Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum
Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum
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DOI：
10.1016/0166-6851(96)02643-6
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发表时间：
1996-07-01
影响因子：
1.5
通讯作者：
Kappes, B
中科院分区：
文献类型：
--
作者：
Graeser, R;Franklin, RM;Kappes, B
The kinase activity of PfPK5 (Plasmodium falciparumprotein kinase 5) was stimulated 5- to 10-fold by the replacement of Thr158with glutamic acid (negatively charged amino acids introduced at the position of a phosphorylatable residue can mimic phosphorylation). Thus, a phosphorylation of PfPK5 on Thr158would activate the native enzyme, indicating that the kinase may be regulatedin vivoby reversible phosphorylation of the same site as other cyclin-dependent kinases. Substitution of Thr158by valine, and replacement of Lys32by arginine produced catalytically inactive mutants. Both the wild type PfPK5 and the PfPK5E158mutant (with Thr158replaced by glutamic acid) incorporated [32P] linearly in a time-dependent manner, indicating that the enzyme autophosphorylates. Both PfPK5wtand PfPK5E158autophosphorylated on a threonine residue, but neither Thr14nor Thr158were autophosphorylated.
