Stereospecific oxidation of calmodulin by methionine sulfoxide reductase A.
Stereospecific oxidation of calmodulin by methionine sulfoxide reductase A.
复制标题
蛋氨酸亚砜还原酶 A 立体定向氧化钙调蛋白。
DOI:
10.1016/j.freeradbiomed.2013.04.004
复制
发表时间:
2013-08
影响因子:
7.4
通讯作者:
Levine, Rodney L.
中科院分区:
文献类型:
--
作者:
Lim, Jung Chae;Kim, Geumsoo;Levine, Rodney L.
关键词:
Methionine sulfoxide reductase A has long been known to reduce S-methionine sulfoxide, both as a free amino acid and within proteins. Recently the enzyme was shown to be bidirectional, capable of oxidizing free methionine and methionine in proteins to S-methionine sulfoxide. A feasible mechanism for controlling the directionality has been proposed, raising the possibility that reversible oxidation and reduction of methionine residues within proteins is a redox-based mechanism for cellular regulation. We undertook studies aimed at identifying proteins that are subject to site-specific, stereospecific oxidation and reduction of methionine residues. We found that calmodulin, which has 9 methionine residues, is such a substrate for methionine sulfoxide reductase A. When calmodulin is in its calcium bound form, Met77 is oxidized to S-methionine sulfoxide by methionine sulfoxide reductase A. When methionine sulfoxide reductase A operates in the reducing direction, the oxidized calmodulin is fully reduced back to its native form. We conclude that reversible covalent modification of Met77 may regulate the interaction of calmodulin with one or more of its many targets.
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DOI:
10.1073/pnas.0802779105
发表时间:
2008-10-28
影响因子:
11.1
作者:
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通讯作者:
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DOI:
10.1073/pnas.94.18.9932
发表时间:
1997-09-02
影响因子:
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影响因子:
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通讯作者:
Hoenderop, Joost G. J.
影响因子:
64.8
作者:
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通讯作者:
COOK, WJ