AI Article Synopsis
- The study analyzed the kinetic properties of mammalian and yeast methionine sulfoxide reductases (MsrBs and MsrAs) to compare their abilities to reduce free and peptide methionine sulfoxide (Met-O).
- The results showed that MsrBs were significantly less efficient at reducing free Met-O compared to yeast fRMsr, with a ratio of free to peptide activity being 1:20-40.
- Conversely, MsrAs from both organisms exhibited much higher catalytic efficiency for free Met-O, with yeast MsrA showing a near-equal ability to reduce free and peptide Met-O, validated by in vivo assays.
Article Abstract
There have been insufficient kinetic data that enable a direct comparison between free and peptide methionine sulfoxide reductase activities of either MsrB or MsrA. In this study, we determined the kinetic parameters of mammalian and yeast MsrBs and MsrAs for the reduction of both free methionine sulfoxide (Met-O) and peptidyl Met-O under the same assay conditions. Catalytic efficiency of mammalian and yeast MsrBs towards free Met-O was >2000-fold lower than that of yeast fRMsr, which is specific for free Met-R-O. The ratio of free to peptide Msr activity in MsrBs was 1:20-40. In contrast, mammalian and yeast MsrAs reduced free Met-O much more efficiently than MsrBs. Their k(cat) values were 40-500-fold greater than those of the corresponding MsrBs. The ratio of free to peptide Msr activity was 1:0.8 in yeast MsrA, indicating that this enzyme can reduce free Met-O as efficiently as peptidyl Met-O. In addition, we analyzed the in vivo free Msr activities of MsrBs and MsrAs in yeast cells using a growth complementation assay. Mammalian and yeast MsrBs, as well as the corresponding MsrAs, had apparent in vivo free Msr activities. The in vivo free Msr activities of MsrBs and MsrAs agreed with their in vitro activities.
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| http://dx.doi.org/10.1016/j.abb.2012.07.009 | DOI Listing |
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