Maize leaf phosphoenolpyruvate carboxylase: phosphorylation of Ser15 with a mammalian cyclic AMP‐dependent protein kinase diminishes sensitivity to inhibition by malate
- 1 January 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 259 (2) , 241-244
- https://doi.org/10.1016/0014-5793(90)80018-e
Abstract
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.Keywords
This publication has 15 references indexed in Scilit:
- Regulatory seryl-phosphorylation of C4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leavesArchives of Biochemistry and Biophysics, 1989
- Light/dark regulation of maize leaf phosphoenolpyruvate carboxylase by in vivo phosphorylationArchives of Biochemistry and Biophysics, 1988
- Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivoFEBS Letters, 1988
- Changes in the kinetic properties and phosphorylation state of phosphoenolpyruvate carboxylase in Zea mays leaves in reponse to light and darkFEBS Letters, 1987
- Sequence analysis of phosphoserine‐containing peptidesFEBS Letters, 1986
- Changes in Sensitivity to Effectors of Maize Leaf Phosphoenolypyruvate Carboxylase during Light/Dark TransitionsPlant Physiology, 1986
- Cloning and sequence analysis of cDNA encoding active phosphoenolpyruvate carboxylase of the C4-pathway from maizeNucleic Acids Research, 1986
- Rapid analysis of amino acids using pre-column derivatizationJournal of Chromatography B: Biomedical Sciences and Applications, 1984
- Transforming gene product of Rous sarcoma virus phosphorylates tyrosineProceedings of the National Academy of Sciences, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976