Table 1.

Kinetic Parameters for Wild Type and Variant OMPDC-Catalyzed Decarboxylation of OMP and EO at 25 °C.

Enzyme	OMPa		EOb		EO + HPib
	kcat/Km (M−1 s−1)c	ΔΔG‡ (kcal/mol)d	(kcat/Km)E (M−1 s−1)	ΔΔG‡ (kcal/mol)d	(kcat/Km)E•HPi/Kd (M−2 s−1)	ΔΔG‡ (kcal/mol)d
WT	1.1 × 107		0.026e		1.2 × 104 e
D37G	3.2 × 105	2.1	(2.7 ± 0.1) × 10−3 f	1.4	290 g	2.2
T100’A	2.1 × 105	2.3	(2.3 ± 0.1) × 10−3 f	1.4	85 g	2.9

^aAt pH 7.1 (30 mM MOPS) and I = 0.105 (NaCl).

^bRate constant defined in Scheme 2.

^cPublished kinetic parameters.¹⁴

^dThe effect of the side chain substitution on the activation barrier for the reaction catalyzed by wild type OMPDC.

^ePublished kinetic parameter.¹⁸

^fAverage of two determinations at pH 7.0 (25 mM MOPS) and I = 0.14 (NaCl).

^gDetermined from the fit of data shown in Figure 2 to eq 2.