Table 1.

Steady-state kinetic parameters for the aldol condensation of erythrose and pyruvate and the aldol condensation of ManNAc and pyruvate for both wild-type and F190Dpc NAL

Enzyme	Substrate	kcatapp, min−1	Kmapp, mM	kcatapp/Kmapp, min−1⋅mM−1
F190Dpc	Erythrose	7.6 ± 0.56	4.4 ± 0.81	1.7
F190Dpc	ManNAc	0.22 ± 0.01	2.5 ± 0.43	0.09
Wild type	Erythrose	0.5 ± 0.05	3.0 ± 0.9	0.17
Wild type	ManNAc	0.8 ± 0.05	3.1 ± 0.7	0.26

Initial rates of enzyme reactions were measured in duplicate using the thiobarbituric acid assay at a fixed concentration of pyruvate of 80 mM while varying the concentration of aldehyde (0.8–15 mM). Data were fitted to the Michaelis–Menten equation to estimate the apparent kinetic parameters. Parameter values ± SE of the fit are shown.