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Determination of steady-state kinetic parameters. Double-reciprocal plot of initial velocity data for holoenzyme MtCS-FMNox in the presence of varying concentration of NADH (10, 25, 50, 75, 100, 200, 300 μM). Inset: Michaelis-Menten representation. The data were fitted to equation 1, yielding the following values: KNADH = 36 ± 4 μM, kcat = 8.3 (± 0.3) × 10-3 s-1 and kcat/KNADH = 231 M-1 s-1.
