Table 1 Kinetic constants for proteolysis of VWF96 and VWF96 variants by ADAMTS13

Substrate	k_cat/K_m ± SEM^a (×10⁴ M⁻¹ s⁻¹)	Fold decrease^a (↓)	k_cat ± SEM^b (s⁻¹)	Fold difference^b (↑/↓)	K_m ± SEM^b (μM)	Fold increase^b (↑)	k_cat/K_m ± SEM^b (×10⁴ M⁻¹ s⁻¹)	Fold decrease^b (↓)
VWF96	110.7 ± 2.28	–	5.65 ± 0.16	–	3.99 ± 0.41	–	141.6 ± 15.22	–
VWF87(ΔSpacer)	7.51 ± 0.39	14.7↓	3.97 ± 0.25	1.42↓	46.1 ± 7.45	11.6↑	8.60 ± 1.49	16.5↓
VWF96-Spacer	13.1 ± 0.56	8.45↓	4.11 ± 0.28	1.37↓	32.7 ± 6.23	8.20↑	12.6 ± 2.55	11.2↓
VWF96-Cys	7.11 ± 0.26	15.6↓	8.31 ± 0.53	1.47↑	123.4 ± 14.0	30.9↑	6.73 ± 0.92	21.0↓
VWF96-Dis	0.21 ± 0.01	527↓	0.101 ± 0.006	55.9↓	56.4 ± 10.2	14.1↑	0.18 ± 0.03	787↓
VWF96-MP	0.80 ± 0.03	138↓	0.086 ± 0.006	66.0↓	13.3 ± 2.79	3.33↑	0.65 ± 0.14	218↓

The catalytic efficiency (k_cat/K_m) of proteolysis for each VWF96 variant was derived from time-course assays (a) that monitored proteolysis of each variant over time (Fig. 2a–f). The fold decrease in proteolysis for each VWF96 variant is shown relative to VWF96—downward arrow denotes decreases; upward arrow denotes increases. From the Michaelis–Menten kinetics (b) monitoring the initial rate of proteolysis as a function of substrate concentration (Fig. 2g–l), the individual constants, k_cat and K_m, were derived and the independent derivation of the k_cat/K_m. Fold changes for each constant relative to VWF96 are shown. Raw data underlying all reported averages are provided in the Source Data file corresponding to the data from Fig. 2a–l
VWF Von Willebrand factor, MP metalloprotease, Dis disintegrin-like, Cys cysteine-rich
^aData derived from time-course assays
^bData derived from Michaelis–Menten kinetics

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