Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3 like kinase).
Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3 like kinase).
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ATP-柠檬酸裂解酶和磷酸酶抑制剂 2 上被多功能蛋白激酶（糖原合酶激酶 3 样激酶）磷酸化的位点序列。
DOI：
10.1021/bi00485a011
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发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Benjamin,WB
中科院分区：
文献类型：
--
作者：
Ramakrishna,S;D'Angelo,G;Benjamin,WB
摘要：多功能蛋白激酶（MFPK）磷酸化ATP-柠檬酸裂解酶的两个位点，Bt和Bs，分别在苏氨酸和丝氨酸上的肽B上，抑制剂2在苏氨酰残基上，糖原合成酶在位点2和3上。ATP-柠檬酸裂解酶的磷酸化位点BT和Bs依赖于位点A的预先磷酸化，而位点A的磷酸化被位点BT和Bs的预先磷酸化所降低。为了研究MFPK的识别位点和位点-位点相互作用，
Revised Manuscript Received May 15, 1990 abstract: Multifunctional protein kinase (MFPK) phosphorylates ATP-citrate lyase on peptide B on two sites, Bt and Bs, on threonine and serine, respectively, inhibitor 2 on a threonyl residue, and glycogen synthase at sites 2 and 3. The phosphorylation sites BT and Bs of ATP-citrate lyase are dependent on prior phos-phorylation at site A whereas site A phosphorylation is decreased by prior phosphorylationat sitesBT and Bs. To study the MFPK recognition sites and the site-site interactions, the amino acid sequences of