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. Author manuscript; available in PMC: 2016 May 9.
Published in final edited form as: Methods Enzymol. 2015 Jun 2;560:91–116. doi: 10.1016/bs.mie.2015.04.012

Figure 2.

Figure 2

Pre-steady-state kinetics of m1G37-tRNA synthesis. (A) Monitoring the time course of synthesis upon mixing EcTrmD (1 µM) with EctRNALeu (10 µM) and AdoMet (30 µM) at 37 °C. The time-dependent synthesis is calculated as the amount of synthesis per active site of the enzyme (%) and is fit to equation 1 to determine the slope (a = slope and b = 0). (B) Monitoring the time course of synthesis upon mixing MjTrm5 (1 µM), MjtRNACys (10 µM), and AdoMet (25 µM). The time-dependent synthesis is calculated as the amount of synthesis per active site of the enzyme (%) and is fit to equation 3 to determine kchem and kcat. This figure is adapted from Figure 1 in (Christian et al., 2010b).