. 2024 Jul 2;90(7):e01014-24. doi: 10.1128/aem.01014-24

TABLE 1.

Michaelis-Menten kinetic parameters for selected substrates

Enzyme	Substrate	K_M (mM)	k_cat (s⁻¹)	k_cat/K_M (M⁻¹ s⁻¹)	pH	Temperature (°C)	Reference
FgrGalOx	Galactose	82	503	6,370			(47)
FgrGalOx	Galactose	102	1,060	10,400			(48)
XpaGalOx	Galactose	10 ± 0.2	241 ± 2	24,100	6.5	25	This work
	Lactose	58.4 ± 0.4	190 ± 2	3,250 (1,500)^a
	Melibiose	19.7 ± 2.8 (23.9 ± 5.5)^b	206 ± 9 (234 ± 25)^b	10,460 (9,790)^b
	Raffinose	6.9 ± 0.3	189 ± 4	27,400
	Glycerol			(76)^a
	HMF			(330)^a
BspGalOx	Galactose	36.3 ± 1.4	52.1 ± 0.2	1,420	6.0	25	This work
	Lactose	186 ± 10	16.5 ± 0.6	89 (72)^a
	Melibiose	140 ± 7	13 ± 0.3	93 (54)^a
	Raffinose	156 ± 6	8.4 ± 0.2	54 (51)^a
	Glycerol			(3)^a
EfeGalOx	Galactose	8.2 ± 1.8 (8.1 ± 2.5)^b	0.7 ± 0.1 (0.7 ± 0.1)^b	85 (86)^b	8.5	50	This work
NexGalOx	Galactose	828 ± 78	7.5 ± 0.6	9 (7.2)^a	5.0	30	This work
NhaGalOx	Galactose	930 ± 98	4.3 ± 0.4	5 (4)^a	8.0	30	This work
AstAAO	Galactose	931 ± 138	13.8 ± 1.3	15 (14)^a	7.5	30	This work
	Lactose			(6)^a
	Melibiose	486 ± 68	2.1 ± 0.2	4 (3)^a
	Raffinose	75.3 ± 2.6	2.8 ± 0.1	37 (30)^a
	Glycerol	1,697 ± 163	30.6 ± 2.2	18 (18)^a
	Hexanol	2 ± 7.5	8.3 ± 0.7	130 (107)^a
	Benzyl alcohol			(230)^a
	HMF	2.0 ± 1.0 (9.4 ± 1.0)^b	24.9 ± 1.4 (42.7 ± 2.2)^b	12,400 (4,540)^b
	Cinnamyl alcohol	11.6 ± 1.0	43.8 ± 1.5	3,780 (4,800)^a
	Veratryl alcohol	1.8 ± 0.3 (6.4 ± 0.8)^b	16.5 ± 1.5 (38.3 ± 2.6)^b	9,160 (5,980)^b
	Furfuryl alcohol	24.0 ± 3.7	15.6 ± 1.7	650 (510)^a
	Methylglyoxal	45 ± 11	6.8 ± 1.2	150 (119)^a
	Glyoxal			(15)^a

^{^a}

Values in parentheses correspond to k_cat/K_M values determined from the slopes of linear fits to initial-rate kinetic data substrate concentrations well below saturation (see Fig. S6 to S9); individual K_M and k_cat values were not calculated.

^{^b}

Kinetic parameters were obtained by fitting a modified Michaelis-Menten equation including a term for substrate inhibition.