Functional properties of myosin 5a constructs^a.

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].