受磷蛋白的亲水区抑制Ca(2+)-ATP酶的Ca2+转运步骤。
The hydrophilic domain of phospholamban inhibits the Ca2+ transport step of the Ca(2+)-ATPase.
作者信息
Hughes G, East J M, Lee A G
机构信息
Department of Biochemistry, University of Southampton, U.K.
出版信息
Biochem J. 1994 Oct 15;303 ( Pt 2)(Pt 2):511-6. doi: 10.1042/bj3030511.
Abstract
The peptide MEKVQYLTRSAIRRASTIEMPQQAR-Cys corresponding to residues 1-25 of phospholamban was found to inhibit the ATPase activity of skeletal muscle Ca(2+)-ATPase, but to have no effect on the Ca(2+)-dependence of its activity. The peptide was found to decrease the rate of the Ca2+ transport step (E1PCa2-->E2P) by a factor of 2.4. The rate of this same step was decreased by poly(L-Arg) by a factor of 2.2. The peptide shifted the E2-E1 equilibrium of the ATPase towards E1 by a factor of 4 due to stronger binding to the E1 than to the E2 conformation of the ATPase; dissociation constants for binding to E1 and E2 were estimated as 3 and 10 microM respectively. The peptide had no effect on the level of phosphorylation by Pi in the absence of Ca2+ or on the rate of phosphorylation by ATP in the presence of Ca2+.
摘要
与受磷蛋白1 - 25位残基相对应的肽MEKVQYLTRSAIRRASTIEMPQQAR - Cys被发现可抑制骨骼肌Ca(2 +)-ATP酶的ATP酶活性，但对其活性的Ca(2 +)依赖性没有影响。该肽使Ca2 +转运步骤（E1PCa2→E2P）的速率降低了2.4倍。相同步骤的速率被聚（L - 精氨酸）降低了2.2倍。由于该肽与ATP酶的E1构象的结合强于与E2构象的结合，它使ATP酶的E2 - E1平衡向E1方向移动了4倍；与E1和E2结合的解离常数分别估计为3和10 microM。该肽在无Ca2 +时对Pi的磷酸化水平或在有Ca2 +时对ATP的磷酸化速率均无影响。
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