Table I. Thermodynamic Parameters of Interaction Derived from ITC and Spectral Titrations.
| Enzyme | ΔH (kcal/mol) |
ΔS (cal/mol/K) |
ΔG (kcal/mol) |
N (unitless) |
KD1 (10−6 M) |
Ks (10−6 M) |
ΔFh (%) |
|---|---|---|---|---|---|---|---|
| 2A62 | −3.8 (2.3)4 | 18.2 (7.3) | −9.3 (0.2) | 1.0 (0.0) | 0.17 (0.05) | 34.20 (7.21) | 78.5 (2.1) |
| 2B62 | −13.1 (2.3) | −12.1 (9.4) | −9.4 (1.0) | 0.9 (0.2) | 0.22 (0.17) | 0.38 (0.23) | 49.3 (11.0) |
| 2B63 | −6.3 (2.2) | 3.2 (2.3) | −7.5 (1.4) | 1.2 (0.3) | 1.82 (0.61) | 1.60 (0.14)* | 42.5 (3.4) |
1
KA−1 from ITC
2
(+)-α-pinene
3
(+)-3-carene
4
Values represent mean of at least three unique experiments. The standard deviation is displayed in parentheses.
*
Measured using the Hill equation giving the S50 with n=2.