Skip to main content
. 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 1.

Multiple Turnover Kinetics for CacOgga

glycosylase
 lyase
Km (nM) kcat (min−1) efficiency Km (nM) kcat (min−1) efficiency
24 (8, 39) 31.2 (2.04, inf) 1.32 (1.02, 1.74) 1.2 (0.93, 1.6) 0.0462 (0.045, 0.048) 0.0372 (0.0306, 0.0558)
a

Enzyme = 1 nM, substrate = 5−20 nM. Kinetics were modeled from time course data using each 8-oxoG·C and AP·C as substrates. 95% confidence intervals are listed in parentheses.