Simões A P, Schnabel P, Pipkorn R, Camps M, Gierschik P
German Cancer Research Center, Heidelberg.
FEBS Lett. 1993 Oct 4;331(3):248-51. doi: 10.1016/0014-5793(93)80346-v.
A peptide corresponding to a basic consensus amino acid motif present in both actin-binding proteins and phosphoinositide-specific phospholipases C was synthesized and its effect on the activity of a recombinant phospholipase C-beta 2 (PLC beta 2) expressed in baculovirus-infected insect cells was studied. The peptide markedly and specifically stimulated the activity of the enzyme. This stimulatory effect required a particular primary and/or secondary structure of the peptide and occurred without lowering the affinity of the enzyme for Ca2+. The function of the PLC beta 2 segment corresponding to the peptide might be to bind and offer the substrate to the catalytic domain of this enzyme in a more favorable configuration or, alternatively, to interact with a hypothetical inhibitory constraint.
合成了一种与肌动蛋白结合蛋白和磷酸肌醇特异性磷脂酶C中存在的碱性共有氨基酸基序相对应的肽，并研究了其对在杆状病毒感染的昆虫细胞中表达的重组磷脂酶C-β2（PLCβ2）活性的影响。该肽显著且特异性地刺激了该酶的活性。这种刺激作用需要该肽具有特定的一级和/或二级结构，并且在不降低该酶对Ca2+亲和力的情况下发生。与该肽相对应的PLCβ2片段的功能可能是以更有利的构型结合并将底物提供给该酶的催化结构域，或者与一种假设的抑制性限制相互作用。
