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. Author manuscript; available in PMC: 2018 Apr 26.
Published in final edited form as: Methods Enzymol. 2017 Apr 26;592:357–376. doi: 10.1016/bs.mie.2017.03.016

Fig. 5.

Fig. 5

Enhancement of TDG steady-state turnover by APE1. (A) Single-turnover experiments, performed with 1.0 μM TDG and 0.3μM G·caC substrate, yield a rate constant of kobs = 0.50 ±0.02 min−1, reflecting the maximal rate of product formation (kmax). (B) Multiple-turnover experiments performed with 0.05 μM TDG and 1.0 μM G·caC substrate give a slow steady-state rate constant of kcat = 0.011 ±0.002 min−1 in the absence of APE1 (blue line, circles). Steady-state turnover is much (32-fold) higher for TDG in the presence of 1.2 μM APE1, kcat+APE1=0.35±0.04min-1 (triangles), and approaches the theoretical maximum ( kcat+APE1=0.7kmax).