Use of fluorinated tyrosine phosphates to probe the substrate specificity of the low molecular weight phosphatase activity of calcineurin.
Use of fluorinated tyrosine phosphates to probe the substrate specificity of the low molecular weight phosphatase activity of calcineurin.
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DOI：
10.1016/s0021-9258(18)95682-6
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发表时间：
1985-12
期刊：
影响因子：
--
通讯作者：
B. Martin;C. Pallen;J. H. Wang;D. Graves
中科院分区：
文献类型：
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作者：
B. Martin;C. Pallen;J. H. Wang;D. Graves
钙调神经磷酸酶是一种钙调蛋白激活的蛋白磷酸酶，已知可以使某些低分子量磷酸酯去磷酸化。已利用酪氨酸磷酸衍生物研究了钙调神经磷酸酶的低分子量磷酸酶活性。动力学研究表明，底物特异性取决于底物的电子性质，这与使用大肠杆菌碱性磷酸酶获得的结果相反。钙调神经磷酸酶和酸催化水解的比较表明，两个过程的速率常数之间存在 1:1 的相关性。这种相关性和其他模型研究已被用来深入了解钙调神经磷酸酶的化学机制。讨论了钙调神经磷酸酶可能的化学机制。
Calcineurin, a calmodulin-activated protein phosphatase, is known to dephosphorylate certain low molecular weight phosphate esters. The low molecular weight phosphatase activity of calcineurin has been studied by utilizing tyrosine phosphate derivatives. Kinetic studies suggest that the substrate specificity is dependent upon the electronic nature of the substrate in contrast to results obtained with alkaline phosphatase from Escherichia coli. Comparison of calcineurin and acid-catalyzed hydrolyses indicates a 1:1 correlation between the rate constants for the two processes. This correlation and other model studies have been utilized to provide insight into the chemical mechanism of calcineurin. Possible chemical mechanisms for calcineurin are discussed.