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. Author manuscript; available in PMC: 2008 May 2.
Published in final edited form as: J Mol Biol. 2007 Aug 14;373(4):851–865. doi: 10.1016/j.jmb.2007.07.067

Table 1.

Nucleotide Binding and Hydrolysis by Full-Length gpA, gpA-ΔN179 and gpA-ΔN179,K497D

Nucleotide gpA-FL gpA-ΔN179 gpA-ΔN179,K497D
aATP KD,app= 0.8 ± 0.1 mM KD,app= 1.7 ± 0.6 mM KD,app= 2.5 ± 0.6 mM
aADP KD,app= 1.2 ± 0.2 mM KD,app= 63 ± 10 μM KD,app= 192 ± 26 μM
AMP bN.C. bN.C. bN.C.
Single-Turnover
ATPase Activity
ck1= 0.706 ± 0.089 min−1
k2= 0.017 ± 0.025 min−1
dkobs= 0.086 ± 0.008 min−1 dkobs= 0.0072 ± 0.0004 min−1
a

The fluorescence-monitored titration data presented in Figure 3 were quantified as described in Materials and Methods.

b

No Change.

c

Data taken from42.

d

The kinetic data presented in Figure 4C were quantified as described in Materials and Methods.