生物化学
蛋白激酶C
亮氨酸拉链
自磷酸化
蛋白质水解
蛋白激酶A
细胞周期蛋白依赖激酶9
分子生物学
花生四烯酸
氨基酸
生物
化学
肽序列
激酶
丝裂原活化蛋白激酶激酶
酶
基因
作者
Hideyuki Mukai,Michinori Kitagawa,Hideki Shibata,Hiromi Takanaga,Kotaro Mori,Mutsumi SHIMAKAWA,Masako Miyahara,Koichi Hirao,Yoshitaka Ono
标识
DOI:10.1006/bbrc.1994.2466
摘要
PKN, a novel protein kinase with catalytic domain homologous to PKC family and unique amino terminal leucine zipper-like sequences, was purified partially from COS7 cells transfected with the cDNA construct encoding human PKN for enzymatic characterization of the enzyme. Using serine containing synthetic peptides based on PKC pseudosubstrate sites as the phosphate acceptors, kinase activities estimated from partially purified PKN were not stimulated by Ca2+/phosphatidylserine/diolein but were activated several-fold to several tens-fold by 40 μM unsaturated fatty acids, such as arachidonic acid, linoleic acid, and oleic acid. Autophosphorylation of the immunoprecipitates using anti-PKN antiserum was also stimulated by various unsaturated fatty acids. Limited proteolysis of PKN with trypsin induced an enhancement of the peptide kinase activity that was almost independent of arachidonic acid.
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