. 2022 Nov 10;10(6):e03818-22. doi: 10.1128/spectrum.03818-22

TABLE 2.

Kinetic constants of glucose-6-phosphate dehydrogenases (ZwfA, ZwfB, and ZwfC) from Pseudomonas bharatica strain CSV86^T

Enzyme	G6P with fixed NADP⁺ conc.					G6P with fixed NAD⁺ conc.					NADP⁺ with fixed G6P conc.				NAD⁺ with fixed G6P conc.
Enzyme	K_m ^a	V_max	K_cat	k_cat/K_m	n	K_m	V_max	k_cat	k_cat/K_m	n	K_m	V_max	K_cat	k_cat/K_m	K_m	V_max	K_cat	k_cat/K_m
ZwfA^b	1827 ± 235	191 ± 12	177 ± 11	0.096 ± 0.016	1.84 ± 0.3	1697 ± 284	248 ± 42	230 ± 37	0.16 ± 0.04	2.1 ± 0.17	110.5 ± 20	201 ± 28	187 ± 26	1.7 ± 0.3	366 ± 70	329 ± 74	306 ± 69	0.86 ± 0.15
ZwfB^c	5827 ± 94	ND^d	ND	ND	NA^e	9968 ± 2716	ND	ND	ND	NA	67.5 ± 3	ND	ND	ND	577 ± 34	ND	ND	ND
ZwfC	1940 ± 172	11.4 ± 2.7	10.9 ± 2.6	0.0056 ± 0.0014	NA	364 ± 22	11.9 ± 1.6	11.4 ± 1.6	0.03 ± 0.0043	NA	18 ± 4.4	8.9 ± 1.6	8.5 ± 1.5	0.48 ± 0.05	3100 ± 285	12.4 ± 3.3	11.9 ± 3.2	0.0041 ± 0.0014

K_m, μM; V_max, μmol min⁻¹ mg⁻¹; k_cat, s⁻¹; k_cat/K_m, μM⁻¹ s⁻¹.

Enzyme displayed cooperativity for G6P binding (see Fig. 5B).

Kinetics were performed using a partially purified enzyme.

ND, not determined due to impure ZwfB preparations.

NA, not applicable because enzyme displayed a hyperbolic Michaelis-Menten saturation profile under these conditions.