Goris J, Pallen C J, Parker P J, Hermann J, Waterfield M D, Merlevede W
Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Campus Gasthuisberg, Belgium.
Biochem J. 1988 Dec 15;256(3):1029-34. doi: 10.1042/bj2561029.
By use of the autophosphorylated epidermal-growth-factor receptor and the synthetic peptide RRLIE-DAEY(P)AARG, representing an autophosphorylation site of the transforming protein of Rous-sarcoma virus, it is demonstrated that the phosphotyrosyl phosphatase activity of the polycation-stimulated phosphatases is substantially increased by an enzyme-directed effect of ATP or PPi. Concomitant with this increase in phosphotyrosyl phosphatase activity, the phosphorylase phosphatase activity is decreased, thus dramatically changing the substrate specificity of these enzymes. The dephosphorylation of four different phosphotyrosyl sites of the epidermal-growth-factor receptor is neither consecutive nor at random, but a preferred dephosphorylation of the P1 site over the P3 greater than P2 greater than P4 sites is observed. This phosphatase activity represents a substantial fraction of the total phosphotyrosyl phosphatase activity in the post-mitochondrial supernatant of Xenopus laevis oocytes.
通过使用自磷酸化的表皮生长因子受体以及代表劳氏肉瘤病毒转化蛋白自磷酸化位点的合成肽RRLIE-DAEY(P)AARG,已证明多阳离子刺激的磷酸酶的磷酸酪氨酸磷酸酶活性因ATP或PPi的酶导向作用而显著增加。伴随着磷酸酪氨酸磷酸酶活性的这种增加,磷酸化酶磷酸酶活性降低,从而极大地改变了这些酶的底物特异性。表皮生长因子受体的四个不同磷酸酪氨酸位点的去磷酸化既不是连续的也不是随机的,而是观察到P1位点比P3位点优先去磷酸化,且P3大于P2大于P4位点。这种磷酸酶活性在非洲爪蟾卵母细胞的线粒体后上清液中的总磷酸酪氨酸磷酸酶活性中占很大一部分。