Regulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1.
Seoul, South Korea. In Antioxid Redox Signal, Nov 2015
RECENT ADVANCES: Reversible oxidation of methionine residues by monooxygenases of the Mical family and subsequent reduction of methionine sulfoxides by a selenocysteine-containing methionine sulfoxide reductase B1 (MsrB1) was found to control the assembly and disassembly of actin in mammals, and the Mical/MsrB pair similarly regulates actin in fruit flies.
Prevalence and characterization of methicillin susceptible Staphylococcus aureus ST398 isolates from retail foods.
China. In Int J Food Microbiol, Apr 2015
No isolate carried mecA, tet(M), tet(O), fexA, aac(6')/aph(2″), cfr, ermT, msrB, cat::pC194, cat::pC223, catpIp-501, dfrD, dfrG and dfrS1 genes.
The biological significance of methionine sulfoxide stereochemistry.
Boston, United States. In Free Radic Biol Med, 2011
Both free amino acid and protein-based forms of methionine-S-sulfoxide are stereospecifically reduced by MsrA, whereas the reduction of methionine-R-sulfoxide requires two enzymes, MsrB and fRMsr, which act on its protein-based and free amino acid forms, respectively.