A peptide corresponding to a potential polyphosphoinositide binding site of phospholipase C‐β2 enhances its catalytic activity

FEBS Letters

Camps, Montserrat¹  Simoes, Ana Paula¹  Pipkom, Rüdiger¹  Gierschik, Peter¹  Schnabel, Petra¹ 

[1] German Cancer Research Center, Heidelberg, Germany

关键词: Phospholipase C;    Polyphosphoinositide;    Actin-binding protein;    Synthetic peptide;    Signal transduction;    Baculovirus;    InsP;    inositol monophosphate;    InsP 2;    inositol 4;    5-bis-phosphate;    IasP 3;    inositol 1;    4;    5-trisphosphate;    PLC;    phospholipase C;    PtdInsP 2;    phosphatidylinositol 4;    5-bisphosphate;    Sf9 cells;    Spodoptera frugiperda cells;   

DOI  :  10.1016/0014-5793(93)80346-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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-β₂ (PLCβ₂) 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 PLCβ₂ 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.

【 授权许可】

Unknown