Table 2.
Steady-state ATP hydrolysis rates of RLC-TS and RLC mutants.
|
RLC |
kbasal (s−1) |
s.d. |
k100 (s−1) |
s.d. |
|---|---|---|---|---|
RLC-TS |
0.013 |
0.007 |
0.12 |
0.03 |
|
RLC-TS |
0.010 |
0.001 |
0.82 |
0.01 |
RLC-AS |
0.024 |
0.005 |
0.15 |
0.02 |
|
RLC-AS |
0.024 |
0.008 |
0.81 |
0.04 |
RLC-TA |
0.009 |
0.002 |
0.12 |
0.01 |
|
RLC-TA |
0.008 |
0.002 |
0.37 |
0.01 |
RLC-AA |
0.014 |
0.006 |
0.16 |
0.03 |
|
RLC-AA |
0.012 |
0.002 |
0.23 |
0.02 |
RLC-AE |
0.010 |
0.002 |
0.21 |
0.03 |
|
RLC-AE |
0.009 |
0.002 |
0.23 |
0.01 |
RLC-EE |
0.011 |
0.007 |
0.19 |
0.01 |
|
RLC-EE |
0.010 |
0.002 |
0.22 |
0.01 |
The actin-activated ATPase activity was measured at 25°C, as described under ‘Materials and methods’. Treatment of RLC with MLCK is indicated by bold print. For comparison, kbasal the steady-state ATPase activity in the absence of actin filaments, and k100, the steady-state ATPase activity at 100 µM actin filaments, are listed.