D-amino acid residues as substrate specificity determinants for casein kinase II.
A set of diastereomeric peptides RRRDDDSDDD each with a corresponding D-amino acid residue successively in every position (except the arginines) was tested as substrates for casein kinase II. It was found that the D-serine containing peptide was not detectably phosphorylated. The replacements at the positions +1, -1 and +2 decreased the kII values more than 60, 30 and 20 times, respectively. The effect of the L/D replacements decreased with increased distance from the serine. The D-amino acid scan used herein seems to be a helpful complementary tool for studies of substrate specificity determinants for different protein kinases.
Toomik
R
R
Department of Medical and Physiological Chemistry, Uppsala University, Sweden.
Eller
M
M
Ekman
P
P
Ragnarsson
U
U
Engström
L
L
D000595:Amino Acid Sequence; D000818:Animals; D047390:Casein Kinase II; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D051381:Rats; D013237:Stereoisomerism; D013379:Substrate Specificity
D010455:Peptides; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases