"In-gel" assay for identifying alternative nucleotide substrates for protein kinases.
"In-gel" assay for identifying alternative nucleotide substrates for protein kinases.
复制标题
用于鉴定蛋白激酶替代核苷酸底物的“凝胶内”测定。
DOI：
10.1006/abio.1999.4150
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Kennelly,PJ
中科院分区：
文献类型：
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作者：
Bischoff,KM;Kennelly,PJ
蛋白激酶催化磷酰基从高能供体转移到蛋白质上氨基酸残基（例如丝氨酸、苏氨酸、酪氨酸、天冬氨酸或组氨酸）的侧链官能团 (1)。虽然许多蛋白激酶表现出完全依赖 ATP 作为磷酰基供体底物，但已报道了这种模式的一些例外情况。其中最著名且记录最详尽的是酪蛋白激酶 II，它可以在体外利用 ATP 或 GTP 作为磷酰基供体 (2)。来自枯草芽孢杆菌的 HPr 激酶显示出类似的功能 (3)，零散的报告表明蛋白激酶 C 也可能具有这种功能 (4, 5)。此外，在人呼吸道上皮提取物中检测到了氯依赖性 GTP 利用蛋白激酶活性 (6)。在玉米 (7-9)、大霍 (10) 和莱茵衣藻 (11) 中检测到了将 ADP 的磷酰基转移到蛋白质上的丝氨酸和/或苏氨酸残基的蛋白激酶。
Protein kinases catalyze the transfer of phosphoryl groups from a high-energy donor to the side-chain functional groups of amino acid residues such as serine, threonine, tyrosine, aspartic acid, or histidine on proteins (1). While many protein kinases exhibit an exclusive dependence on ATP as phosphoryl donor substrate, several exceptions to this pattern have been reported. The best known and most thoroughly documented of these is casein kinase II, which can utilize either ATP or GTP as phosphoryl donor in vitro (2). The HPr kinase from Bacillus subtilis displays similar capabilities (3), and scattered reports indicate that protein kinase C may do so as well (4, 5). In addition, a chloride-dependent, GTP-utilizing protein kinase activity has been detected in extracts from human respiratory epithelium (6). Protein kinases that transfer the-phosphoryl group of ADP to serine and/or threonine residues on proteins have been detected in Zea mays (7–9), Horedeum vulgare (10), and Chlamydomonas reinhardtii (11).