Feramisco, J. R., Krebs, E. G. (1978) Inhibition of Cyclic Amp Dependent Protein Kinase Ec-2.7.1.37 by Analogs of a Synthetic Peptide Substrate. Journal of Biological Chemistry, 253 (24). pp. 8968-8971.
Abstract
Analogs of the synthetic substrate Leu-Arg-Arg-Ala-Ser-Leu-Gly in which the serine is replaced by other amino acids inhibited the activity of the catalytic subunit of cyclic AMP-dependent protein kinase [EC 2.7.1.37] from beef skeletal muscle (Peak I). All of the analogs were competitive with respect to peptide substrate but apparent Ki values varied depending on the particular amino acid that was substituted for serine. Inhibition was also competitive with respect to mixed histone as determined in experiments utilizing one of the analogs. Acetylation of the terminal amino group of Leu-Arg-Arg-Ala-Ser-Leu-Gly lowered the Km for this substrate from 16 .mu.M to 3 .mu.M, but a similar modification of the inhibitory analog Leu-Arg-Arg-Ala-Ala-Leu-Gly resulted in no major change in the Ki value. An amount of inhibitory peptide sufficient to inhibit the cyclic AMP-dependent protein kinase by 90% caused less than 10% inhibition of several cyclic AMP-independent protein kinases indicating a high degree of specificity of inhibition by the peptide analogs. Synthetic peptide analogs could be useful in identifying phosphorylation reactions catalyzed by cyclic AMP-dependent protein kinase as distinguished from other protein kinase reactions.
| Item Type: | Paper |
|---|---|
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor > Cyclic AMP |
| CSHL Authors: | |
| Communities: | CSHL labs |
| Depositing User: | Matt Covey |
| Date: | 1978 |
| Date Deposited: | 13 Dec 2016 17:30 |
| Last Modified: | 13 Dec 2016 17:30 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/33305 |
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