A Ca2+‐dependent protein kinase phosphorylates phosphoenolpyruvate carboxylase in maize

FEBS Letters

Ogawa, Noriyuki¹  Okumura, Satoru¹  Izui, Katsura¹ 

[1] Department of Chemistry, Faculty of Science, Kyoto University, Kyoto 606-01, Japan

关键词: Phosphoenolpyruvate carboxylase;    C4 photosynthesis;    Phosphorylation;    Protein kinase inhibitor;    Ca2+-dependent protein kinase;    Maize;    PEPC;    phosphoenolpyruvate carboxylase;    PK;    protein kinase;    A-kinase;    cyclic AMP-dependent protein kinase;    MLCK;    myosin light chain kinase;    IC50;    concentration required for 50% inhibition;   

DOI  :  10.1016/0014-5793(92)80291-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In C₄ plants the activity of phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is regulated by phosphorylation/dephosphorylation which is mediated by light/dark signals. The study using protein kinase inhibitors showed that the inhibition pattern of maize PEPC-protein kinase (PEPC-PK) is similar to that of myosin light chain kinase, a Ca²⁺-calmodulin-dependent PK. The kinase activity was also inhibited by EGTA and the inhibition was relieved by Ca²⁺. These results suggest that PEPC-PK is Ca²⁺-dependent in contrast with previous observations by other research groups.

【 授权许可】

Unknown