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. Author manuscript; available in PMC: 2014 Jan 1.
Published in final edited form as: Arch Biochem Biophys. 2012 Oct 27;529(1):11–17. doi: 10.1016/j.abb.2012.10.010

Table 3.

Maximal values of rate constants for the hydration of CO2 and dehydration of bicarbonate catalyzed by variants of cam, and related kinetic pKa values.a

Variant kcatexch/KeffCO2
(µM−1 s−1)
pKa b kB
(ms−1)
pKZnH2O c pK donor c
Wild-type 14 ± 1 5.7, 8.1 65 ± 7 6.0 8.6
W19N 1.2 ± 0.1 5.3, 8.4 4.9 ± 0.5 5.7 7.8
W19F 0.9 ± 0.1 5.7, 8.2 13 ± 4 6.0 7.2
Y200A 4.0 ± 0.4 5.2, 7.8 30 ± 3 5.7 8.3
Y200F 3.7 ± 0.4 5.6, 8.1 150 ± 60 6.5 6.8
a

Obtained from 18O exchange data under the conditions of Figure 7 by published procedures (1719).

b

The standard errors are 0.3 pK units or less. These data were obtained from values of kcatexch/KeffCO2 using a fit to the following: (k/K)obs = (k/K)1/(1 + 10pK1-pH) + (k/K)2/(1 + 10pK2-pH).

c

The standard errors are 0.3 pK units or less. These data were obtained from values of the rate constant for release of 18O-labeled water from the enzyme RH2O/[E] using a fit to the following: RH2O/[E] = kB / ([1 + (Ka)His64 /[H+]][1 + [H+]/(Ka)ZnH2O]).