Zhao Z, Shen S H, Fischer E H
Department of Biochemistry, University of Washington, Seattle 98195.
Proc Natl Acad Sci U S A. 1993 May 1;90(9):4251-5. doi: 10.1073/pnas.90.9.4251.
PTP1C, a protein-tyrosine-phosphatase (protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) containing two src homology 2 domains, is poorly active when assayed with various protein substrates in vitro. Its activity is stimulated > 1000-fold by anionic phospholipids when myelin basic protein or mitogen-activated protein kinase is used as substrate but reduced in the presence of several other substrates. Data are presented to indicate a direct interaction of the enzyme with phospholipids. Enzyme stimulation directed only toward certain specific substrates is interpreted by assuming that these compounds also bind to the phospholipid vesicles where they will be subjected to rapid enzymatic attack. A possible regulation of PTP1C by its translocation to the cell membrane is hypothesized.
蛋白酪氨酸磷酸酶1C（PTP1C）是一种含有两个src同源结构域2的蛋白酪氨酸磷酸酶（蛋白酪氨酸磷酸磷酸水解酶，EC 3.1.3.48），在体外使用各种蛋白质底物进行检测时活性较低。当以髓鞘碱性蛋白或丝裂原活化蛋白激酶为底物时，其活性受到阴离子磷脂的刺激，活性增加超过1000倍，但在存在其他几种底物时活性降低。提供的数据表明该酶与磷脂存在直接相互作用。仅针对某些特定底物的酶刺激作用可以通过假设这些化合物也与磷脂囊泡结合来解释，在磷脂囊泡中它们将受到快速的酶促攻击。推测PTP1C可能通过转位到细胞膜而受到调节。
