Peptide fragments of myelin basic protein as substrates of protein kinase C.
A set of peptides derived from myelin basic protein was synthesized and the kinetics of their phosphorylation by protein kinase C was studied. The replacement or the removal of the N-terminal Gln had no effect on the activity of the parent peptide. The removal of the following Lys or Arg led to a systematic decrease in substrate activity. The modifications in the C-terminal part of the peptide had a weaker influence on the parameters Vmax and KM than those in the N-terminal. The rather regular dependence of the activity of substrates upon their structure does not allow the strict definition of a minimum substrate for protein kinase C.
Eller
M
M
Department of Biochemistry, Uppsala University, Sweden.
Järv
J
J
Toomik
R
R
Ragnarsson
U
U
Ekman
P
P
Engström
L
L
D000595:Amino Acid Sequence; D007700:Kinetics; D008969:Molecular Sequence Data; D004676:Myelin Basic Protein / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000737:chemistry / Q000378:metabolism*; D011761:Pyrrolidonecarboxylic Acid / Q000737:chemistry; D013379:Substrate Specificity
D004676:Myelin Basic Protein; D010446:Peptide Fragments; D011493:Protein Kinase C; D011761:Pyrrolidonecarboxylic Acid