. 2026 May 20;7(7):1359–1371. doi: 10.1039/d6cb00090h

Table 1. Kinetic parameters for the hydrolysis of pNPB by wild-type (WT) LCC and its variants in 50 mM citrate, 100 mM phosphate (pH 8.0) at 45 °C. The k_cat and K_M values were determined with the Michaelis–Menten equation (Fig. S11).

Enzyme	k _cat (s⁻¹)	K _M (µM)	k _cat/K_M (s⁻¹ mM⁻¹)
WT	45.8 ± 1.7	48.8 ± 2.3	(9.39 ± 0.19) × 10²
V212T	51.9 ± 4.3	49.7 ± 8.0	(10.5 ± 0.85) × 10²
L102F–V212T	42.4 ± 0.4	67.7 ± 1.5	(6.27 ± 0.19) × 10²

Table 1. Kinetic parameters for the hydrolysis of pNPB by wild-type (WT) LCC and its variants in 50 mM citrate, 100 mM phosphate (pH 8.0) at 45 °C. The kcat and KM values were determined with the Michaelis–Menten equation (Fig. S11).