Peptide phosphorylation by calcium-dependent protein kinase from maize seedlings.

@article{Loog2000PeptidePB,
  title={Peptide phosphorylation by calcium-dependent protein kinase from maize seedlings.},
  author={Mart Loog and Reet Toomik and Katrin Sak and Grażyna Muszyńska and Jaak J{\"a}rv and Pia Ek},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 2},
  pages={337-43}
}
Ca2+-dependent protein kinase (CDPK-1) was purified from maize seedlings, and its substrate specificity studied using a set of synthetic peptides derived from the phosphorylatable sequence RVLSRLHS15VRER of maize sucrose synthase 2. The decapeptide LARLHSVRER was found to be efficiently phosphorylated as a minimal substrate. The same set of peptides were found to be phosphorylated by mammalian protein kinase Cbeta (PKC), but showed low reactivity with protein kinase A (PKA). Proceeding from the… CONTINUE READING