Table 3.

ligand	steady state parametersa			equilibrium bindingb
	Km app (μM)	Hill coefficient	kcat (s−1)	Ki app (μM)	Hill coefficient	Kd (μM)
NADPH	3.5 ± 0.2	2.5 ± 0.5	0.082 ± 0.002c	–	1.0d	2.7 ± 0.2d
NADPH	3.7 ± 0.2	2.6 ± 0.3	0.082 ± 0.002c	–
DAB	1.6 ± 0.3e	1.0e	0.0127 ± 0.009e	14 ± 2e
DAB	1.2 ± 0.2f	1.0f	0.014 ± 0.01f	108 ± 67f

^aFit to eq 1 or 2 in Experimental Procedures.

^bNADPH binding fit to eq 4 in Experimental Procedures.

^cBased on a NADPH saturation curve with DAB not fully saturated.

^dBased on intrinsic tryptophan fluorescence quenching and fit to equation 6 (see Figure 3C).

^eBased on DAB saturation kinetics with 10K_d of NADPH.

^fBased on DAB saturation kinetics with 200K_d of NADPH.