Functional properties of myosin 5a constructsa.

aSolution kinetic data are for m5aS1 and motility data are for m5aHMM. Nomenclature of kinetic constants refers to Fig. 1B. All parameters were measured at 25°C. Mean ± SD values for two to four independent experiments are shown.bAt 1 mM ATP.cHalf-saturating actin concentration (at 1 mM ATP).dHalf-saturating ATP concentration (at 10 µM actin).eAt 1 mM ATP.fResults of exponential analysis are shown (Fig. 2; rapid phase data for I67K-m5aS1). See also Fig. S1 for global fitting results on I67K-m5aS1.gLower bounds set by maximal rate constant of rapid pre-steady state burst at 30 µM ATP.hFrom steady-state slopes recorded at 100 µM ATP.iLower bounds set by maximal rate constant of rapid pre-steady state burst at 10 µM actin.jMaximal amplitude of rapid pre-steady state burst at 10 µM actin.kRate constants of the rapid (40±3% amplitude) and slow phases of biphasic mdADP release.lFrom ref. [17].