Functions and evolution of selenoprotein methionine sulfoxide reductases.
Functions and evolution of selenoprotein methionine sulfoxide reductases.
复制标题
硒蛋白硫氨酸还原酶的功能和进化。
DOI:
10.1016/j.bbagen.2009.04.014
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发表时间:
2009-11
期刊:
影响因子:
--
通讯作者:
Gladyshev VN
中科院分区:
文献类型:
--
作者:
Lee BC;Dikiy A;Kim HY;Gladyshev VN
Methionine sulfoxide reductases (Msrs) are thiol-dependent enzymes which catalyze conversion of methionine sulfoxide to methionine. Three Msr families, MsrA, MsrB, and fRMsr, are known. MsrA and MsrBs are responsible for the reduction of methionine-S-sulfoxide and methionine-R-sulfoxide residues in proteins, respectively, whereas fRMsr reduces free methionine-R-sulfoxide. Besides acting on proteins, MsrA can additionally reduce free methionine-S-sulfoxide. Some MsrAs and MsrBs evolved to utilize catalytic selenocysteine. This includes MsrB1, which is a major MsrB in cytosol and nucleus in mammalian cells. Specialized machinery is used for insertion of selenocysteine into MsrB1 and other selenoproteins at in-frame UGA codons. Selenocysteine offers catalytic advantage to the protein repair function of Msrs, but also makes these proteins dependent on the supply of selenium and requires adjustments in their strategies for regeneration of active enzymes. Msrs have roles in protecting cellular proteins from oxidative stress and through this function they may regulate lifespan in several model organisms.
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