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Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser 15 with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate
Author(s) -
Terada Kazutoyo,
Kai Takako,
Okuno Sachiko,
Fujisawa Hitoshi,
Izui Katsura
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80018-e
Subject(s) - phosphoenolpyruvate carboxylase , phosphorylation , biochemistry , protein kinase a , protein phosphorylation , phosphoenolpyruvate carboxykinase , c4 photosynthesis , pyruvate carboxylase , kinase , chemistry , photosynthesis , enzyme , residue (chemistry) , biology
The so‐called light‐activation of phosphoenolpyruvate carboxylase (PEPC) (EC 4.1.1.31) involved in C 4 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 Ser 15 .