AMINO-ACID-SEQUENCE ROUND THE SITE OF PHOSPHORYLATION IN ISOCITRATE DEHYDROGENASE FROM ESCHERICHIA-COLI ML308
AMINO-ACID-SEQUENCE ROUND THE SITE OF PHOSPHORYLATION IN ISOCITRATE DEHYDROGENASE FROM ESCHERICHIA-COLI ML308
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DOI：
10.1016/0014-5793(84)81087-x
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发表时间：
1984-01-01
期刊：
影响因子：
3.5
通讯作者：
NIMMO, HG
中科院分区：
文献类型：
--
作者：
BORTHWICK, AC;HOLMS, WH;NIMMO, HG
来自大肠杆菌的异柠檬酸脱氢酶受可逆磷酸化机制调节。我们在此报告磷酸化位点周围的氨基酸序列；这是第一个报道的细菌蛋白激酶序列。该序列与环 AMP 依赖性蛋白激酶磷酸化的序列不同。
Isocitrate dehydrogenase fromEscherichia coliis regulated by a reversible phosphorylation mechanism. We report here the amino acid sequence round the phosphorylation site; this is the first such sequence to be reported for a bacterial protein kinase. The sequence does not resemble sequences phosphorylated by cyclic AMP-dependent protein kinase.