Analyses of methionine sulfoxide reductase activities towards free and peptidyl methionine sulfoxides

Title
Analyses of methionine sulfoxide reductase activities towards free and peptidyl methionine sulfoxides
Author(s)
김화영곽근희황광연[황광연]
Keywords
R-SULFOXIDE; SACCHAROMYCES-CEREVISIAE; MAMMALS; YEAST; EXPRESSION; PROTEINS; REVEALS; REPAIR; MSRA; ZINC
Issue Date
201211
Publisher
ELSEVIER SCIENCE INC
Citation
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.527, no.1, pp.1 - 5
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. (C) 2012 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/27023http://dx.doi.org/10.1016/j.abb.2012.07.009
ISSN
0003-9861
Appears in Collections:
의과대학 > 생화학.분자생물학교실 > Articles
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