. 2015 Dec 1;109(11):2371–2381. doi: 10.1016/j.bpj.2015.10.023

Table 2.

Thermodynamic parameters determined from the temperature-dependent measurements of the MT1-MMP enzymatic reaction

Parameter	kJ mol⁻¹
ΔH°(1/K_M)	−41 ± 5
ΔS°(1/K_M)	(−0.028 ± 0.003) K⁻¹
ΔG°₂₉₈(1/K_M)	−33 ± 5
E_a(k_cat)_37–55°C	30 ± 2
E_a(k_cat)_10–37°C	82 ± 2
ΔH^‡ (k_cat)	80 ± 2
ΔS^‡ (k_cat)	(0.085 ± 0.007) K⁻¹
ΔG^‡₂₉₈ (k_cat)	55 ± 4
ΔH_T^‡	42 ± 7
ΔS_T^‡	(0.06 ± 0.01) K⁻¹
ΔG_T^‡₂₉₈	22 ± 9

The binding values of the thermodynamic functions (ΔH°, ΔS°, ΔG°) were determined from the van ’t Hoff analysis of the temperature dependence of K_M. Activation values (ΔH^‡, ΔS^‡, ΔG^‡) and the apparent activation energy, E_a, were derived from the temperature dependence of k_cat and the Eyring plot. Thermodynamic quantities associated with the catalytic specificity (ΔH_T^‡, ΔS_T^‡, ΔG_T^‡) were calculated from the corresponding binding and activation parameters.