Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser15 with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate

FEBS Letters

Izui, Katsura²  Fujisawa, Hitoshi¹  Okuno, Sachiko¹  Terada, Kazutoyo²  Kai, Takako² 

[1] Department of Biochemistry, Asahikawa Medical College, Asahikawa 078, Japan;Department of Chemistry, Faculty of Science, Kyoto University, Kyoto 606, Japan

关键词: Phosphoenolpyruvate carboxylase;    C4 photosynthesis;    Phosphorylation;    Cyclic AMP-dependent protein kinase;    Malate sensitivity;    (Maize);    A-kinase;    cyclic AMP-dependent protein kinase;    API;    Achromobacter protease I;    Hepes;    N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid;    HPLC;    high performance liquid chromatography;    Mes;    2-(N-morpholino)ethanesulfonic acid;    PEPC;    phosphoenolpyruvate carboxylase;    PTH;    phenylthiohydantoin;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(90)80018-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The so-called light-activation of phosphoenolpyruvate carboxylase (PEPC) (EC 4.1.1.31) involved in C₄ photosynthesis is known to be mediated by phosphorylation. A cyclic AMP-dependent protein kinase from bovine heart was found to be able to phosphorylate PEPC. The phosphorylation was accompanied by the changes in kinetic properties, which were very similar to the reported light activation. The phosphorylated amino acid residue was identified as Ser and the position of this Ser on the primary structure [(1988) FEBS Lett. 229, 107-110] was determined to be Ser¹⁵.

【 授权许可】

Unknown