMsr-based intermolecular intermediates with thioredoxin 1. In addition, transfection of fRMsr into mammalian SK-Hep1 cells increased oxidative stress resistance and restored deficiency of these cells in the reduction of free Met-R-SO. Altogether, the data shows yeast fRMsr is the major protein that reduces free Met-R-SO in yeast cells and can also support this function in mammalian cells." @default.
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- W67760834 date "2009-04-01" @default.
- W67760834 modified "2023-09-27" @default.
- W67760834 title "Functional analysis of yeast fRMsr and its role in the reduction of free methionine‐R‐sulfoxides in yeast and mammalian cells" @default.
- W67760834 doi "https://doi.org/10.1096/fasebj.23.1_supplement.861.3" @default.
- W67760834 hasPublicationYear "2009" @default.
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