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. Author manuscript; available in PMC: 2009 Jul 22.
Published in final edited form as: Biochemistry. 2008 Jun 26;47(29):7626–7636. doi: 10.1021/bi800162e

Table 2.

Single Turnover Kineticsa

enzyme substrate glycosylase efficiency kcat/Kd (min−1 nM−1) 95% conf intervals lyase catalytic rate kcat (min−1) 95% conf intervals
CacOgg 8-oxoG·C 0.420 0.378−0.456 0.0420 0.0378−0.0468
CacOgg 8-oxoG·A 0.384 0.276−0.576 0.0252 0.0168−1.02E+06
M132R 8-oxoG·C 1.800 1.620−2.040 0.0960 0.0900−0.1080
M132R 8-oxoG·A 0.108 0.078−0.156 0.0342 0.0252−0.0444
F179Y 8-oxoG·C 0.336 0.300−0.384 0.0234 0.0210−0.0258
F179Y 8-oxoG·A 0.027 0.018−0.033 0.0078 0.0054−0.0090
M132R/F179Y 8-oxoG·C 1.080 0.900−1.200 0.1140 0.0960−0.1380
M132R/F179Y 8-oxoG·A 0.021 0.016−0.025 0.0072 0.0048−2.64E+14
hOGG1 8-oxoG·C 0.270 0.180−0.390 0.0234 0.0174−0.0582
a

The efficiency (kcat/Kd) of the glycosylase reaction and kcat of the bifunctional reaction for CacOgg and variants with the substrates 8-oxoG·C and 8-oxoG·A were obtained under single turnover conditions (0.025 nM 8-oxoG·C and 0.25, 1, or 2.5 nM enzyme for the glycosylase reaction and 2.5, 12, or 25 nM enzyme for the bifunctional reaction). Each reaction was prepared as a 70 μL pool, and 10 μL aliquots were removed at various times and added to NaOH or formamide as described in Materials and Methods.