Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase.

@article{Yonemoto1993IdentificationOP,
  title={Identification of phosphorylation sites in the recombinant catalytic subunit of cAMP-dependent protein kinase.},
  author={W M Yonemoto and Siv M Garrod and Sean M. Bell and Susan S. Taylor},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 25},
  pages={18626-32}
}
The catalytic subunit of cAMP-dependent protein kinase expressed in Escherichia coli is a phosphoprotein. By in vivo labeling with [32Pi]orthophosphate, the sites of phosphorylation were identified as Ser-10, Ser-139, Thr-197, and Ser-338. Two of these sites, Thr-197 and Ser-338, are found in the mammalian enzyme (Shoji, S., Titani, K., Demaille, J. G., and Fischer, E. H. (1979) J. Biol. Chem. 254, 6211-6214). The predominant isoform is phosphorylated at Ser-10, Ser-338, and Thr-197. The… CONTINUE READING