Table 1.

Rate constants

Experiment	Rate constant
Decatenation with hydrolysis of two ATP
wt + ATP*	7.1  ±  1.4 s−1
Decatenation with no ATP hydrolysis
wt + AMPPNP†	0.2  ±  0.1 s−1
E66Q + ATP†	0.3  ±  0.1 s−1
Decatenation with hydrolysis of one ATP
E66Q/wtΔC-his + ATP†	4.3  ±  0.4 s−1
wt + ATP + vanadate†	6.6  ±  1.3 s−1
Presteady-state ATPase‡
ATP binding§	>200 s−1
Hydrolysis of first ATP	40  ±  10 s−1
Product release	4  ±  1 s−1

*Averaged from seven separate experiments. 

^†Averaged from three separate experiments. 

^‡The ATPase rate constants are from previously published data (13). 

^§The apparent first-order binding rate constant at 1 mM ATP.