. 2021 Aug 17;12(4):e00329-21. doi: 10.1128/mBio.00329-21

TABLE 2.

Apparent steady state parameters of MaeA variants^a

Enzyme	Substrate	K_M (mM)	K_cat (s⁻¹)	K_cat/K_M (s⁻¹ mM⁻¹)	(k_cat/K_M)_NADP⁺/(k_cat/K_M)_NAD⁺
MaeA WT	L-malate	0.63 ± 0.04			0.0059
	NAD⁺	0.10 ± 0.02	188 ± 9	1843
	NADP⁺	3.6 ± 0.4	39 ± 2	11
MaeA D336N	L-malate	1.8 ± 0.2			17.6
	NAD⁺	1.5 ± 0.2	74 ± 3	49
	NADP⁺	0.091 ± 0.01	79 ± 2	868
MaeA D336N L176V	L-malate	1.4 ± 0.3			16.7
	NAD⁺	0.27 ± 0.03	105 ± 2	389
	NADP⁺	0.016 ± 0.001	102 ± 1	6497
MaeA D336A I283N	L-malate	0.48 ± 0.04			18.0
	NAD⁺	0.27 ± 0.03	130 ± 3	480
	NADP⁺	0.013 ± 0.00	112 ± 2	8615

Parameters are indicated as mean value ± standard error. The underlying Michaelis-Menten kinetics can be found in Fig. S2.