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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

Figure 4.

Figure 4

Opposite base specificity of the glycosylase and bifunctional activity in hOGG1, CacOgg, and variants. The glycosylase activity is indicated by closed symbols and solid lines, and bifunctional activity is indicated by open symbols and dashed lines. The substrate is 8-oxoG opposite C (■, □), A (▲, △), T (▼, ▽), and G (◆, ◇). (A) hOGG1. (B) CacOgg. (C) M132R. (D) F179Y. (E) M132R/F179Y. Each reaction was prepared as a 150 μL pool, and 10 μL aliquots were removed at t minutes and added to NaOH or formamide as described in Materials and Methods. Substrate (5 nM) was in excess of enzyme (CacOgg, 1 nM; hOGG1, 1.67 nM). A representative experiment is shown.