. Author manuscript; available in PMC: 2014 Sep 17.

Published in final edited form as: Biochemistry. 2013 Aug 30;52(37):10.1021/bi400444y. doi: 10.1021/bi400444y

Table 3. Kinetic parameters for wild-type enzyme and mutant proteins for the full reaction with ATP varied^a.

	V_max^b (μmol min-¹mg-¹)	K_m^b (μM)	K_m (fold change)	K_cat^c (min^-1)	K_cat/K_m (μM^-1 min^-1)	K_cat/K_m (fold change)
wild-type	79 ± 3	59 ± 8	0	7,100 ± 230	120 ± 31	1
R271A	0.0011 ± 0.0001	213 ± 37	4	0.099 ± 0.005	0.0005 ± 0.0001	240,000
R271Q	0.0014 ± 0.0001	108 ± 28	2	0.13 ± 0.009	0.001 ± 0.0003	120,000
R271K^d	0.11 ± 0.006	131 ± 16	2	9.5 ± 0.5	0.074 ± 0.03	1,600
H273A	0.26 ± 0.02	175 ± 39	3	23 ± 2	0.13 ± 0.04	920
H273Q	0.003 ± 0.0001	95 ± 17	2	0.2 ± 0.008	0.002 ± 0.0005	60,000

Reported data are average of duplicates and errors are those obtained from curve fitting (equation 1) the appropriate data set.

Steady-state values were determined using the ATP coupled assay system with the concentration of AIR (fixed at K_m) and bicarbonate fixed and the concentration of ATP is varied.

Calculated using the molecular weight of the dimer.

Kinetic parameters obtained using equation 3

Table 3. Kinetic parameters for wild-type enzyme and mutant proteins for the full reaction with ATP varieda.

Table 3. Kinetic parameters for wild-type enzyme and mutant proteins for the full reaction with ATP varied^a.