. 2014 Jun 23;136(28):10156–10165. doi: 10.1021/ja505037v

Table 3. Effect of Mutations on the Activation Barrier (ΔG^⧧)_OMP for Decarboxylation of OMP Catalyzed by Wild-Type OMPDC, and by Previously Mutated OMPDC^a.

	(ΔΔG_X^∓)_OMP (kcal/mol)^b
mutated OMPDC	Q215A	Y217F	R235A	∑(ΔΔG_X^∓)_OMP^c
wild type	2.2	2.4	5.6	10.2
single mutant^d	2.5 (R235A)	2.5 (Q215A)	5.8 (Q215A)	10.8
	2.3 (Y217F)	3.2 (R235A)	6.3 (Y217F)	11.8
double mutant	2.8	3.5	6.8	13.4

For OMPDC-catalyzed decarboxylation at 25 °C, pH 7.1 (30 mM MOPS), and ionic strength of 0.105 (NaCl).

The effect of the point mutation on (ΔG^⧧)_OMP for decarboxylation of OMP catalyzed by the precursor enzyme, calculated from the ratio of values of k_cat/K_m for the precursor and mutant enzymes.

The sum of the effects of the Q215A, Y217F, and R235A mutations on (ΔΔG_X^∓)_OMP.

The enzyme that was mutated is given in parentheses.

Table 3. Effect of Mutations on the Activation Barrier (ΔG⧧)OMP for Decarboxylation of OMP Catalyzed by Wild-Type OMPDC, and by Previously Mutated OMPDCa.

Table 3. Effect of Mutations on the Activation Barrier (ΔG^⧧)_OMP for Decarboxylation of OMP Catalyzed by Wild-Type OMPDC, and by Previously Mutated OMPDC^a.