MAIZE LEAF PHOSPHOENOLPYRUVATE CARBOXYLASE - PHOSPHORYLATION OF SER15 WITH A MAMMALIAN CYCLIC AMP-DEPENDENT PROTEIN-KINASE DIMINISHES SENSITIVITY TO INHIBITION BY MALATE

被引：59

作者：

TERADA, K

KAI, T

OKUNO, S

FUJISAWA, H

IZUI, K

机构：

[1] KYOTO UNIV,FAC SCI,DEPT CHEM,KYOTO 606,JAPAN

[2] ASAHIKAWA MED COLL,DEPT BIOCHEM,ASAHIKAWA 078,JAPAN

来源：

FEBS LETTERS | 1990年 / 259卷 / 02期

关键词：

(Maize); C[!sub]4[!/sub] photosynthesis; Cyclic AMP-dependent protein kinase; Malate sensitivity; Phosphoenolpyruvate carboxylase; Phosphorylation;

D O I：

10.1016/0014-5793(90)80018-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. © 1990.

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页码：241 / 244

页数：4

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