PROTEIN SERINE THREONINE PHOSPHATASES - AN EXPANDING FAMILY
PROTEIN SERINE THREONINE PHOSPHATASES - AN EXPANDING FAMILY
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DOI：
10.1016/0014-5793(90)81285-v
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发表时间：
1990-08-01
期刊：
影响因子：
3.5
通讯作者：
MANN, DJ
中科院分区：
文献类型：
--
作者：
COHEN, PTW;BREWIS, ND;MANN, DJ
从哺乳动物和果蝇中克隆了5种丝氨酸/苏氨酸磷酸酶（PP）的cDNA。这些尚未被蛋白质化学和酶学技术检测到的新酶被称为PPV、PP 2Bw、PPX、PPY和PPZ。给出了PPX、PPY和PPZ的完整氨基酸序列以及PPV的几乎完整的序列。在催化结构域中，PPV和PPX与PP 2A（57-69%同一性）比PPI（45-49%同一性）更相似，而PPY和PPZ与PP 1（66-68%同一性）比PP 2A（44%同一性）更相似。PP 2BW的cDNA编码一种新的Ca ~（2+）/钙调素依赖性蛋白磷酸酶，在催化结构域中与PP 2B只有62%的相同性。确定这些蛋白磷酸酶的细胞功能的方法进行了讨论。
Five protein serine/threonine phosphatases (PP) have been identified by cloning cDNA from mammalian andDrosophilalibraries. These novel enzymes, which have not yet been detected by the techniques of protein chemistry and enzymology, are termed PPV, PP2Bw, PPX, PPY and PPZ. The complete amino acid sequences of PPX, PPY and PPZ and an almost complete sequence of PPV are presented. In the catalytic domain PPV and PPX are more similar to PP2A (57–69% identity) than PPI (45–49% identity), while PPY and PPZ are more similar to PP1 (66–68% identity) than PP2A (44% identity). The cDNA for PP2BWencodes a novel Ca2+/calmodulin-dependent protein phosphatase only 62% identical to PP2B in the catalytic domain. Approaches for determining the cellular functions of these protein phosphatases are discussed.