Glutathione transferases: new functions
Glutathione transferases: new functions
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DOI：
10.1016/j.sbi.2005.10.005
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发表时间：
2005-12-01
影响因子：
6.8
通讯作者：
Oakley, AJ
中科院分区：
文献类型：
--
作者：
Oakley, AJ
众所周知，谷胱甘肽转移酶是解毒酶，在前列腺素和类固醇激素的合成中也起作用。典型的谷胱甘肽转移酶折叠的新用途变得越来越明显;细菌严格饥饿蛋白SspA和酵母朊病毒蛋白Ure 2 p（两种转录因子）被发现采用这种折叠，但它们的作用仍然不清楚。细胞内氯离子通道CLIC 1以其可溶性形式采用典型的谷胱甘肽转移酶折叠，并且似乎作为其膜插入过程的一部分进行了彻底的结构修饰。大鼠和人类线粒体谷胱甘肽转移酶的结构已经得到解决：它们采用了类似于细菌二硫键异构酶的拓扑结构，这表明它们独立于典型酶进化。最近的结构研究的整体膜谷胱甘肽S-转移酶从微粒体揭示了共同的模式的三级和四级结构。
Well known as detoxification enzymes, the glutathione transferases also function in prostaglandin and steroid hormone synthesis. New uses for the canonical glutathione transferase fold are becoming apparent; the bacterial stringent starvation protein SspA and the yeast prion protein Ure2p (both transcription factors) were found to adopt this fold, but their roles remain unclear. The intracellular chloride ion channel CLIC1 adopts the canonical glutathione transferase fold in its soluble form and appears to undergo radical structural modification as part of its membrane insertion process. The structures of rat and human mitochondrial glutathione transferases have been solved: they adopt a topology similar to that of bacterial disulfide bond isomerases, leading to the suggestion that they have evolved independently of the canonical enzymes. Recent structural studies of integral membrane glutathione S-transferases from microsomes have revealed common patterns of tertiary and quaternary structure.