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. 1999 Jun 8;96(12):6666–6671. doi: 10.1073/pnas.96.12.6666

Table 1.

Effect on ATPase activities of dephosphorylated and phosphorylated myosins

Actin-activated ATPase
Myosin ATPase
Dephosphorylated myosin
Phosphorylated myosin
Dephosphorylated myosin
Vmax (-fold) Km (μM) Vmax (-fold) Km (μM) Vmax (-fold) Km (μM)
Native MLCK 4.31 ± 0.89 (6) 1.14 ± 0.26 (6) Inhibition  (refs. 31, 40) () 3.85 (1) 0.59 (1)
777D/972E fragment 7.36 ± 0.44 (4) 1.06 ± 0.20 (4) No stimulation (2) No stimulation (2) 3.70 (1) 0.67 (1)
816M/972E fragment No stimulation (2) No stimulation (2) NT NT NT NT
native Telokin No stimulation (2) No stimulation (2) NT NT NT NT
777D/815S peptide 3.03 ± 0.22 (3) 6.93 ± 1.61 (3) No stimulation (1) No stimulation (1) 3.45, 2.70 (2) 9.70, 3.17 (2)
777D/795M peptide No stimulation (6) No stimulation (6) No stimulation (2) No stimulation (2) No stimulation (1) No stimulation (1)
796A/815S peptide 3.24 ± 0.48 (5) 20.0 ± 0.96 (5) NT NT NT NT
787S/815S peptide 2.68 ± 0.68 (3) 15.4 ± 4.57 (3) NT NT NT NT
7776A/834S peptide 1.47, 2.94 14.7, 37.0 NT NT NT NT
1M/41P peptide No stimulation (2) No stimulation (2) NT NT NT NT

The numbers in parentheses refer to the number of experiments. NT, not tested; No stimulation, relative ATPase activities were plotted against the protein (0–5 μM) and peptide (0–0.3 mM) concentrations. When they were within 0.95–1.19-fold for the proteins and 0.90–1.50-fold for the peptides, it was considered no stimulation. ∗, half-maximal inhibition was observed at 0.15–0.20 μM, as described in refs. 31 and 40