. 2024 Jun 27;300(8):107501. doi: 10.1016/j.jbc.2024.107501

Table 3.

Kinetic properties of rbHSD17B14, hHSD17B14, and rHSD17B14 proteins

Substrate	rbHSD17B14			hHSD17B14			rHSD17B14
Substrate	V_max	K_M	k_cat^a	V_max	K_M	k_cat^a	V_max	K_M	k_cat^a
	μmol min⁻¹mg⁻¹	μM	s⁻¹	μmol min⁻¹mg⁻¹	μM	s⁻¹	μmol min^-1mg⁻¹	μM	s⁻¹
L-fucose	13.15 ± 0.22	136.36 ± 9.10	7.00 ± 0.12	27.20 ± 0.48	172.20 ± 11.40	14.00 ± 0.25	0.26 ± 0.01	21.45 ± 4.09	0.13 ± 0.01
NAD⁺	15.88 ± 0.19	45.69 ± 1.89	8.46 ± 0.10	32.82 ± 0.59	149.02 ± 8.13	16.89 ± 0.30	0.30 ± 0.01	47.06 ± 7.56	0.15 ± 0.01

Kinetic properties were determined with the use of purified recombinant N-terminal His₆-tagged HSD17B14 proteins. Determinations for L-fucose were performed with 1.05 to 2.2 μg of the enzyme preparations in the presence of 1.5 mM NAD⁺ and variable concentrations of L-fucose, whereas the measurements for NAD⁺ were done in the presence of 2 mM L-fucose and variable concentrations of NAD⁺. Values are the means ± SD (error bars) of three independent experiments.

Calculated for the His₆-tagged recombinant enzymes with molecular weight =31,948 Da, 30,874 Da, and 30,314 Da for the rabbit, human, and rat enzyme, respectively.