Table 1.
Phosphorylation of synthetic peptides by PKAa
| Peptide sequence | Apparent KM | Vmax |
|---|---|---|
| LRRASLG | 16 | 20.2 mmol min−1 mg−1 |
| LKRASLG | 1400 | 17.1 mmol min−1 mg−1 |
| LRKASLG | 260 | 16.9 mmol min−1 mg−1 |
| LRRASLG | 14 | 266.4 cpm/min |
| EKARLKSRPSAPWTGQ | 532 | 130.9 cpm/min |
| LDEYASKKRASTQASSQ | 993 | 42.0 cpm/min |
| RVCAKRVSTQEDEEQE | 1027 | 66.5 cpm/min |
a
The upper part of the table lists apparent KM and Vmax values for a well characterized peptide substrate (kemptide) for PKA (Kemp et al., 1977) and two derivatives. The lower part summarizes our measurements using kemptide, a peptide from myomesin (see Obermann et al., 1996) and the two peptides from M-protein described in this study. Phosphorylation reactions were carried out as described in MATERIALS AND METHODS. Peptide sequences are given in column 1.