RECRUITMENT OF ENZYMES AS LENS STRUCTURAL PROTEINS
RECRUITMENT OF ENZYMES AS LENS STRUCTURAL PROTEINS
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DOI：
10.1126/science.3589669
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发表时间：
1987-06-19
期刊：
影响因子：
56.9
通讯作者：
PIATIGORSKY, J
中科院分区：
文献类型：
--
作者：
WISTOW, G;PIATIGORSKY, J
晶体蛋白是透镜的主要成分，一直被简单地认为是可溶性的结构蛋白。现在看来，脊椎动物和无脊椎动物的主要分类群特异性晶体蛋白是酶或与酶密切相关。在序列相似性、大小和其它物理特征方面。晶状体蛋白与氨基琥珀酸裂解酶密切相关，晶状体蛋白转化为烯醇化酶，以及SIII-晶状体蛋白转化为谷胱甘肽S-转移酶;此外，最近已经证明，ε-晶状体蛋白转化为烯醇化酶，以及ε-晶状体蛋白转化为谷胱甘肽S-转移酶。晶状体蛋白是一种活性乳酸脱氢酶。酶可能作为透镜蛋白被多次招募，这也许是因为组织的发育历史，或者仅仅是因为进化的实用主义（选择现有的稳定结构来扮演新的结构角色）。
Crystallins, the principal components of the lens, have been regarded simply as soluble, structural proteins. It now appears that the major taxon-specific crystallins of vertebrates and invertebrates are either enzymes or closely related to enzymes. In terms of sequence similarity, size, and other physical characteristics .delta.-crystallin is closely related to argininosuccinate lyase, .tau.-crystallin to enolase, and SIII-crystallin to glutathione S-transferase; moreover, it has recently been demonstrated that .epsilon.-crystallin is an active lactate dehydrogenase. Enzymes may have been recruited several times as lens proteins, perhaps because of the developmental history of the tissue or simply because of evolutionary pragmatism (the selection of existing stable structures for a new structural role).