J. Biochem, 1993, Vol. 114, No. 2 177-180
© 1993 Japanese Biochemical Society
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Substrate Specificity of Protein Kinase C Studied with Peptides Containing D-Amino Acid Residues1
*Laboratory of Bioorganic Chemistry, Tartu University EE2400 Tartu, Estonia;
**Department of Biochemistry, Uppsala University S-751 23 Uppsala, Sweden
***Department of Medical and Physiological Chemistry, Uppsala University S-751 23 Uppsala, Sweden
A set of stereoisomeric nonapeptides KRPSQRAKY with one, two, or all L-ami no acid residues replaced by the corresponding D-ami no acids, and two analogs with L- and D-threonine instead of serine, were synthesized and tested as substrates for protein kinase C. All of the peptides were phosphorylated by the enzyme. The maximal rate of the reaction with the all-D peptide was more than one order of magnitude lower than that for the all-L peptide with serine. The same applied to the peptides with D-Ser or with D-Arg in position + 2 with respect to Ser. The.Km values for the peptides containing one D-amino acid were close to that for the prototype peptide (53 /µM). On the other hand, when two or more D-amino acids were present, the Km value increased considerably. Replacement of serine by threonine also reduced the phosphorylation rate and increased the Km values. One can conclude that the stereospecificity of protein kinase C is much less pronounced than that of protein kinase A, which is in agreement with the less clearly pronounced substrate specificity of the former enzyme.
1This work was supported by grants from the Swedish Natural Science Research Council (3020–319) and the Swedish Medical Research Council (13X-50). M.E. also acknowledges a scholarship from the Swedish Institute and R.T. one from the Procordia Biotechnology Foundation.
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