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. Author manuscript; available in PMC: 2010 Jun 9.
Published in final edited form as: Biochemistry. 2009 Jun 9;48(22):4808–4815. doi: 10.1021/bi900172q

Figure 3. Time Course of M. tb Catalysis.

Figure 3

The conversion of NADH to NAD+ by native M. tb PGDH is monitored under conditions where substrate is depleted. Two mixing protocols where performed on a stopped flow instrument. The data are represented by symbols and the simulation to Scheme 2 is represented by a solid line. For clarity, not every data point is shown. 1) Enzyme (2.5 μM) was rapidly mixed with HPAP (1000 μM) and NADH (350 μM), Ο; 2) Enzyme (2.5 μM) and NADH (175 μM) were rapidly mixed with HPAP (1000 μM) and NADH (175 μM), □.