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. 2012 May 9;287(28):23840–23849. doi: 10.1074/jbc.M112.362111

TABLE 2.

Single turnover misincorporation opposite template A

Kinetic constants obtained from single turnover misincorporation experiments are listed for each enzyme (± S.E. of the fit).

dNTP Enzyme kpol Kd kpolc/kpolia Kdi/Kdca Efficiencyb Fold changec
s1 μm μm1 s1
dTTP WT 46 ± 2 35 ± 5 1.3 55
G231D 13.1 ± 0.9 550 ± 70 2.4 × 10−2
dATP WT 0.025 ± 0.001 57 ± 10 1800 1.6 4.4 × 10−4 58
G231D 0.00250 ± 0.00007 330 ± 30 5200 0.60 7.6 × 10−6
dCTP WT 0.079 ± 0.004 280 ± 40 580 8.0 2.8 × 10−4 110
G231D 0.0016 ± 0.0002 610 ± 110 8200 1.1 2.6 × 10−6
dGTP WT 0.031 ± 0.002 84 ± 18 1500 2.4 3.7 × 10−4 93
G231D 0.00119 ± 0.00007 300 ± 50 11,000 0.55 4.0 × 10−6

a Subscript c denotes correct nucleotide; subscript i denotes incorrect nucleotide.

b Efficiency was calculated by dividing kpol by Kd for each condition.

c Fold change in efficiency (WT/G231D) is shown.