These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase.
    Author: Alessi DR, Caudwell FB, Andjelkovic M, Hemmings BA, Cohen P.
    Journal: FEBS Lett; 1996 Dec 16; 399(3):333-8. PubMed ID: 8985174.
    Abstract:
    The substrate specificity of protein kinase-B alpha (PKBalpha, also known as RAC kinase or Akt) was investigated using synthetic peptide substrates related to the sequence surrounding the phosphorylation site on glycogen synthase kinase-3 (GSK3). The minimum sequence motif required for efficient phosphorylation was Arg-Xaa-Arg-Yaa-Zaa-Ser/Thr-Hyd, where Xaa is any amino acid, Yaa and Zaa are small residues other than glycine and Hyd is a bulky hydrophobic residue (Phe, Leu). The most effective substrate, Arg-Pro-Arg-Thr-Ser-Ser-Phe, was phosphorylated with a Km of 5 microM and Vmax of 260 U/mg. PKBalpha phosphorylated histone H2B (Km 5 microM, Vmax 68 U/mg) specifically at Ser-36 which also lies in an Arg-Xaa-Arg-Xaa-Xaa-Ser-Hyd motif. The peptide Arg-Pro-Arg-Ala-Ala-Thr-Phe may be a relatively specific substrate for PKBalpha because, unlike other substrates, it is not phosphorylated by p70 S6 kinase or MAP kinase activated protein (MAPKAP) kinase-1.
    [Abstract] [Full Text] [Related] [New Search]