整合膜磷酸酶与可溶性卤过氧化物酶之间意想不到的结构关系。
An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
作者信息
Neuwald A F
机构信息
National Center for Biotechnology Information, National Institutes of Health, Bethesda, Maryland 20894, USA.
出版信息
Protein Sci. 1997 Aug;6(8):1764-7. doi: 10.1002/pro.5560060817.
Abstract
The mechanism of a membrane-bound enzyme important in phospholipid signaling, type 2 phosphatidic acid phosphatase, is suggested by sequence motifs shared with a soluble vanadium-dependent chloroperoxidase of known structure. These regions are also conserved in other soluble globular and membrane-associated proteins, including bacterial acid phosphatases, mammalian glucose-6-phosphatases, and the Drosophila developmental protein Wunen. This implies that a similar arrangement of catalytic residues specifies the active site within both soluble and membrane spanning domains.
摘要
一种在磷脂信号传导中起重要作用的膜结合酶——2型磷脂酸磷酸酶的作用机制，可通过与已知结构的可溶性钒依赖性氯过氧化物酶共有的序列基序来推测。这些区域在其他可溶性球状蛋白和膜相关蛋白中也保守，包括细菌酸性磷酸酶、哺乳动物葡萄糖-6-磷酸酶以及果蝇发育蛋白Wunen。这意味着催化残基的类似排列确定了可溶性结构域和跨膜结构域内的活性位点。
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